ID   CRU4_ARATH              Reviewed;         472 AA.
AC   P15455; Q3E711; Q56Z11; Q9FFH7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   16-MAY-2012, entry version 95.
DE   RecName: Full=12S seed storage protein CRU4;
DE   AltName: Full=Cruciferin 4;
DE            Short=AtCRU4;
DE   AltName: Full=Cruciferin A1;
DE   AltName: Full=Legumin-type globulin storage protein CRU4;
DE   Contains:
DE     RecName: Full=12S seed storage protein CRU4 alpha chain;
DE     AltName: Full=12S seed storage protein CRU4 acidic chain;
DE   Contains:
DE     RecName: Full=12S seed storage protein CRU4 beta chain;
DE     AltName: Full=12S seed storage protein CRU4 basic chain;
DE   Flags: Precursor;
GN   Name=CRU4; Synonyms=CRA1; OrderedLocusNames=At5g44120;
GN   ORFNames=MLN1.4;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   AGRICOLA=IND91035197; DOI=10.1007/BF00019521;
RA   Pang P.P., Pruitt R.E., Meyerowitz E.M.;
RT   "Molecular cloning, genome organization, expression and evolution of
RT   12S seed storage protein genes of Arabidopsis thaliana.";
RL   Plant Mol. Biol. 11:805-820(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=97471969; PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned
RT   P1 clones.";
RL   DNA Res. 4:215-230(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 126-134, AND PROTEOLYSIS.
RX   PubMed=14688293; DOI=10.1105/tpc.016378;
RA   Gruis D., Schulze J., Jung R.;
RT   "Storage protein accumulation in the absence of the vacuolar
RT   processing enzyme family of cysteine proteases.";
RL   Plant Cell 16:270-290(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-472 (ISOFORM 1/2).
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 420-472 (ISOFORM 1/2).
RC   STRAIN=cv. Columbia; TISSUE=Green siliques;
RX   MEDLINE=94108489; PubMed=8281187;
RX   DOI=10.1046/j.1365-313X.1993.04061051.x;
RA   Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA   Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P.,
RA   Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R.,
RA   Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y.,
RA   de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M.,
RA   Bardet C., Tremousaygue D., Lescure B.;
RT   "An inventory of 1152 expressed sequence tags obtained by partial
RT   sequencing of cDNAs from Arabidopsis thaliana.";
RL   Plant J. 4:1051-1061(1993).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=12417707; DOI=10.1105/tpc.005009;
RA   Gruis D.F., Selinger D.A., Curran J.M., Jung R.;
RT   "Redundant proteolytic mechanisms process seed storage proteins in the
RT   absence of seed-type members of the vacuolar processing enzyme family
RT   of cysteine proteases.";
RL   Plant Cell 14:2863-2882(2002).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT THR-115;
RP   TYR-312 AND SER-314.
RX   PubMed=17313365; DOI=10.1042/BJ20061569;
RA   Wan L., Ross A.R., Yang J., Hegedus D.D., Kermode A.R.;
RT   "Phosphorylation of the 12 S globulin cruciferin in wild-type and
RT   abi1-1 mutant Arabidopsis thaliana (thale cress) seeds.";
RL   Biochem. J. 404:247-256(2007).
RN   [11]
RP   PROTEOLYSIS, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=17562289;
RA   Li Q., Wang B.-C., Xu Y., Zhu Y.-X.;
RT   "Systematic studies of 12S seed storage protein accumulation and
RT   degradation patterns during Arabidopsis seed maturation and early
RT   seedling germination stages.";
RL   J. Biochem. Mol. Biol. 40:373-381(2007).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION.
RX   PubMed=18768909; DOI=10.1104/pp.108.124594;
RA   Ghelis T., Bolbach G., Clodic G., Habricot Y., Miginiac E., Sotta B.,
RA   Jeannette E.;
RT   "Protein tyrosine kinases and protein tyrosine phosphatases are
RT   involved in abscisic acid-dependent processes in Arabidopsis seeds and
RT   suspension cells.";
RL   Plant Physiol. 148:1668-1680(2008).
RN   [13]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19292762; DOI=10.1111/j.1365-313X.2009.03862.x;
RA   Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M.,
RA   Vierstra R.D.;
RT   "Tandem affinity purification and mass spectrometric analysis of
RT   ubiquitylated proteins in Arabidopsis.";
RL   Plant J. 59:344-358(2009).
CC   -!- FUNCTION: Seed storage protein.
CC   -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a
CC       basic chain derived from a single precursor and linked by a
CC       disulfide bond.
CC   -!- SUBCELLULAR LOCATION: Protein storage vacuole (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P15455-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15455-2; Sequence=VSP_026066;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Accumulates in seeds 8 days after anthesis.
CC   -!- DEVELOPMENTAL STAGE: Detected in siliques at nucleotide level from
CC       6 days post anthesis (dpa) to 17 dpa. First observed in siliques
CC       at protein level 15 dpa and accumulates progressively as native
CC       isoforms or proteolytic fragments during the last week of seed
CC       maturation/desiccation. Present in dry seeds, essentially in
CC       cotyledons and hypocotyls, but disappears during their germination
CC       (at protein level).
CC   -!- PTM: Ubiquitinated.
CC   -!- PTM: Phosphorylated in seeds on some Tyr residues in response to
CC       abscisic acid (ABA).
CC   -!- PTM: Proteolytically processed during seed maturation at a
CC       conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to
CC       produce two mature polypeptides referred to as alpha and beta
CC       subunits that are joined together by a disulfide bond.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins)
CC       family.
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DR   EMBL; M37247; AAA32777.1; -; Genomic_DNA.
DR   EMBL; X14312; CAA32493.1; -; Genomic_DNA.
DR   EMBL; AB005239; BAB10979.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95062.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95064.1; -; Genomic_DNA.
DR   EMBL; AY070730; AAL50071.1; -; mRNA.
DR   EMBL; BT029491; ABL66748.1; -; mRNA.
DR   EMBL; AK221158; BAD95189.1; -; mRNA.
DR   EMBL; Z17590; CAA79005.1; -; mRNA.
DR   IPI; IPI00533916; -.
DR   IPI; IPI00542873; -.
DR   PIR; S08509; S08509.
DR   RefSeq; NP_199225.1; NM_123779.4.
DR   RefSeq; NP_851128.1; NM_180797.1.
DR   UniGene; At.20540; -.
DR   UniGene; At.74770; -.
DR   ProteinModelPortal; P15455; -.
DR   SMR; P15455; 30-459.
DR   STRING; P15455; -.
DR   PRIDE; P15455; -.
DR   EnsemblPlants; AT5G44120; AT5G44120; AT5G44120.
DR   GeneID; 834435; -.
DR   GenomeReviews; BA000015_GR; AT5G44120.
DR   KEGG; ath:AT5G44120; -.
DR   TAIR; At5g44120; -.
DR   eggNOG; NOG261521; -.
DR   HOGENOM; HOG000217279; -.
DR   InParanoid; P15455; -.
DR   OMA; ANAQINT; -.
DR   PhylomeDB; P15455; -.
DR   ProtClustDB; CLSN2679899; -.
DR   ArrayExpress; P15455; -.
DR   Genevestigator; P15455; -.
DR   GO; GO:0000326; C:protein storage vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0045735; F:nutrient reservoir activity; IDA:UniProtKB.
DR   GO; GO:0071215; P:cellular response to abscisic acid stimulus; IDA:UniProtKB.
DR   GO; GO:0010431; P:seed maturation; IDA:UniProtKB.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   InterPro; IPR022379; 11S_seedstore_CS.
DR   InterPro; IPR006044; 11S_seedstore_pln.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR011051; Cupin_RmlC_type.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00190; Cupin_1; 2.
DR   PRINTS; PR00439; 11SGLOBULIN.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; RmlC_like_cupin; 1.
DR   PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Phosphoprotein; Reference proteome;
KW   Seed storage protein; Signal; Storage protein; Ubl conjugation;
KW   Vacuole.
FT   SIGNAL        1     24       By similarity.
FT   CHAIN        25    282       12S seed storage protein CRU4 alpha chain
FT                                (By similarity).
FT                                /FTId=PRO_0000031999.
FT   CHAIN       283    472       12S seed storage protein CRU4 beta chain
FT                                (By similarity).
FT                                /FTId=PRO_0000032000.
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   MOD_RES      77     77       Phosphotyrosine (By similarity).
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     115    115       Phosphothreonine.
FT   MOD_RES     312    312       Phosphotyrosine.
FT   MOD_RES     314    314       Phosphoserine.
FT   MOD_RES     408    408       Phosphothreonine (By similarity).
FT   MOD_RES     433    433       Phosphothreonine (By similarity).
FT   MOD_RES     450    450       Phosphothreonine (By similarity).
FT   DISULFID     36     69       By similarity.
FT   DISULFID    112    289       Interchain (between alpha and beta
FT                                chains) (Potential).
FT   VAR_SEQ       1    104       Missing (in isoform 2).
FT                                /FTId=VSP_026066.
FT   CONFLICT    167    167       E -> Q (in Ref. 1; AAA32777/CAA32493).
FT   CONFLICT    356    356       V -> E (in Ref. 1; AAA32777/CAA32493).
SQ   SEQUENCE   472 AA;  52595 MW;  700B468E4D251994 CRC64;
     MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW
     DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS
     EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQEPLV IVSVFDLASH
     QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN
     QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP
     SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYVTDGE
     AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR
     TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA
//
ID   5HT1D_TAKRU             Reviewed;         379 AA.
AC   P79748;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   16-MAY-2012, entry version 78.
DE   RecName: Full=5-hydroxytryptamine receptor 1D;
DE            Short=5-HT-1D;
DE            Short=5-HT1D;
DE            Short=5HT1D;
DE   AltName: Full=F1D;
DE   AltName: Full=Serotonin receptor 1D;
GN   Name=htr1d;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4;
RA   Yamaguchi F., Brenner S.;
RT   "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes
RT   from the Japanese puffer fish, Fugu rubripes.";
RL   Gene 191:219-223(1997).
CC   -!- FUNCTION: This is one of the several different receptors for 5-
CC       hydroxytryptamine (serotonin), a biogenic hormone that functions
CC       as a neurotransmitter, a hormone, and a mitogen. The activity of
CC       this receptor is mediated by G proteins that inhibit adenylate
CC       cyclase activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; X83865; CAA58745.1; -; Genomic_DNA.
DR   ProteinModelPortal; P79748; -.
DR   SMR; P79748; 121-152.
DR   eggNOG; NOG249628; -.
DR   InParanoid; P79748; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000505; 5HT1D_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00514; 5HT1DRECEPTR.
DR   PRINTS; PR01101; 5HTRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    379       5-hydroxytryptamine receptor 1D.
FT                                /FTId=PRO_0000068932.
FT   TOPO_DOM      1     36       Extracellular (By similarity).
FT   TRANSMEM     37     60       Helical; Name=1; (By similarity).
FT   TOPO_DOM     61     73       Cytoplasmic (By similarity).
FT   TRANSMEM     74     96       Helical; Name=2; (By similarity).
FT   TOPO_DOM     97    106       Extracellular (By similarity).
FT   TRANSMEM    107    132       Helical; Name=3; (By similarity).
FT   TOPO_DOM    133    152       Cytoplasmic (By similarity).
FT   TRANSMEM    153    174       Helical; Name=4; (By similarity).
FT   TOPO_DOM    175    192       Extracellular (By similarity).
FT   TRANSMEM    193    216       Helical; Name=5; (By similarity).
FT   TOPO_DOM    217    307       Cytoplasmic (By similarity).
FT   TRANSMEM    308    331       Helical; Name=6; (By similarity).
FT   TOPO_DOM    332    339       Extracellular (By similarity).
FT   TRANSMEM    340    364       Helical; Name=7; (By similarity).
FT   TOPO_DOM    365    379       Cytoplasmic (By similarity).
FT   CARBOHYD      5      5       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     14     14       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     21     21       N-linked (GlcNAc...) (Potential).
FT   DISULFID    109    186       By similarity.
SQ   SEQUENCE   379 AA;  42302 MW;  99B6E2C0379EBC78 CRC64;
     MELDNNSLDY FSSNFTDIPS NTTVAHWTEA TLLGLQISVS VVLAIVTLAT MLSNAFVIAT
     IFLTRKLHTP ANFLIGSLAV TDMLVSILVM PISIVYTVSK TWSLGQIVCD IWLSSDITFC
     TASILHLCVI ALDRYWAITD ALEYSKRRTM RRAAVMVAVV WVISISISMP PLFWRQAKAH
     EELKECMVNT DQISYTLYST FGAFYVPTVL LIILYGRIYV AARSRIFKTP SYSGKRFTTA
     QLIQTSAGSS LCSLNSASNQ EAHLHSGAGG EGGGSPLFVN SVKVKLADNV LERKRLCAAR
     ERKATKTLGI ILGAFIICWL PFFVVTLVWA ICKECSFDPL LFDVFTWLGY LNSLINPVIY
     TVFNDEFKQA FQKLIKFRR
//
ID   ACH2_DROME              Reviewed;         576 AA.
AC   P17644; Q0KI18; Q9VC73;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   18-APR-2012, entry version 123.
DE   RecName: Full=Acetylcholine receptor subunit alpha-like 2;
DE   Flags: Precursor;
GN   Name=nAcRalpha-96Ab; Synonyms=Acr96Ab, AcrE, sad; ORFNames=CG6844;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Head;
RX   MEDLINE=90353591; PubMed=2117557; DOI=10.1016/0014-5793(90)81170-S;
RA   Jonas P., Baumann A., Merz B., Gundelfinger E.D.;
RT   "Structure and developmental expression of the D alpha 2 gene encoding
RT   a novel nicotinic acetylcholine receptor protein of Drosophila
RT   melanogaster.";
RL   FEBS Lett. 269:264-268(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90360975; PubMed=1697262;
RA   Sawruk E., Schloss P., Betz H., Schmitt B.;
RT   "Heterogeneity of Drosophila nicotinic acetylcholine receptors: SAD, a
RT   novel developmentally regulated alpha-subunit.";
RL   EMBO J. 9:2671-2677(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Head;
RX   MEDLINE=90301489; PubMed=2114015; DOI=10.1093/nar/18.12.3640;
RA   Baumann A., Jonas P., Gundelfinger E.D.;
RT   "Sequence of D alpha 2, a novel alpha-like subunit of Drosophila
RT   nicotinic acetylcholine receptors.";
RL   Nucleic Acids Res. 18:3640-3640(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Head;
RX   MEDLINE=22426066; PubMed=12537569;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
RA   George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
RA   Rubin G.M., Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and
CC       leads to opening of an ion-conducting channel across the plasma
CC       membrane.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: CNS in embryos.
CC   -!- DEVELOPMENTAL STAGE: Late embryonic and late pupal stages.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Acetylcholine receptor (TC 1.A.9.1) subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X52274; CAA36517.1; -; mRNA.
DR   EMBL; X53583; CAA37652.1; -; mRNA.
DR   EMBL; AE014297; AAF56302.2; -; Genomic_DNA.
DR   EMBL; AY058446; AAL13675.1; -; mRNA.
DR   PIR; S11679; ACFFA2.
DR   RefSeq; NP_524482.1; NM_079758.2.
DR   RefSeq; NP_733001.1; NM_170146.1.
DR   UniGene; Dm.2363; -.
DR   ProteinModelPortal; P17644; -.
DR   SMR; P17644; 42-547.
DR   DIP; DIP-22674N; -.
DR   IntAct; P17644; 1.
DR   MINT; MINT-888559; -.
DR   STRING; P17644; -.
DR   PRIDE; P17644; -.
DR   EnsemblMetazoa; FBtr0084639; FBpp0084023; FBgn0000039.
DR   EnsemblMetazoa; FBtr0084640; FBpp0084024; FBgn0000039.
DR   GeneID; 42919; -.
DR   KEGG; dme:Dmel_CG6844; -.
DR   CTD; 42919; -.
DR   FlyBase; FBgn0000039; nAcRalpha-96Ab.
DR   eggNOG; NOG290206; -.
DR   GeneTree; ENSGT00630000089708; -.
DR   InParanoid; P17644; -.
DR   KO; K05312; -.
DR   OMA; LELCHPP; -.
DR   OrthoDB; EOG4W6MB5; -.
DR   PhylomeDB; P17644; -.
DR   NextBio; 831266; -.
DR   ArrayExpress; P17644; -.
DR   Bgee; P17644; -.
DR   GermOnline; CG6844; Drosophila melanogaster.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004889; F:acetylcholine-activated cation-selective channel activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Complete proteome; Disulfide bond;
KW   Glycoprotein; Ion transport; Ionic channel; Ligand-gated ion channel;
KW   Membrane; Postsynaptic cell membrane; Receptor; Reference proteome;
KW   Signal; Synapse; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     21       Probable.
FT   CHAIN        22    576       Acetylcholine receptor subunit alpha-like
FT                                2.
FT                                /FTId=PRO_0000000300.
FT   TOPO_DOM     22    261       Extracellular (Potential).
FT   TRANSMEM    262    285       Helical; (Potential).
FT   TRANSMEM    293    311       Helical; (Potential).
FT   TRANSMEM    327    346       Helical; (Potential).
FT   TOPO_DOM    347    526       Cytoplasmic (Potential).
FT   TRANSMEM    527    545       Helical; (Potential).
FT   CARBOHYD     65     65       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    570    570       N-linked (GlcNAc...) (Potential).
FT   DISULFID    169    183       By similarity.
FT   DISULFID    243    244       Associated with receptor activation (By
FT                                similarity).
SQ   SEQUENCE   576 AA;  65506 MW;  97D6A46CADC3F42F CRC64;
     MAPGCCTTRP RPIALLAHIW RHCKPLCLLL VLLLLCETVQ ANPDAKRLYD DLLSNYNRLI
     RPVSNNTDTV LVKLGLRLSQ LIDLNLKDQI LTTNVWLEHE WQDHKFKWDP SEYGGVTELY
     VPSEHIWLPD IVLYNNADGE YVVTTMTKAI LHYTGKVVWT PPAIFKSSCE IDVRYFPFDQ
     QTCFMKFGSW TYDGDQIDLK HISQKNDKDN KVEIGIDLRE YYPSVEWDIL GVPAERHEKY
     YPCCAEPYPD IFFNITLRRK TLFYTVNLII PCVGISYLSV LVFYLPADSG EKIALCISIL
     LSQTMFFLLI SEIIPSTSLA LPLLGKYLLF TMLLVGLSVV ITIIILNIHY RKPSTHKMRP
     WIRSFFIKRL PKLLLMRVPK DLLRDLAANK INYGLKFSKT KFGQALMDEM QMNSGGSSPD
     SLRRMQGRVG AGGCNGMHVT TATNRFSGLV GALGGGLSTL SGYNGLPSVL SGLDDSLSDV
     AARKKYPFEL EKAIHNVMFI QHHMQRQDEF NAEDQDWGFV AMVMDRLFLW LFMIASLVGT
     FVILGEAPSL YDDTKAIDVQ LSDVAKQIYN LTEKKN
//
ID   ACTB1_TAKRU             Reviewed;         375 AA.
AC   P68142; P53484;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-MAY-2012, entry version 49.
DE   RecName: Full=Actin, cytoplasmic 1;
DE   AltName: Full=Beta-actin A;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
GN   Name=actba;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Widely distributed. Not expressed in skeletal
CC       muscle.
CC   -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins
CC       in Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U37499; AAC59889.1; -; Genomic_DNA.
DR   PIR; S71124; S71124.
DR   ProteinModelPortal; P68142; -.
DR   SMR; P68142; 2-375.
DR   Ensembl; ENSTRUT00000013141; ENSTRUP00000013080; ENSTRUG00000005447.
DR   eggNOG; COG5277; -.
DR   GeneTree; ENSGT00630000089629; -.
DR   InParanoid; P68142; -.
DR   OMA; IKNLMER; -.
DR   OrthoDB; EOG41JZC9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Methylation; Nucleotide-binding; Oxidation; Reference proteome.
FT   CHAIN         1    375       Actin, cytoplasmic 1.
FT                                /FTId=PRO_0000367094.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    375       Actin, cytoplasmic 1, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000000809.
FT   MOD_RES       1      1       N-acetylmethionine; in Actin, cytoplasmic
FT                                1; alternate (By similarity).
FT   MOD_RES       2      2       N-acetylglutamate; in Actin, cytoplasmic
FT                                1, N-terminally processed (By
FT                                similarity).
FT   MOD_RES      44     44       Methionine sulfoxide (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   375 AA;  41767 MW;  9C505616D33E9495 CRC64;
     MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTB2_TAKRU             Reviewed;         375 AA.
AC   P53485;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 69.
DE   RecName: Full=Actin, cytoplasmic 2;
DE   AltName: Full=Beta-actin B;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
GN   Name=actbb;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins
CC       in Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U38848; AAC59890.1; -; Genomic_DNA.
DR   PIR; S71125; S71125.
DR   ProteinModelPortal; P53485; -.
DR   SMR; P53485; 2-375.
DR   eggNOG; COG5277; -.
DR   InParanoid; P53485; -.
DR   OrthoDB; EOG41JZC9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Methylation; Nucleotide-binding; Oxidation; Reference proteome.
FT   CHAIN         1    375       Actin, cytoplasmic 2.
FT                                /FTId=PRO_0000367095.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    375       Actin, cytoplasmic 2, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000000811.
FT   MOD_RES       1      1       N-acetylmethionine; in Actin, cytoplasmic
FT                                2; alternate (By similarity).
FT   MOD_RES       2      2       N-acetylaspartate; in Actin, cytoplasmic
FT                                2, N-terminally processed (By
FT                                similarity).
FT   MOD_RES      44     44       Methionine sulfoxide (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   375 AA;  41767 MW;  1AE990BC0AED0D1C CRC64;
     MDDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITSL APTTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTB3_TAKRU             Reviewed;         375 AA.
AC   P53486;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 71.
DE   RecName: Full=Actin, cytoplasmic 3;
DE   AltName: Full=Beta-actin C;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 3, N-terminally processed;
GN   Name=actbc;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in gills, kidney and
CC       skin.
CC   -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins
CC       in Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U38849; AAC59891.1; -; Genomic_DNA.
DR   PIR; S71126; S71126.
DR   ProteinModelPortal; P53486; -.
DR   SMR; P53486; 2-375.
DR   STRING; P53486; -.
DR   PRIDE; P53486; -.
DR   eggNOG; COG5277; -.
DR   InParanoid; P53486; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Methylation; Nucleotide-binding; Oxidation; Reference proteome.
FT   CHAIN         1    375       Actin, cytoplasmic 3.
FT                                /FTId=PRO_0000367096.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    375       Actin, cytoplasmic 3, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000000841.
FT   MOD_RES       1      1       N-acetylmethionine; in Actin, cytoplasmic
FT                                3; alternate (By similarity).
FT   MOD_RES       2      2       N-acetylglutamate; in Actin, cytoplasmic
FT                                3, N-terminally processed (By
FT                                similarity).
FT   MOD_RES      44     44       Methionine sulfoxide (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   375 AA;  41783 MW;  8B451E0DB3399C0B CRC64;
     MEDEVASLVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA SSSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SSGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTB_OREMO              Reviewed;         375 AA.
AC   P68143; P53484;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   18-APR-2012, entry version 37.
DE   RecName: Full=Actin, cytoplasmic 1;
DE   AltName: Full=Beta-actin;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
GN   Name=actb;
OS   Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei;
OC   Cichlidae; African cichlids; Pseudocrenilabrinae; Tilapiini;
OC   Oreochromis.
OX   NCBI_TaxID=8127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gill;
RA   Takeuchi K.;
RT   "Cloning of Tilapia actin cDNAs.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- PTM: Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB037865; BAA90688.1; -; mRNA.
DR   ProteinModelPortal; P68143; -.
DR   SMR; P68143; 2-375.
DR   HOVERGEN; HBG003771; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW   Nucleotide-binding; Oxidation.
FT   CHAIN         1    375       Actin, cytoplasmic 1.
FT                                /FTId=PRO_0000367091.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    375       Actin, cytoplasmic 1, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000000803.
FT   MOD_RES       1      1       N-acetylmethionine; in Actin, cytoplasmic
FT                                1; alternate (By similarity).
FT   MOD_RES       2      2       N-acetylglutamate; in Actin, cytoplasmic
FT                                1, N-terminally processed (By
FT                                similarity).
FT   MOD_RES      44     44       Methionine sulfoxide (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   375 AA;  41767 MW;  9C505616D33E9495 CRC64;
     MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTC_TAKRU              Reviewed;         377 AA.
AC   P53480;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 76.
DE   RecName: Full=Actin, alpha cardiac;
DE   Flags: Precursor;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in heart. Lower levels
CC       in skeletal muscle and skin.
CC   -!- PTM: Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are three genes coding for cardiac actin in
CC       Fugu.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U38959; AAC59894.1; -; Genomic_DNA.
DR   EMBL; U38960; AAC59895.1; -; Genomic_DNA.
DR   EMBL; U38961; AAC59896.1; -; Genomic_DNA.
DR   PIR; S71120; S71120.
DR   ProteinModelPortal; P53480; -.
DR   Ensembl; ENSTRUT00000011488; ENSTRUP00000011428; ENSTRUG00000004787.
DR   Ensembl; ENSTRUT00000036073; ENSTRUP00000035943; ENSTRUG00000014049.
DR   Ensembl; ENSTRUT00000046301; ENSTRUP00000046146; ENSTRUG00000018009.
DR   GeneTree; ENSGT00390000011529; -.
DR   GeneTree; ENSGT00630000089596; -.
DR   InParanoid; P53480; -.
DR   OMA; IXMESAG; -.
DR   OrthoDB; EOG4W9J40; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Methylation; Muscle protein; Nucleotide-binding; Oxidation;
KW   Reference proteome.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000826.
FT   CHAIN         3    377       Actin, alpha cardiac.
FT                                /FTId=PRO_0000000827.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      46     46       Methionine sulfoxide (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  41975 MW;  0499A43921D9BBCF CRC64;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTSA_TAKRU             Reviewed;         377 AA.
AC   P68140; P53481;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-MAY-2012, entry version 48.
DE   RecName: Full=Actin, alpha skeletal muscle A;
DE   AltName: Full=Alpha-actin-1 A;
DE   Flags: Precursor;
GN   Name=acta1a;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle.
CC       Lower levels in heart.
CC   -!- PTM: Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are two different alpha-skeletal actins in
CC       Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U38850; AAC59892.1; -; Genomic_DNA.
DR   PIR; S71118; S71118.
DR   ProteinModelPortal; P68140; -.
DR   SMR; P68140; 6-377.
DR   Ensembl; ENSTRUT00000019970; ENSTRUP00000019889; ENSTRUG00000007989.
DR   eggNOG; COG5277; -.
DR   GeneTree; ENSGT00630000089596; -.
DR   InParanoid; P68140; -.
DR   OMA; MIGMENP; -.
DR   OrthoDB; EOG4W9J40; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Methylation; Muscle protein; Nucleotide-binding; Oxidation;
KW   Reference proteome.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000862.
FT   CHAIN         3    377       Actin, alpha skeletal muscle A.
FT                                /FTId=PRO_0000000863.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      46     46       Methionine sulfoxide (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  41945 MW;  1C7185C0F7C19A26 CRC64;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTSB_TAKRU             Reviewed;         377 AA.
AC   P53482;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 69.
DE   RecName: Full=Actin, alpha skeletal muscle B;
DE   AltName: Full=Alpha-actin-1 B;
DE   Flags: Precursor;
GN   Name=acta1b;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle.
CC       Lower levels in heart, gills and skin.
CC   -!- PTM: Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- MISCELLANEOUS: There are two different alpha-skeletal actins in
CC       Fugu rubripes.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U38958; AAC59893.1; -; Genomic_DNA.
DR   PIR; S71119; S71119.
DR   ProteinModelPortal; P53482; -.
DR   SMR; P53482; 6-377.
DR   InParanoid; P53482; -.
DR   OrthoDB; EOG4W9J40; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Methylation; Muscle protein; Nucleotide-binding; Oxidation;
KW   Reference proteome.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000864.
FT   CHAIN         3    377       Actin, alpha skeletal muscle B.
FT                                /FTId=PRO_0000000865.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      46     46       Methionine sulfoxide (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  41977 MW;  A0973DD7B23B0C82 CRC64;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMG TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTS_OREMO              Reviewed;         377 AA.
AC   P68264; P53481;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   18-APR-2012, entry version 36.
DE   RecName: Full=Actin, alpha skeletal muscle;
DE   AltName: Full=Alpha-actin-1;
DE   Flags: Precursor;
GN   Name=acta1;
OS   Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei;
OC   Cichlidae; African cichlids; Pseudocrenilabrinae; Tilapiini;
OC   Oreochromis.
OX   NCBI_TaxID=8127;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Takeuchi K.;
RT   "Cloning of Tilapia actin cDNAs.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- PTM: Oxidation of Met-46 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB037866; BAA90689.1; -; mRNA.
DR   ProteinModelPortal; P68264; -.
DR   SMR; P68264; 6-377.
DR   HOVERGEN; HBG003771; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW   Muscle protein; Nucleotide-binding; Oxidation.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000866.
FT   CHAIN         3    377       Actin, alpha skeletal muscle.
FT                                /FTId=PRO_0000000867.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      46     46       Methionine sulfoxide (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  41945 MW;  1C7185C0F7C19A26 CRC64;
     MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTX_TAKRU              Reviewed;         376 AA.
AC   P53483;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 65.
DE   RecName: Full=Actin, alpha anomalous;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347;
RA   Venkatesh B., Tay B.H., Elgar G., Brenner S.;
RT   "Isolation, characterization and evolution of nine pufferfish (Fugu
RT   rubripes) actin genes.";
RL   J. Mol. Biol. 259:655-665(1996).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in testis.
CC   -!- PTM: Oxidation of Met-45 by MICALs (MICAL1, MICAL2 or MICAL3) to
CC       form methionine sulfoxide promotes actin filament
CC       depolymerization. Methionine sulfoxide is produced
CC       stereospecifically, but it is not known whether the (S)-S-oxide or
CC       the (R)-S-oxide is produced (By similarity).
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U38962; AAC59897.1; -; Genomic_DNA.
DR   PIR; S71123; S71123.
DR   ProteinModelPortal; P53483; -.
DR   SMR; P53483; 7-365.
DR   Ensembl; ENSTRUT00000013262; ENSTRUP00000013201; ENSTRUG00000005494.
DR   eggNOG; COG5277; -.
DR   GeneTree; ENSGT00630000089629; -.
DR   InParanoid; P53483; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Nucleotide-binding; Oxidation; Reference proteome.
FT   CHAIN         1    376       Actin, alpha anomalous.
FT                                /FTId=PRO_0000089056.
FT   MOD_RES      45     45       Methionine sulfoxide (By similarity).
SQ   SEQUENCE   376 AA;  41979 MW;  DB037F47BA1371D8 CRC64;
     MSDYDETALV CDNGSGLVKA GFAGDDTPRA VFHAIVGRPR HQDDMDDMGK KGYYVGDEAQ
     SKRDILSLKH PIERGIITNW DDMEKIWHHT FYNELCVAPE EHPTLLTEAP LNPKANREKM
     TQIMLETFNM PAMYVSIQAV LSLYASGRTT GIVLDSGEGV THAVPIAEGY ALPPAIMRLN
     LAGRDLTDYL MKILNERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKR
     YELPDGQVIT IGNERFCCPE TLFQPSFMGM ESAGIHEITH SSIMKCDIEI RKDLYANNVL
     TGGATLFPGI ADRMQKEITA LAPSTMKIQI IAPPERKYSV WIGGSILASL STFQQMWISK
     QEYEEIGPSI IHCKCF
//
ID   AMIC_PSEAE              Reviewed;         385 AA.
AC   P27017;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   16-MAY-2012, entry version 83.
DE   RecName: Full=Aliphatic amidase expression-regulating protein;
GN   Name=amiC; OrderedLocusNames=PA3364;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG
OS   12228).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19.
RC   STRAIN=PAC;
RX   MEDLINE=91317707; PubMed=1907262;
RA   Wilson S.A., Drew R.E.;
RT   "Cloning and DNA sequence of amiC, a new gene regulating expression of
RT   the Pseudomonas aeruginosa aliphatic amidase, and purification of the
RT   amiC product.";
RL   J. Bacteriol. 173:4914-4921(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   CRYSTALLIZATION.
RX   MEDLINE=92106343; PubMed=1762155; DOI=10.1016/0022-2836(91)90579-U;
RA   Wilson S.A., Chayen N.E., Hemmings A.M., Drew R.E., Pearl L.H.;
RT   "Crystallization of and preliminary X-ray data for the negative
RT   regulator (AmiC) of the amidase operon of Pseudomonas aeruginosa.";
RL   J. Mol. Biol. 222:869-871(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 27-28.
RX   MEDLINE=95112789; PubMed=7813419;
RA   Pearl L.H., O'Hara B.P., Drew R.E., Wilson S.A.;
RT   "Crystal structure of AmiC: the controller of transcription
RT   antitermination in the amidase operon of Pseudomonas aeruginosa.";
RL   EMBO J. 13:5810-5817(1994).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIR.
RC   STRAIN=PAC1;
RX   MEDLINE=99437995; PubMed=10508151; DOI=10.1093/emboj/18.19.5175;
RA   O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E.,
RA   Pearl L.H.;
RT   "Crystal structure and induction mechanism of AmiC-AmiR: a ligand-
RT   regulated transcription antitermination complex.";
RL   EMBO J. 18:5175-5186(1999).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RC   STRAIN=PAC1;
RX   MEDLINE=20175740; PubMed=10708652; DOI=10.1093/protein/13.2.129;
RA   O'Hara B.P., Wilson S.A., Lee A.W., Roe S.M., Siligardi G., Drew R.E.,
RA   Pearl L.H.;
RT   "Structural adaptation to selective pressure for altered ligand
RT   specificity in the Pseudomonas aeruginosa amide receptor, AmiC.";
RL   Protein Eng. 13:129-132(2000).
CC   -!- FUNCTION: Negatively regulates the expression of the aliphatic
CC       amidase operon. AmiC functions by inhibiting the action of AmiR at
CC       the protein level. It exhibits protein kinase activity.
CC   -!- SUBUNIT: Homodimer. Forms a complex with AmiR.
CC   -!- DOMAIN: Consists of two beta-alpha-beta domains with a central
CC       cleft in which the amide binds.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; X13776; CAA32024.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06752.1; -; Genomic_DNA.
DR   PIR; A40359; A40359.
DR   PIR; C83226; C83226.
DR   RefSeq; NP_252054.1; NC_002516.2.
DR   PDB; 1PEA; X-ray; 2.10 A; A=1-385.
DR   PDB; 1QNL; X-ray; 2.70 A; A=1-385.
DR   PDB; 1QO0; X-ray; 2.25 A; A/B=1-385.
DR   PDBsum; 1PEA; -.
DR   PDBsum; 1QNL; -.
DR   PDBsum; 1QO0; -.
DR   ProteinModelPortal; P27017; -.
DR   SMR; P27017; 7-380.
DR   IntAct; P27017; 1.
DR   GeneID; 877798; -.
DR   GenomeReviews; AE004091_GR; PA3364.
DR   KEGG; pae:PA3364; -.
DR   PATRIC; 19841329; VBIPseAer58763_3523.
DR   PseudoCAP; PA3364; -.
DR   eggNOG; COG0683; -.
DR   HOGENOM; HOG000202643; -.
DR   KO; K01999; -.
DR   OMA; TLYEGFE; -.
DR   ProtClustDB; CLSK867930; -.
DR   BioCyc; PAER208964:PA3364-MONOMER; -.
DR   EvolutionaryTrace; P27017; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:InterPro.
DR   InterPro; IPR000709; Leu_Ile_Val-bd.
DR   PRINTS; PR00337; LEUILEVALBP.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing; Kinase;
KW   Reference proteome; Repressor; Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    385       Aliphatic amidase expression-regulating
FT                                protein.
FT                                /FTId=PRO_0000064581.
FT   VARIANT     106    106       T -> N (in strain: PAC181; butyramide
FT                                inducible phenotype).
FT   CONFLICT     27     28       QR -> HA (in Ref. 1; CAA32024).
FT   CONFLICT    186    186       V -> L (in Ref. 1; CAA32024).
FT   CONFLICT    263    263       A -> P (in Ref. 1; CAA32024).
FT   CONFLICT    305    305       S -> N (in Ref. 1; CAA32024).
FT   CONFLICT    319    319       C -> D (in Ref. 1; CAA32024).
FT   CONFLICT    383    383       A -> P (in Ref. 1; CAA32024).
FT   STRAND        9     13
FT   STRAND       16     18
FT   HELIX        21     39
FT   TURN         40     43
FT   STRAND       50     54
FT   HELIX        60     72
FT   STRAND       78     81
FT   HELIX        85     97
FT   STRAND      101    104
FT   STRAND      117    119
FT   HELIX       124    126
FT   HELIX       128    136
FT   TURN        137    139
FT   STRAND      141    150
FT   HELIX       151    166
FT   STRAND      170    177
FT   HELIX       183    196
FT   STRAND      199    204
FT   HELIX       209    221
FT   STRAND      229    233
FT   HELIX       236    239
FT   HELIX       244    247
FT   STRAND      251    255
FT   HELIX       263    273
FT   HELIX       284    303
FT   HELIX       308    315
FT   STRAND      320    322
FT   STRAND      325    329
FT   TURN        331    333
FT   STRAND      336    338
FT   STRAND      341    345
FT   STRAND      351    356
FT   HELIX       369    371
FT   HELIX       376    378
SQ   SEQUENCE   385 AA;  42807 MW;  33924B6C36017B79 CRC64;
     MGSHQERPLI GLLFSETGVT ADIERSQRYG ALLAVEQLNR EGGVGGRPIE TLSQDPGGDP
     DRYRLCAEDF IRNRGVRFLV GCYMSHTRKA VMPVVERADA LLCYPTPYEG FEYSPNIVYG
     GPAPNQNSAP LAAYLIRHYG ERVVFIGSDY IYPRESNHVM RHLYRQHGGT VLEEIYIPLY
     PSDDDVQRAV ERIYQARADV VFSTVVGTGT AELYRAIARR YGDGRRPPIA SLTTSEAEVA
     KMESDVAEGQ VVVAPYFSSI DTAASRAFVQ ACHGFFPENA TITAWAEAAY WQTLLLGRAA
     QAAGSWRVED VQRHLYDICI DAPQGPVRVE RQNNHSRLSS RIAEIDARGV FQVRWQSPEP
     IRPDPYVVVH NLDDWSASMG GGALP
//
ID   AMIR_PSEAE              Reviewed;         196 AA.
AC   P10932;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   16-MAY-2012, entry version 93.
DE   RecName: Full=Aliphatic amidase regulator;
GN   Name=amiR; OrderedLocusNames=PA3363;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG
OS   12228).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PAC433;
RX   MEDLINE=89211409; PubMed=2495988; DOI=10.1016/0014-5793(89)80249-2;
RA   Lowe N., Rice P.M., Drew R.E.;
RT   "Nucleotide sequence of the aliphatic amidase regulator gene (amiR) of
RT   Pseudomonas aeruginosa.";
RL   FEBS Lett. 246:39-43(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   CHARACTERIZATION.
RX   MEDLINE=95286483; PubMed=7539417;
RA   Wilson S.A., Drew R.E.;
RT   "Transcriptional analysis of the amidase operon from Pseudomonas
RT   aeruginosa.";
RL   J. Bacteriol. 177:3052-3057(1995).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIC.
RC   STRAIN=PAC1;
RX   MEDLINE=99437995; PubMed=10508151; DOI=10.1093/emboj/18.19.5175;
RA   O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E.,
RA   Pearl L.H.;
RT   "Crystal structure and induction mechanism of AmiC-AmiR: a ligand-
RT   regulated transcription antitermination complex.";
RL   EMBO J. 18:5175-5186(1999).
CC   -!- FUNCTION: Positive controlling element of AmiE, the gene for
CC       aliphatic amidase. Acts as a transcriptional antitermination
CC       factor. It is thought to allow RNA polymerase read through a rho-
CC       independent transcription terminator between the AmiE promoter and
CC       gene.
CC   -!- SUBUNIT: Forms a complex with AmiC.
CC   -!- SIMILARITY: Contains 1 ANTAR domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; X13776; CAA32023.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06751.1; -; Genomic_DNA.
DR   PIR; B83226; B83226.
DR   PIR; S03884; S03884.
DR   RefSeq; NP_252053.1; NC_002516.2.
DR   PDB; 1QO0; X-ray; 2.25 A; D/E=1-196.
DR   PDBsum; 1QO0; -.
DR   ProteinModelPortal; P10932; -.
DR   SMR; P10932; 2-195.
DR   IntAct; P10932; 1.
DR   DNASU; 880573; -.
DR   GeneID; 880573; -.
DR   GenomeReviews; AE004091_GR; PA3363.
DR   KEGG; pae:PA3363; -.
DR   PATRIC; 19841327; VBIPseAer58763_3522.
DR   PseudoCAP; PA3363; -.
DR   eggNOG; COG3707; -.
DR   HOGENOM; HOG000247749; -.
DR   OMA; QRIGCQV; -.
DR   ProtClustDB; CLSK867929; -.
DR   BioCyc; PAER208964:PA3363-MONOMER; -.
DR   EvolutionaryTrace; P10932; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   InterPro; IPR005561; ANTAR.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR008327; Sig_transdc_resp-reg_antiterm.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF03861; ANTAR; 1.
DR   PIRSF; PIRSF036382; RR_antiterm; 1.
DR   SMART; SM01012; ANTAR; 1.
DR   SUPFAM; SSF52172; CheY_like; 1.
DR   PROSITE; PS50921; ANTAR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Reference proteome; Transcription;
KW   Transcription antitermination; Transcription regulation.
FT   CHAIN         1    196       Aliphatic amidase regulator.
FT                                /FTId=PRO_0000064582.
FT   DOMAIN      129    190       ANTAR.
FT   CONFLICT     48     48       S -> A (in Ref. 1; CAA32023).
FT   CONFLICT     64     64       R -> G (in Ref. 1; CAA32023).
FT   CONFLICT    141    141       E -> D (in Ref. 1; CAA32023).
FT   CONFLICT    154    154       A -> V (in Ref. 1; CAA32023).
FT   CONFLICT    170    170       Y -> H (in Ref. 1; CAA32023).
FT   HELIX         3      8
FT   HELIX         9     12
FT   STRAND       14     19
FT   HELIX        23     35
FT   STRAND       38     42
FT   STRAND       54     59
FT   HELIX        65     75
FT   STRAND       81     86
FT   HELIX        91    100
FT   STRAND      103    109
FT   HELIX       112    114
FT   HELIX       115    160
FT   HELIX       164    175
FT   TURN        176    179
FT   HELIX       182    189
SQ   SEQUENCE   196 AA;  21903 MW;  306A4F30E8E4C6C0 CRC64;
     MSANSLLGSL RELQVLVLNP PGEVSDALVL QLIRIGCSVR QCWPPPESFD VPVDVVFTSI
     FQNRHHDEIA ALLAAGTPRT TLVALVEYES PAVLSQIIEL ECHGVITQPL DAHRVLPVLV
     SARRISEEMA KLKQKTEQLQ ERIAGQARIN QAKALLMQRH GWDEREAHQY LSREAMKRRE
     PILKIAQELL GNEPSA
//
ID   AQP1_HUMAN              Reviewed;         269 AA.
AC   P29972; B5BU39; Q8TBI5; Q8TDC1;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-MAY-2012, entry version 142.
DE   RecName: Full=Aquaporin-1;
DE            Short=AQP-1;
DE   AltName: Full=Aquaporin-CHIP;
DE   AltName: Full=Urine water channel;
DE   AltName: Full=Water channel protein for red blood cells and kidney proximal tubule;
GN   Name=AQP1; Synonyms=CHIP28;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=92107900; PubMed=1722319; DOI=10.1073/pnas.88.24.11110;
RA   Preston G.M., Agre P.;
RT   "Isolation of the cDNA for erythrocyte integral membrane protein of 28
RT   kilodaltons: member of an ancient channel family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93340184; PubMed=8340403;
RA   Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.;
RT   "The human aquaporin-CHIP gene. Structure, organization, and
RT   chromosomal localization.";
RL   J. Biol. Chem. 268:15772-15778(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retinal pigment epithelium;
RX   MEDLINE=96326579; PubMed=8703970; DOI=10.1016/0005-2736(96)00076-4;
RA   Ruiz A.C., Bok D.;
RT   "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in
RT   human retinal pigment epithelium.";
RL   Biochim. Biophys. Acta 1282:174-178(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Uterus;
RX   MEDLINE=94290349; PubMed=7517253;
RA   Li X., Yu H., Koide S.S.;
RT   "The water channel gene in human uterus.";
RL   Biochem. Mol. Biol. Int. 32:371-377(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-45 AND ASP-165.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA   Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA   Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA   Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA   Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA   Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA   Isogai T., Imai J., Watanabe S., Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in
RT   vitro-expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-269.
RC   TISSUE=Articular cartilage;
RA   Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.;
RT   "Human chondrocytes in situ express aquaporin water channels: changes
RT   in AQP1 abundance in pathologies of articular cartilage.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   PROTEIN SEQUENCE OF 2-36.
RX   PubMed=2007592;
RA   Smith B.L., Agre P.;
RT   "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit
RT   oligomer similar to channel proteins.";
RL   J. Biol. Chem. 266:6407-6415(1991).
RN   [12]
RP   FUNCTION.
RX   MEDLINE=92229472; PubMed=1373524; DOI=10.1126/science.256.5055.385;
RA   Preston G.M., Carroll T.P., Guggino W.B., Agre P.;
RT   "Appearance of water channels in Xenopus oocytes expressing red cell
RT   CHIP28 protein.";
RL   Science 256:385-387(1992).
RN   [13]
RP   TARGET OF MERCURY INHIBITION.
RX   MEDLINE=93106996; PubMed=7677994;
RA   Preston G.M., Jung J.S., Guggino W.B., Agre P.;
RT   "The mercury-sensitive residue at cysteine 189 in the CHIP28 water
RT   channel.";
RL   J. Biol. Chem. 268:17-20(1993).
RN   [14]
RP   TOPOLOGY.
RX   MEDLINE=94124503; PubMed=7507481;
RA   Preston G.M., Jung J.S., Guggino W.B., Agre P.;
RT   "Membrane topology of aquaporin CHIP. Analysis of functional epitope-
RT   scanning mutants by vectorial proteolysis.";
RL   J. Biol. Chem. 269:1668-1673(1994).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [16]
RP   STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS).
RX   MEDLINE=94313979; PubMed=7518771;
RA   Walz T., Smith B.L., Agre P., Engel A.;
RT   "The three-dimensional structure of human erythrocyte aquaporin
RT   CHIP.";
RL   EMBO J. 13:2985-2993(1994).
RN   [17]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
RX   MEDLINE=97320502; PubMed=9177353; DOI=10.1038/42512;
RA   Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., Fujiyoshi Y.,
RA   Smith B.L., Agre P., Engel A.;
RT   "The three-dimensional structure of aquaporin-1.";
RL   Nature 387:624-627(1997).
RN   [18]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS).
RX   MEDLINE=20487015; PubMed=11034202; DOI=10.1038/35036519;
RA   Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B.,
RA   Engel A., Fujiyoshi Y.;
RT   "Structural determinants of water permeation through aquaporin-1.";
RL   Nature 407:599-605(2000).
RN   [19]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
RX   MEDLINE=21423577; PubMed=11532455; DOI=10.1016/S0014-5793(01)02743-0;
RA   de Groot B.L., Engel A., Grubmueller H.;
RT   "A refined structure of human aquaporin-1.";
RL   FEBS Lett. 504:206-211(2001).
RN   [20]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS).
RX   PubMed=11171962; DOI=10.1073/pnas.041489198;
RA   Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.;
RT   "Visualization of a water-selective pore by electron crystallography
RT   in vitreous ice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001).
RN   [21]
RP   VARIANT BLOOD GROUP COLTON VAL-45.
RX   MEDLINE=94365170; PubMed=7521882; DOI=10.1172/JCI117418;
RA   Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.;
RT   "Human red cell aquaporin CHIP. I. Molecular characterization of ABH
RT   and Colton blood group antigens.";
RL   J. Clin. Invest. 94:1043-1049(1994).
RN   [22]
RP   VARIANT LEU-38.
RX   MEDLINE=94360246; PubMed=7521540; DOI=10.1126/science.7521540;
RA   Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.;
RT   "Mutations in aquaporin-1 in phenotypically normal humans without
RT   functional CHIP water channels.";
RL   Science 265:1585-1587(1994).
CC   -!- FUNCTION: Forms a water-specific channel that provides the plasma
CC       membranes of red cells and kidney proximal tubules with high
CC       permeability to water, thereby permitting water to move in the
CC       direction of an osmotic gradient.
CC   -!- SUBUNIT: Homotetramer. Interacts with EPHB2; involved in endolymph
CC       production in the inner ear (By similarity).
CC   -!- INTERACTION:
CC       Q99750:MDFI; NbExp=4; IntAct=EBI-745213, EBI-724076;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in a number of tissues including
CC       erythrocytes, renal tubules, retinal pigment epithelium, heart,
CC       lung, skeletal muscle, kidney and pancreas. Weakly expressed in
CC       brain, placenta and liver.
CC   -!- DOMAIN: Aquaporins contain two tandem repeats each containing
CC       three membrane-spanning domains and a pore-forming loop with the
CC       signature motif Asn-Pro-Ala (NPA).
CC   -!- POLYMORPHISM: AQP1 is responsible for the Colton blood group
CC       system. Approximately 92% of Caucasians are Co(A+B-) (Ala-46),
CC       approximately 8% are Co(A+B+), and only 0.2% are Co(A-B+) (Val-
CC       46). Co(A-B-) which is very rare, is due to a complete absence of
CC       AQP1.
CC   -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar
CC       concentrations of mercury.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC   -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
CC       mutation database;
CC       URL="http://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=colton";
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/aqp1/";
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Liquid states - Issue
CC       36 of July 2003;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt036.shtml";
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DR   EMBL; M77829; AAA58425.1; -; mRNA.
DR   EMBL; U41517; AAC50648.1; -; mRNA.
DR   EMBL; U41518; AAC50649.1; -; mRNA.
DR   EMBL; S73482; AAB31193.1; -; mRNA.
DR   EMBL; AC004691; AAC16481.1; -; Genomic_DNA.
DR   EMBL; AC005155; AAC23788.1; -; Genomic_DNA.
DR   EMBL; AY953319; AAX24129.1; -; Genomic_DNA.
DR   EMBL; AB451275; BAG70089.1; -; mRNA.
DR   EMBL; AB451402; BAG70216.1; -; mRNA.
DR   EMBL; CH471073; EAW93971.1; -; Genomic_DNA.
DR   EMBL; BC022486; AAH22486.1; -; mRNA.
DR   EMBL; AF480415; AAL87136.1; -; Genomic_DNA.
DR   IPI; IPI00024689; -.
DR   PIR; A41616; A41616.
DR   PIR; I52366; I52366.
DR   RefSeq; NP_932766.1; NM_198098.2.
DR   UniGene; Hs.76152; -.
DR   PDB; 1FQY; X-ray; 3.80 A; A=1-269.
DR   PDB; 1H6I; X-ray; 3.54 A; A=1-269.
DR   PDB; 1IH5; X-ray; 3.70 A; A=1-269.
DR   PDBsum; 1FQY; -.
DR   PDBsum; 1H6I; -.
DR   PDBsum; 1IH5; -.
DR   ProteinModelPortal; P29972; -.
DR   SMR; P29972; 9-233.
DR   DIP; DIP-29607N; -.
DR   IntAct; P29972; 7.
DR   MINT; MINT-1439356; -.
DR   STRING; P29972; -.
DR   TCDB; 1.A.8.8.1; major intrinsic protein (MIP) family.
DR   PhosphoSite; P29972; -.
DR   DMDM; 267412; -.
DR   PRIDE; P29972; -.
DR   DNASU; 358; -.
DR   Ensembl; ENST00000311813; ENSP00000311165; ENSG00000240583.
DR   GeneID; 358; -.
DR   KEGG; hsa:358; -.
DR   UCSC; uc003tbv.2; human.
DR   CTD; 358; -.
DR   GeneCards; GC07P030917; -.
DR   HGNC; HGNC:633; AQP1.
DR   HPA; CAB001707; -.
DR   HPA; HPA019206; -.
DR   MIM; 107776; gene.
DR   MIM; 110450; phenotype.
DR   neXtProt; NX_P29972; -.
DR   PharmGKB; PA24918; -.
DR   eggNOG; COG0580; -.
DR   GeneTree; ENSGT00550000074347; -.
DR   HOGENOM; HOG000288286; -.
DR   HOVERGEN; HBG000312; -.
DR   InParanoid; P29972; -.
DR   KO; K09864; -.
DR   OMA; ITHNFKD; -.
DR   OrthoDB; EOG46T328; -.
DR   PhylomeDB; P29972; -.
DR   Reactome; REACT_15518; Transmembrane transport of small molecules.
DR   DrugBank; DB00819; Acetazolamide.
DR   EvolutionaryTrace; P29972; -.
DR   NextBio; 1497; -.
DR   ArrayExpress; P29972; -.
DR   Bgee; P29972; -.
DR   CleanEx; HS_AQP1; -.
DR   Genevestigator; P29972; -.
DR   GermOnline; ENSG00000106125; Homo sapiens.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR   GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR   GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR   GO; GO:0020003; C:symbiont-containing vacuole; ISS:UniProtKB.
DR   GO; GO:0051739; F:ammonia transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0035379; F:carbon dioxide transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005223; F:intracellular cGMP activated cation channel activity; IDA:UniProtKB.
DR   GO; GO:0030184; F:nitric oxide transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005267; F:potassium channel activity; IMP:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR   GO; GO:0015696; P:ammonium transport; IDA:UniProtKB.
DR   GO; GO:0006884; P:cell volume homeostasis; IMP:UniProtKB.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IMP:UniProtKB.
DR   GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR   GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
DR   GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:UniProtKB.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR   GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB.
DR   GO; GO:0071288; P:cellular response to mercury ion; IDA:UniProtKB.
DR   GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR   GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB.
DR   GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR   GO; GO:0033326; P:cerebrospinal fluid secretion; IEP:UniProtKB.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:UniProtKB.
DR   GO; GO:0021670; P:lateral ventricle development; IEP:UniProtKB.
DR   GO; GO:0085018; P:maintenance of symbiont-containing vacuole via substance secreted by host; IMP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR   GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
DR   GO; GO:0030157; P:pancreatic juice secretion; IEP:UniProtKB.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
DR   GO; GO:0046878; P:positive regulation of saliva secretion; IMP:UniProtKB.
DR   GO; GO:0003097; P:renal water transport; IDA:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IDA:UniProtKB.
DR   GO; GO:0035377; P:transepithelial water transport; IDA:UniProtKB.
DR   Gene3D; G3DSA:1.20.1080.10; MIP; 1.
DR   InterPro; IPR012269; Aquaporin.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR023274; Aquaporin_1.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR19139; MIP; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR02013; AQUAPORIN1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; MIP; 1.
DR   TIGRFAMs; TIGR00861; MIP; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Blood group antigen; Complete proteome;
KW   Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    269       Aquaporin-1.
FT                                /FTId=PRO_0000063920.
FT   TOPO_DOM      2      7       Cytoplasmic.
FT   TRANSMEM      8     36       Helical; Name=Helix 1.
FT   TOPO_DOM     37     48       Extracellular.
FT   TRANSMEM     49     66       Helical; Name=Helix 2.
FT   TOPO_DOM     67     70       Cytoplasmic.
FT   INTRAMEM     71     76
FT   INTRAMEM     77     84       Helical; Name=Helix B.
FT   TOPO_DOM     85     94       Cytoplasmic.
FT   TRANSMEM     95    115       Helical; Name=Helix 3.
FT   TOPO_DOM    116    136       Extracellular.
FT   TRANSMEM    137    155       Helical; Name=Helix 4.
FT   TOPO_DOM    156    166       Cytoplasmic.
FT   TRANSMEM    167    183       Helical; Name=Helix 5.
FT   TOPO_DOM    184    186       Extracellular.
FT   INTRAMEM    187    192
FT   INTRAMEM    193    200       Helical; Name=Helix E.
FT   TOPO_DOM    201    207       Extracellular.
FT   TRANSMEM    208    228       Helical; Name=Helix 6.
FT   TOPO_DOM    229    269       Cytoplasmic.
FT   MOTIF        76     78       NPA 1.
FT   MOTIF       192    194       NPA 2.
FT   COMPBIAS    159    162       Poly-Arg.
FT   SITE         56     56       Substrate discrimination.
FT   SITE        180    180       Substrate discrimination.
FT   SITE        189    189       Hg(2+)-sensitive residue.
FT   SITE        195    195       Substrate discrimination.
FT   MOD_RES     246    246       Phosphothreonine (By similarity).
FT   MOD_RES     247    247       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphoserine.
FT   CARBOHYD     42     42       N-linked (GlcNAc...).
FT   CARBOHYD    205    205       N-linked (GlcNAc...) (Potential).
FT   VARIANT      38     38       P -> L (in Co(A-B-) antigen; non
FT                                functional AQP1; red cells show low
FT                                osmotic water permeability).
FT                                /FTId=VAR_013279.
FT   VARIANT      45     45       A -> V (in Co(A-B+) antigen;
FT                                dbSNP:rs28362692).
FT                                /FTId=VAR_004400.
FT   VARIANT     165    165       G -> D (in dbSNP:rs28362731).
FT                                /FTId=VAR_022318.
FT   CONFLICT     45     45       A -> T (in Ref. 9; AAH22486).
FT   HELIX         8     35
FT   STRAND       37     42
FT   HELIX        48     65
FT   STRAND       68     71
FT   HELIX        76     83
FT   HELIX        94    114
FT   TURN        119    122
FT   STRAND      132    135
FT   HELIX       136    154
FT   HELIX       166    182
FT   TURN        183    185
FT   HELIX       192    199
FT   HELIX       207    227
SQ   SEQUENCE   269 AA;  28526 MW;  BA204D82FB26352E CRC64;
     MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI
     ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT
     GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH
     LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD
     RVKVWTSGQV EEYDLDADDI NSRVEMKPK
//
ID   ARF3_TAKRU              Reviewed;         181 AA.
AC   P61207; P16587;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 60.
DE   RecName: Full=ADP-ribosylation factor 3;
GN   Name=arf3;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99177347; PubMed=10077531;
RA   Gellner K., Brenner S.;
RT   "Analysis of 148 kb of genomic DNA around the wnt1 locus of Fugu
RT   rubripes.";
RL   Genome Res. 9:251-258(1999).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; AF056116; AAC34390.1; -; Genomic_DNA.
DR   ProteinModelPortal; P61207; -.
DR   SMR; P61207; 18-177.
DR   PRIDE; P61207; -.
DR   eggNOG; COG1100; -.
DR   InParanoid; P61207; -.
DR   OrthoDB; EOG4PZJ7Q; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   3: Inferred from homology;
KW   Complete proteome; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW   Lipoprotein; Myristate; Nucleotide-binding; Protein transport;
KW   Reference proteome; Transport.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    181       ADP-ribosylation factor 3.
FT                                /FTId=PRO_0000207390.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   181 AA;  20601 MW;  D6FA234DFAED3E5F CRC64;
     MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
     K
//
ID   ARF3_HUMAN              Reviewed;         181 AA.
AC   P61204; A8K6G8; P16587;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 83.
DE   RecName: Full=ADP-ribosylation factor 3;
GN   Name=ARF3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cerebellum;
RX   MEDLINE=89345613; PubMed=2474826; DOI=10.1073/pnas.86.16.6101;
RA   Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J.,
RA   Vaughan M.;
RT   "Molecular cloning, characterization, and expression of human ADP-
RT   ribosylation factors: two guanine nucleotide-dependent activators of
RT   cholera toxin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92078170; PubMed=1744102;
RA   Tsai S.C., Haun R.S., Tsuchiya M., Moss J., Vaughan M.;
RT   "Isolation and characterization of the human gene for ADP-ribosylation
RT   factor 3, a 20-kDa guanine nucleotide-binding protein activator of
RT   cholera toxin.";
RL   J. Biol. Chem. 266:23053-23059(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction
RT   sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Lung, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   INTERACTION WITH PRKCABP.
RX   MEDLINE=20090608; PubMed=10623590; DOI=10.1006/bbrc.1999.1932;
RA   Takeya R., Takeshige K., Sumimoto H.;
RT   "Interaction of the PDZ domain of human PICK1 with class I ADP-
RT   ribosylation factors.";
RL   Biochem. Biophys. Res. Commun. 267:149-155(2000).
RN   [9]
RP   INTERACTION WITH PI4KB AND NCS1, AND SUBCELLULAR LOCATION.
RX   PubMed=17555535; DOI=10.1111/j.1600-0854.2007.00594.x;
RA   Haynes L.P., Sherwood M.W., Dolman N.J., Burgoyne R.D.;
RT   "Specificity, promiscuity and localization of ARF protein interactions
RT   with NCS-1 and phosphatidylinositol-4 kinase-III beta.";
RL   Traffic 8:1080-1092(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SUBUNIT: Interacts with PRKCABP. Interacts with PI4KB and
CC       NCS1/FREQ at the Golgi complex.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear
CC       region.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC   -----------------------------------------------------------------------
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DR   EMBL; M74493; AAA58359.1; -; Genomic_DNA.
DR   EMBL; M33384; AAA83931.1; -; mRNA.
DR   EMBL; M74491; AAB59425.1; -; mRNA.
DR   EMBL; AF493882; AAM12596.1; -; mRNA.
DR   EMBL; BT006670; AAP35316.1; -; mRNA.
DR   EMBL; AK291633; BAF84322.1; -; mRNA.
DR   EMBL; CH471111; EAW58026.1; -; Genomic_DNA.
DR   EMBL; BC007647; AAH07647.1; -; mRNA.
DR   EMBL; BC007762; AAH07762.1; -; mRNA.
DR   EMBL; BC017565; AAH17565.1; -; mRNA.
DR   EMBL; BC028402; AAH28402.1; -; mRNA.
DR   IPI; IPI00215917; -.
DR   PIR; A41570; A41570.
DR   RefSeq; NP_001650.1; NM_001659.2.
DR   UniGene; Hs.119177; -.
DR   ProteinModelPortal; P61204; -.
DR   SMR; P61204; 18-177.
DR   IntAct; P61204; 7.
DR   STRING; P61204; -.
DR   PhosphoSite; P61204; -.
DR   DMDM; 47117657; -.
DR   OGP; P16587; -.
DR   PeptideAtlas; P61204; -.
DR   PRIDE; P61204; -.
DR   DNASU; 377; -.
DR   Ensembl; ENST00000256682; ENSP00000256682; ENSG00000134287.
DR   Ensembl; ENST00000541959; ENSP00000438510; ENSG00000134287.
DR   GeneID; 377; -.
DR   KEGG; hsa:377; -.
DR   UCSC; uc001rsr.2; human.
DR   CTD; 377; -.
DR   GeneCards; GC12M049299; -.
DR   HGNC; HGNC:654; ARF3.
DR   MIM; 103190; gene.
DR   neXtProt; NX_P61204; -.
DR   PharmGKB; PA24936; -.
DR   eggNOG; COG1100; -.
DR   GeneTree; ENSGT00650000093078; -.
DR   HOGENOM; HOG000163691; -.
DR   HOVERGEN; HBG002073; -.
DR   InParanoid; P61204; -.
DR   KO; K07938; -.
DR   OMA; LWGKKEM; -.
DR   OrthoDB; EOG4PZJ7Q; -.
DR   PhylomeDB; P61204; -.
DR   NextBio; 1579; -.
DR   ArrayExpress; P61204; -.
DR   Bgee; P61204; -.
DR   CleanEx; HS_ARF3; -.
DR   Genevestigator; P61204; -.
DR   GermOnline; ENSG00000134287; Homo sapiens.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR   GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW   GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    181       ADP-ribosylation factor 3.
FT                                /FTId=PRO_0000207386.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   181 AA;  20601 MW;  D6FA234DFAED3E5F CRC64;
     MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
     K
//
ID   ARF3_MOUSE              Reviewed;         181 AA.
AC   P61205; P16587;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 82.
DE   RecName: Full=ADP-ribosylation factor 3;
GN   Name=Arf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=97103475; PubMed=8947846;
RA   Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.;
RT   "Structure and intracellular localization of mouse ADP-ribosylation
RT   factors type 1 to type 6 (ARF1-ARF6).";
RL   J. Biochem. 120:813-819(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SUBUNIT: Interacts with PRKCABP (By similarity). Interacts with
CC       PI4KB and NCS1/FREQ at the Golgi complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Cytoplasm,
CC       perinuclear region (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D87900; BAA13492.1; -; mRNA.
DR   EMBL; BC014778; AAH14778.1; -; mRNA.
DR   EMBL; BC024935; AAH24935.1; -; mRNA.
DR   IPI; IPI00221614; -.
DR   PIR; JC4947; JC4947.
DR   RefSeq; NP_031504.1; NM_007478.3.
DR   UniGene; Mm.221298; -.
DR   ProteinModelPortal; P61205; -.
DR   SMR; P61205; 18-177.
DR   IntAct; P61205; 2.
DR   STRING; P61205; -.
DR   PhosphoSite; P61205; -.
DR   PRIDE; P61205; -.
DR   Ensembl; ENSMUST00000053183; ENSMUSP00000050689; ENSMUSG00000051853.
DR   GeneID; 11842; -.
DR   KEGG; mmu:11842; -.
DR   CTD; 377; -.
DR   MGI; MGI:99432; Arf3.
DR   HOGENOM; HOG000163691; -.
DR   HOVERGEN; HBG002073; -.
DR   InParanoid; P61205; -.
DR   KO; K07938; -.
DR   OMA; LWGKKEM; -.
DR   OrthoDB; EOG4PZJ7Q; -.
DR   NextBio; 279791; -.
DR   ArrayExpress; P61205; -.
DR   Bgee; P61205; -.
DR   CleanEx; MM_ARF3; -.
DR   Genevestigator; P61205; -.
DR   GermOnline; ENSMUSG00000051853; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; TAS:MGI.
DR   GO; GO:0015031; P:protein transport; TAS:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW   GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    181       ADP-ribosylation factor 3.
FT                                /FTId=PRO_0000207387.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   181 AA;  20601 MW;  D6FA234DFAED3E5F CRC64;
     MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
     K
//
ID   ARF3_RAT                Reviewed;         181 AA.
AC   P61206; P16587;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 77.
DE   RecName: Full=ADP-ribosylation factor 3;
DE   AltName: Full=Liver regeneration-related protein LRRG202;
GN   Name=Arf3; ORFNames=Ac1-253;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=96408698; PubMed=8813705; DOI=10.1007/BF00226058;
RA   Price S.R., Nightingale M.S., Tsuchiya M., Moss J., Vaughan M.;
RT   "Interspecies relationships among ADP-ribosylation factors (ARFs):
RT   evidence of evolutionary pressure to maintain individual identities.";
RL   Mol. Cell. Biochem. 159:15-23(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RA   Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y.,
RA   Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F.,
RA   Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT   "Liver regeneration after PH.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SUBUNIT: Interacts with PRKCABP (By similarity). Interacts with
CC       PI4KB and NCS1/FREQ at the Golgi complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Cytoplasm,
CC       perinuclear region (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; L12382; AAA40687.1; -; mRNA.
DR   EMBL; AY325223; AAP92624.1; -; mRNA.
DR   EMBL; BC088865; AAH88865.1; -; mRNA.
DR   IPI; IPI00231674; -.
DR   RefSeq; NP_543180.1; NM_080904.2.
DR   UniGene; Rn.106440; -.
DR   ProteinModelPortal; P61206; -.
DR   SMR; P61206; 18-177.
DR   IntAct; P61206; 1.
DR   MINT; MINT-1775307; -.
DR   STRING; P61206; -.
DR   PhosphoSite; P61206; -.
DR   World-2DPAGE; 0004:P61206; -.
DR   PRIDE; P61206; -.
DR   Ensembl; ENSRNOT00000044558; ENSRNOP00000047811; ENSRNOG00000033155.
DR   GeneID; 140940; -.
DR   KEGG; rno:140940; -.
DR   UCSC; NM_080904; rat.
DR   CTD; 377; -.
DR   RGD; 621273; Arf3.
DR   GeneTree; ENSGT00650000093078; -.
DR   HOGENOM; HOG000163691; -.
DR   HOVERGEN; HBG002073; -.
DR   InParanoid; P61206; -.
DR   KO; K07938; -.
DR   OMA; LWGKKEM; -.
DR   OrthoDB; EOG4PZJ7Q; -.
DR   NextBio; 620834; -.
DR   ArrayExpress; P61206; -.
DR   Genevestigator; P61206; -.
DR   GermOnline; ENSRNOG00000033155; Rattus norvegicus.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR024156; Small_GTPase_ARF.
DR   InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; Small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW   GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    181       ADP-ribosylation factor 3.
FT                                /FTId=PRO_0000207389.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   181 AA;  20601 MW;  D6FA234DFAED3E5F CRC64;
     MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
     LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK
     K
//
ID   BGAL_ECOLI              Reviewed;        1024 AA.
AC   P00722; Q2MC80;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 140.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ; OrderedLocusNames=b0344, JW0335;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84028567; PubMed=6313347;
RA   Kalnins A., Otto K., Ruether U., Mueller-Hill B.;
RT   "Sequence of the lacZ gene of Escherichia coli.";
RL   EMBO J. 2:593-597(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-1024.
RX   MEDLINE=78218239; PubMed=97298;
RA   Fowler A.V., Zabin I.;
RT   "Amino acid sequence of beta-galactosidase. XI. Peptide ordering
RT   procedures and the complete sequence.";
RL   J. Biol. Chem. 253:5521-5525(1978).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-476.
RX   MEDLINE=80188189; PubMed=6246435; DOI=10.1038/285038a0;
RA   Calos M.P., Miller J.H.;
RT   "Molecular consequences of deletion formation mediated by the
RT   transposon Tn9.";
RL   Nature 285:38-41(1980).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1008-1024.
RX   MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0;
RA   Buechel D.E., Gronenborn B., Mueller-Hill B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
RN   [8]
RP   INDUCTION BY ALLOLACTOSE.
RX   PubMed=4562709; DOI=10.1016/0022-2836(72)90253-7;
RA   Jobe A., Bourgeois S.;
RT   "lac repressor-operator interaction. VI. The natural inducer of the
RT   lac operon.";
RL   J. Mol. Biol. 69:397-408(1972).
RN   [9]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX   PubMed=114210; DOI=10.1021/bi00586a005;
RA   Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.;
RT   "Interaction of divalent cations with beta-galactosidase (Escherichia
RT   coli).";
RL   Biochemistry 18:4090-4095(1979).
RN   [10]
RP   ACTIVE SITE REGIONS.
RX   MEDLINE=83290932; PubMed=6411710;
RA   Fowler A.V., Smith P.J.;
RT   "The active site regions of lacZ and ebg beta-galactosidases are
RT   homologous.";
RL   J. Biol. Chem. 258:10204-10207(1983).
RN   [11]
RP   ACTIVE SITE GLU-462.
RX   MEDLINE=84108409; PubMed=6420154;
RX   DOI=10.1111/j.1432-1033.1984.tb07947.x;
RA   Herrchen M., Legler G.;
RT   "Identification of an essential carboxylate group at the active site
RT   of lacZ beta-galactosidase from Escherichia coli.";
RL   Eur. J. Biochem. 138:527-531(1984).
RN   [12]
RP   ACTIVE SITE GLU-538.
RX   MEDLINE=92283812; PubMed=1350782;
RA   Gebler J.C., Aebersold R., Withers S.G.;
RT   "Glu-537, not Glu-461, is the nucleophile in the active site of (lac
RT   Z) beta-galactosidase from Escherichia coli.";
RL   J. Biol. Chem. 267:11126-11130(1992).
RN   [13]
RP   MUTAGENESIS OF GLU-462, AND COFACTOR.
RX   PubMed=7577931; DOI=10.1021/bi00041a022;
RA   Martinez-Bilbao M., Gaunt M.T., Huber R.E.;
RT   "E461H-beta-galactosidase (Escherichia coli): altered divalent metal
RT   specificity and slow but reversible metal inactivation.";
RL   Biochemistry 34:13437-13442(1995).
RN   [14]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-541.
RX   PubMed=8662937; DOI=10.1074/jbc.271.24.14296;
RA   Roth N.J., Huber R.E.;
RT   "The beta-galactosidase (Escherichia coli) reaction is partly
RT   facilitated by interactions of His-540 with the C6 hydroxyl of
RT   galactose.";
RL   J. Biol. Chem. 271:14296-14301(1996).
RN   [15]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-358.
RX   PubMed=9665715; DOI=10.1021/bi972796t;
RA   Roth N.J., Rob B., Huber R.E.;
RT   "His-357 of beta-galactosidase (Escherichia coli) interacts with the
RT   C3 hydroxyl in the transition state and helps to mediate catalysis.";
RL   Biochemistry 37:10099-10107(1998).
RN   [16]
RP   MUTAGENESIS OF HIS-392.
RX   PubMed=11310566; DOI=10.1139/bcb-79-2-183;
RA   Huber R.E., Hlede I.Y., Roth N.J., McKenzie K.C., Ghumman K.K.;
RT   "His-391 of beta-galactosidase (Escherichia coli) promotes catalyses
RT   by strong interactions with the transition state.";
RL   Biochem. Cell Biol. 79:183-193(2001).
RN   [17]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TRP-1000.
RX   PubMed=12578395; DOI=10.1021/bi0270642;
RA   Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.;
RT   "Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for
RT   binding, catalysis, and synthesis of allolactose, the natural lac
RT   operon inducer.";
RL   Biochemistry 42:1796-1803(2003).
RN   [18]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-202.
RX   PubMed=15060622; DOI=10.1139/o04-004;
RA   Xu J., McRae M.A., Harron S., Rob B., Huber R.E.;
RT   "A study of the relationships of interactions between Asp-201, Na+ or
RT   K+, and galactosyl C6 hydroxyl and their effects on binding and
RT   reactivity of beta-galactosidase.";
RL   Biochem. Cell Biol. 82:275-284(2004).
RN   [19]
RP   REVIEW.
RX   PubMed=15950161; DOI=10.1016/j.crvi.2005.03.006;
RA   Matthews B.W.;
RT   "The structure of E. coli beta-galactosidase.";
RL   C. R. Biol. 328:549-556(2005).
RN   [20]
RP   COFACTOR, AND MUTAGENESIS OF GLU-798.
RX   PubMed=17126292; DOI=10.1016/j.bbrc.2006.11.061;
RA   Sutendra G., Wong S., Fraser M.E., Huber R.E.;
RT   "Beta-galactosidase (Escherichia coli) has a second catalytically
RT   important Mg2+ site.";
RL   Biochem. Biophys. Res. Commun. 352:566-570(2007).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP   AND SUBUNIT.
RX   MEDLINE=94277211; PubMed=8008071; DOI=10.1038/369761a0;
RA   Jacobson R.H., Zhang X.-J., Dubose R.F., Matthews B.W.;
RT   "Three-dimensional structure of beta-galactosidase from E. coli.";
RL   Nature 369:761-766(1994).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
RP   SODIUM IONS.
RX   PubMed=11045615;
RA   Juers D.H., Jacobson R.H., Wigley D., Zhang X.-J., Huber R.E.,
RA   Tronrud D.E., Matthews B.W.;
RT   "High resolution refinement of beta-galactosidase in a new crystal
RT   form reveals multiple metal-binding sites and provides a structural
RT   basis for alpha-complementation.";
RL   Protein Sci. 9:1685-1699(2000).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ANALOGS
RP   SUBSTRATE, MUTAGENESIS OF GLU-538 AND PHE-602, AND REACTION MECHANISM.
RX   MEDLINE=21590184; PubMed=11732897; DOI=10.1021/bi011727i;
RA   Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L.,
RA   Withers S.G., Matthews B.W.;
RT   "A structural view of the action of Escherichia coli (lacZ) beta-
RT   galactosidase.";
RL   Biochemistry 40:14781-14794(2001).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN
RP   COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND ANALOGS SUBSTRATE,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND MUTAGENESIS OF
RP   GLY-795.
RX   PubMed=14621996; DOI=10.1021/bi035506j;
RA   Juers D.H., Hakda S., Matthews B.W., Huber R.E.;
RT   "Structural basis for the altered activity of Gly794 variants of
RT   Escherichia coli beta-galactosidase.";
RL   Biochemistry 42:13505-13511(2003).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
CC       galactose residues in beta-D-galactosides.
CC   -!- COFACTOR: Binds 2 magnesium ions per monomer. Can also use
CC       manganese.
CC   -!- COFACTOR: Binds 1 sodium ion per monomer.
CC   -!- ENZYME REGULATION: Inhibited by phenylethyl thio-beta-D-
CC       galactoside (PETG), isopropyl thio-beta-D-galactoside (IPTG), L-
CC       ribose, D-galactonolactone, lactose and 2-amino-D-galactose.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.04 mM for p-nitrophenyl beta-D-galactoside;
CC         KM=0.12 mM for o-nitrophenyl beta-D-galactoside;
CC         KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside;
CC         KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside;
CC         KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside;
CC         KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside;
CC         KM=34 uM for p-nitrophenyl beta-D-galactoside (with magnesium as
CC         cofactor and 30 degrees Celsius);
CC         KM=140 uM for o-nitrophenyl beta-D-galactoside (with magnesium
CC         as cofactor and 30 degrees Celsius);
CC         KM=940 uM for allolactose (with magnesium as cofactor and 30
CC         degrees Celsius);
CC         KM=1350 uM for lactose (with magnesium as cofactor and 30
CC         degrees Celsius);
CC         Vmax=30.9 umol/min/mg enzyme with lactose as substrate (with
CC         magnesium as cofactor and 30 degrees Celsius);
CC         Vmax=49.7 umol/min/mg enzyme with allolactose as substrate (with
CC         magnesium as cofactor and 30 degrees Celsius);
CC         Vmax=59.7 umol/min/mg enzyme with p-nitrophenyl beta-D-
CC         galactoside as substrate (with magnesium as cofactor and 30
CC         degrees Celsius);
CC         Vmax=360 umol/min/mg enzyme with o-nitrophenyl beta-D-
CC         galactoside as substrate (with magnesium as cofactor and 30
CC         degrees Celsius);
CC         Note=The values for the enzymatic assays using manganese as
CC         cofactor are very close;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       P03023:lacI; NbExp=1; IntAct=EBI-369998, EBI-909231;
CC       P0ACA1:yibF; NbExp=1; IntAct=EBI-369998, EBI-1133142;
CC   -!- INDUCTION: By allolactose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="http://www.worthington-biochem.com/BG/";
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DR   EMBL; J01636; AAA24053.1; -; Genomic_DNA.
DR   EMBL; V00296; CAA23573.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18068.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73447.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76126.1; -; Genomic_DNA.
DR   EMBL; V00295; CAA23570.1; -; Genomic_DNA.
DR   PIR; A90981; GBEC.
DR   RefSeq; NP_414878.1; NC_000913.2.
DR   PDB; 1BGL; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-1024.
DR   PDB; 1BGM; X-ray; 2.50 A; I/J/K/L/M/N/O/P=2-1024.
DR   PDB; 1DP0; X-ray; 1.70 A; A/B/C/D=10-1024.
DR   PDB; 1F49; X-ray; 2.50 A; A/B/C/D/E/F/G/H=2-1024.
DR   PDB; 1F4A; X-ray; 2.80 A; A/B/C/D=4-1024.
DR   PDB; 1F4H; X-ray; 2.80 A; A/B/C/D=4-1024.
DR   PDB; 1GHO; X-ray; 2.50 A; I/J/K/L/M/N/O/P=2-1024.
DR   PDB; 1HN1; X-ray; 3.00 A; A/B/C/D=10-1023.
DR   PDB; 1JYN; X-ray; 1.80 A; A/B/C/D=10-1024.
DR   PDB; 1JYV; X-ray; 1.75 A; A/B/C/D=10-1024.
DR   PDB; 1JYW; X-ray; 1.55 A; A/B/C/D=10-1024.
DR   PDB; 1JYX; X-ray; 1.75 A; A/B/C/D=10-1024.
DR   PDB; 1JYY; X-ray; 2.70 A; A/B/C/D/E/F/G/H=2-1024.
DR   PDB; 1JYZ; X-ray; 2.70 A; I/J/K/L/M/N/O/P=2-1024.
DR   PDB; 1JZ0; X-ray; 2.60 A; A/B/C/D/E/F/G/H=2-1024.
DR   PDB; 1JZ1; X-ray; 2.60 A; I/J/K/L/M/N/O/P=2-1024.
DR   PDB; 1JZ2; X-ray; 2.10 A; A/B/C/D=2-1024.
DR   PDB; 1JZ3; X-ray; 1.75 A; A/B/C/D=10-1024.
DR   PDB; 1JZ4; X-ray; 2.10 A; A/B/C/D=10-1024.
DR   PDB; 1JZ5; X-ray; 1.80 A; A/B/C/D=10-1024.
DR   PDB; 1JZ6; X-ray; 2.10 A; A/B/C/D=10-1024.
DR   PDB; 1JZ7; X-ray; 1.50 A; A/B/C/D=10-1024.
DR   PDB; 1JZ8; X-ray; 1.50 A; A/B/C/D=10-1024.
DR   PDB; 1PX3; X-ray; 1.60 A; A/B/C/D=10-1024.
DR   PDB; 1PX4; X-ray; 1.60 A; A/B/C/D=10-1024.
DR   PDB; 3CZJ; X-ray; 2.05 A; A/B/C/D=10-1024.
DR   PDB; 3DYM; X-ray; 2.05 A; A/B/C/D=10-1024.
DR   PDB; 3DYO; X-ray; 1.80 A; A/B/C/D=10-1024.
DR   PDB; 3DYP; X-ray; 1.75 A; A/B/C/D=10-1024.
DR   PDB; 3E1F; X-ray; 3.00 A; 1/2/3/4=10-1024.
DR   PDB; 3I3B; X-ray; 2.20 A; A/B/C/D=10-1024.
DR   PDB; 3I3D; X-ray; 2.20 A; A/B/C/D=10-1024.
DR   PDB; 3I3E; X-ray; 2.10 A; A/B/C/D=10-1024.
DR   PDB; 3IAP; X-ray; 2.00 A; A/B/C/D=10-1024.
DR   PDB; 3IAQ; X-ray; 2.70 A; A/B/C/D=10-1024.
DR   PDB; 3MUY; X-ray; 2.50 A; 1/2/3/4=10-1024.
DR   PDB; 3MUZ; X-ray; 1.90 A; 1/2/3/4=10-1024.
DR   PDB; 3MV0; X-ray; 2.20 A; 1/2/3/4=10-1024.
DR   PDB; 3MV1; X-ray; 2.20 A; 1/2/3/4=10-1024.
DR   PDB; 3SEP; X-ray; 2.05 A; A/B/C/D=10-1024.
DR   PDB; 3T08; X-ray; 2.00 A; A/B/C/D=10-1024.
DR   PDB; 3T09; X-ray; 1.75 A; A/B/C/D=10-1024.
DR   PDB; 3T0A; X-ray; 1.90 A; A/B/C/D=10-1024.
DR   PDB; 3T0B; X-ray; 2.40 A; A/B/C/D=10-1024.
DR   PDB; 3T0D; X-ray; 1.93 A; A/B/C/D=10-1024.
DR   PDB; 3T2O; X-ray; 1.85 A; A/B/C/D=10-1024.
DR   PDB; 3T2P; X-ray; 2.60 A; A/B/C/D=10-1024.
DR   PDB; 3T2Q; X-ray; 2.40 A; A/B/C/D=10-1024.
DR   PDB; 3VD3; X-ray; 2.80 A; A/B/C/D=10-1024.
DR   PDB; 3VD4; X-ray; 2.00 A; A/B/C/D=10-1024.
DR   PDB; 3VD5; X-ray; 2.70 A; A/B/C/D=10-1024.
DR   PDB; 3VD7; X-ray; 2.87 A; A/B/C/D=10-1024.
DR   PDB; 3VD9; X-ray; 2.05 A; A/B/C/D=10-1024.
DR   PDB; 3VDA; X-ray; 2.50 A; A/B/C/D=10-1024.
DR   PDB; 3VDB; X-ray; 2.05 A; A/B/C/D=10-1024.
DR   PDB; 3VDC; X-ray; 2.55 A; A/B/C/D=10-1024.
DR   PDBsum; 1BGL; -.
DR   PDBsum; 1BGM; -.
DR   PDBsum; 1DP0; -.
DR   PDBsum; 1F49; -.
DR   PDBsum; 1F4A; -.
DR   PDBsum; 1F4H; -.
DR   PDBsum; 1GHO; -.
DR   PDBsum; 1HN1; -.
DR   PDBsum; 1JYN; -.
DR   PDBsum; 1JYV; -.
DR   PDBsum; 1JYW; -.
DR   PDBsum; 1JYX; -.
DR   PDBsum; 1JYY; -.
DR   PDBsum; 1JYZ; -.
DR   PDBsum; 1JZ0; -.
DR   PDBsum; 1JZ1; -.
DR   PDBsum; 1JZ2; -.
DR   PDBsum; 1JZ3; -.
DR   PDBsum; 1JZ4; -.
DR   PDBsum; 1JZ5; -.
DR   PDBsum; 1JZ6; -.
DR   PDBsum; 1JZ7; -.
DR   PDBsum; 1JZ8; -.
DR   PDBsum; 1PX3; -.
DR   PDBsum; 1PX4; -.
DR   PDBsum; 3CZJ; -.
DR   PDBsum; 3DYM; -.
DR   PDBsum; 3DYO; -.
DR   PDBsum; 3DYP; -.
DR   PDBsum; 3E1F; -.
DR   PDBsum; 3I3B; -.
DR   PDBsum; 3I3D; -.
DR   PDBsum; 3I3E; -.
DR   PDBsum; 3IAP; -.
DR   PDBsum; 3IAQ; -.
DR   PDBsum; 3MUY; -.
DR   PDBsum; 3MUZ; -.
DR   PDBsum; 3MV0; -.
DR   PDBsum; 3MV1; -.
DR   PDBsum; 3SEP; -.
DR   PDBsum; 3T08; -.
DR   PDBsum; 3T09; -.
DR   PDBsum; 3T0A; -.
DR   PDBsum; 3T0B; -.
DR   PDBsum; 3T0D; -.
DR   PDBsum; 3T2O; -.
DR   PDBsum; 3T2P; -.
DR   PDBsum; 3T2Q; -.
DR   PDBsum; 3VD3; -.
DR   PDBsum; 3VD4; -.
DR   PDBsum; 3VD5; -.
DR   PDBsum; 3VD7; -.
DR   PDBsum; 3VD9; -.
DR   PDBsum; 3VDA; -.
DR   PDBsum; 3VDB; -.
DR   PDBsum; 3VDC; -.
DR   ProteinModelPortal; P00722; -.
DR   SMR; P00722; 14-1024.
DR   IntAct; P00722; 76.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   ECO2DBASE; E123.0; 6TH EDITION.
DR   PRIDE; P00722; -.
DR   EnsemblBacteria; EBESCT00000001916; EBESCP00000001916; EBESCG00000001573.
DR   EnsemblBacteria; EBESCT00000001917; EBESCP00000001917; EBESCG00000001573.
DR   EnsemblBacteria; EBESCT00000001918; EBESCP00000001918; EBESCG00000001573.
DR   EnsemblBacteria; EBESCT00000001919; EBESCP00000001919; EBESCG00000001573.
DR   EnsemblBacteria; EBESCT00000016416; EBESCP00000015707; EBESCG00000015476.
DR   GeneID; 945006; -.
DR   GenomeReviews; AP009048_GR; JW0335.
DR   GenomeReviews; U00096_GR; b0344.
DR   KEGG; eco:b0344; -.
DR   PATRIC; 32115821; VBIEscCol129921_0352.
DR   EchoBASE; EB0522; -.
DR   EcoGene; EG10527; lacZ.
DR   HOGENOM; HOG000252443; -.
DR   KO; K01190; -.
DR   OMA; DFHVATH; -.
DR   ProtClustDB; PRK09525; -.
DR   BioCyc; EcoCyc:BETAGALACTOSID-MONOMER; -.
DR   BioCyc; MetaCyc:BETAGALACTOSID-MONOMER; -.
DR   DrugBank; DB01093; Dimethyl sulfoxide.
DR   EvolutionaryTrace; P00722; -.
DR   Genevestigator; P00722; -.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IDA:EcoCyc.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005990; P:lactose catabolic process; IMP:EcoCyc.
DR   Gene3D; G3DSA:2.60.40.320; Glyco_hydro_2/20_Ig-like; 2.
DR   Gene3D; G3DSA:2.70.98.10; Glyco_hydro_42_D5; 1.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   HAMAP; MF_01687; Beta_gal; 1; -.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR011013; Glyco_hydro-type_carb-bd.
DR   InterPro; IPR014718; Glyco_hydro-type_carb-bd_sub.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR013812; Glyco_hydro_2/20_Ig-like.
DR   InterPro; IPR023232; Glyco_hydro_2_AS.
DR   InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR006103; Glyco_hydro_2_TIM.
DR   InterPro; IPR013781; Glyco_hydro_catalytic_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF74650; Gal_mut_like; 1.
DR   SUPFAM; SSF49303; Glyco_hydro_2Ig; 2.
DR   SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Reference proteome; Sodium.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2   1024       Beta-galactosidase.
FT                                /FTId=PRO_0000057650.
FT   REGION      538    541       Substrate binding.
FT   ACT_SITE    462    462       Proton donor.
FT   ACT_SITE    538    538       Nucleophile.
FT   METAL       202    202       Sodium.
FT   METAL       417    417       Magnesium 1.
FT   METAL       419    419       Magnesium 1.
FT   METAL       462    462       Magnesium 1.
FT   METAL       598    598       Magnesium 2.
FT   METAL       602    602       Sodium; via carbonyl oxygen.
FT   METAL       605    605       Sodium.
FT   BINDING     103    103       Substrate.
FT   BINDING     202    202       Substrate.
FT   BINDING     462    462       Substrate.
FT   BINDING     605    605       Substrate.
FT   BINDING    1000   1000       Substrate.
FT   SITE        358    358       Transition state stabilizer.
FT   SITE        392    392       Transition state stabilizer.
FT   SITE       1000   1000       Important for ensuring that an
FT                                appropriate proportion of lactose is
FT                                converted to allolactose.
FT   MUTAGEN     202    202       D->E,N: Causes a significant decrease in
FT                                binding affinity in the absence of
FT                                monovalent cations or in the presence of
FT                                potassium ions, but only a moderate
FT                                decrease in the presence of sodium ions.
FT   MUTAGEN     202    202       D->F: Obliterates all binding and
FT                                catalysis.
FT   MUTAGEN     358    358       H->D,F,L,N: Less stable to heat than
FT                                wild-type. Causes significant
FT                                destabilizations of the first transition
FT                                state.
FT   MUTAGEN     392    392       H->E,F,K: Essentially inactive unless
FT                                very rapid purification. Causes very
FT                                large destabilizations of the transition
FT                                state.
FT   MUTAGEN     462    462       E->H: Slowly inactivates galactosidase
FT                                activity by reducing the binding of
FT                                magnesium. It increases binding
FT                                specificity.
FT   MUTAGEN     538    538       E->Q: 10000-fold decrease in the beta-
FT                                galactosidase activity.
FT   MUTAGEN     541    541       H->E,F,N: Poorly reactive with galactosyl
FT                                substrates. Less stable to heat than
FT                                wild-type.
FT   MUTAGEN     602    602       F->A: Decreases the stability of the loop
FT                                794-804.
FT   MUTAGEN     795    795       G->A: It forces the apoenzyme to adopt
FT                                the closed rather than the open
FT                                conformation. Reduces the binding
FT                                affinity.
FT   MUTAGEN     798    798       E->A,L: The catalytic efficiency is not
FT                                increased, when the sodium concentration
FT                                increases.
FT   MUTAGEN     798    798       E->D,Q: Small increase of the catalytic
FT                                efficiency, when the sodium concentration
FT                                increases.
FT   MUTAGEN    1000   1000       W->F,G,L,T: Decreases affinity for
FT                                substrate.
FT   HELIX        16     18
FT   STRAND       23     26
FT   STRAND       37     39
FT   HELIX        40     45
FT   STRAND       52     54
FT   STRAND       57     66
FT   HELIX        67     69
FT   HELIX        73     76
FT   STRAND       83     88
FT   HELIX        91     94
FT   STRAND      100    105
FT   STRAND      121    130
FT   HELIX       132    136
FT   STRAND      137    145
FT   STRAND      147    155
FT   STRAND      158    164
FT   STRAND      170    173
FT   TURN        175    177
FT   STRAND      180    192
FT   HELIX       194    198
FT   STRAND      202    205
FT   STRAND      213    218
FT   STRAND      220    232
FT   STRAND      236    249
FT   STRAND      255    263
FT   STRAND      266    275
FT   STRAND      289    298
FT   STRAND      304    307
FT   STRAND      310    318
FT   STRAND      323    331
FT   STRAND      336    339
FT   STRAND      342    345
FT   STRAND      352    356
FT   TURN        362    364
FT   HELIX       370    382
FT   STRAND      387    389
FT   HELIX       398    406
FT   STRAND      409    413
FT   STRAND      421    423
FT   TURN        424    429
FT   HELIX       431    433
FT   HELIX       434    448
FT   STRAND      454    458
FT   HELIX       467    479
FT   TURN        489    491
FT   STRAND      492    494
FT   STRAND      498    500
FT   STRAND      514    516
FT   HELIX       521    525
FT   STRAND      534    540
FT   HELIX       550    559
FT   STRAND      563    569
FT   STRAND      576    579
FT   STRAND      585    588
FT   TURN        590    593
FT   HELIX       600    603
FT   HELIX       617    624
FT   STRAND      627    633
FT   STRAND      636    641
FT   STRAND      652    659
FT   STRAND      662    670
FT   STRAND      678    682
FT   STRAND      690    703
FT   STRAND      708    710
FT   STRAND      714    726
FT   STRAND      740    743
FT   STRAND      745    752
FT   STRAND      755    760
FT   TURN        761    763
FT   STRAND      765    771
FT   STRAND      777    784
FT   HELIX       791    794
FT   HELIX       807    814
FT   TURN        815    818
FT   STRAND      820    830
FT   STRAND      832    845
FT   STRAND      848    860
FT   STRAND      865    873
FT   STRAND      881    890
FT   STRAND      894    904
FT   STRAND      915    922
FT   HELIX       923    926
FT   STRAND      939    947
FT   STRAND      950    963
FT   HELIX       965    970
FT   HELIX       974    976
FT   STRAND      981    991
FT   STRAND      999   1001
FT   HELIX      1006   1008
FT   STRAND     1013   1022
SQ   SEQUENCE   1024 AA;  116483 MW;  9D295EF4CEF90B08 CRC64;
     MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
     FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP
     TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA
     GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV
     LEAEVQMCGE LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK
     LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
     HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
     MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
     PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA
     HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
     QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD
     GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
     WRLAENLSVT LPAASHAIPH LTTSEMDFCI ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP
     LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA
     HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG
     LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI
     SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
     WCQK
//
ID   CNR1A_TAKRU             Reviewed;         468 AA.
AC   Q98894;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-MAY-2012, entry version 73.
DE   RecName: Full=Cannabinoid receptor type 1A;
GN   Name=cnr1a; Synonyms=cb1a;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=97001167; PubMed=8812500; DOI=10.1006/geno.1996.0406;
RA   Yamaguchi F., Macrae A., Brenner S.;
RT   "Molecular cloning of two cannabinoid type 1-like receptor genes from
RT   the puffer fish Fugu rubripes.";
RL   Genomics 35:603-605(1996).
CC   -!- FUNCTION: Involved in cannabinoid-induced CNS effects (Potential).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X94401; CAA64174.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q98894; -.
DR   eggNOG; NOG148018; -.
DR   InParanoid; Q98894; -.
DR   OrthoDB; EOG41ZF9S; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004949; F:cannabinoid receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR002230; Cnbnoid_rcpt.
DR   InterPro; IPR000810; Cnoid_rcpt_1.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   PANTHER; PTHR22750:SF10; Cnoid_rcpt_1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PIRSF; PIRSF037995; Cnoid_rcpt_1; 1.
DR   PRINTS; PR00522; CANABINOID1R.
DR   PRINTS; PR00362; CANNABINOIDR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    468       Cannabinoid receptor type 1A.
FT                                /FTId=PRO_0000069320.
FT   TOPO_DOM      1    115       Extracellular (Potential).
FT   TRANSMEM    116    141       Helical; Name=1; (Potential).
FT   TOPO_DOM    142    153       Cytoplasmic (Potential).
FT   TRANSMEM    154    174       Helical; Name=2; (Potential).
FT   TOPO_DOM    175    186       Extracellular (Potential).
FT   TRANSMEM    187    211       Helical; Name=3; (Potential).
FT   TOPO_DOM    212    231       Cytoplasmic (Potential).
FT   TRANSMEM    232    254       Helical; Name=4; (Potential).
FT   TOPO_DOM    255    272       Extracellular (Potential).
FT   TRANSMEM    273    298       Helical; Name=5; (Potential).
FT   TOPO_DOM    299    343       Cytoplasmic (Potential).
FT   TRANSMEM    344    364       Helical; Name=6; (Potential).
FT   TOPO_DOM    365    376       Extracellular (Potential).
FT   TRANSMEM    377    398       Helical; Name=7; (Potential).
FT   TOPO_DOM    399    468       Cytoplasmic (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     87     87       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   468 AA;  52391 MW;  B8628C1B043B42D7 CRC64;
     MKSVLDGVAD TTFRTITSGL QYLGSNDANY DDPLNDAAFK TGFSLQKPLS AFRSNSFPNK
     VPADEELIFK GIPFFPTNST DLFGNRNTTR DENSIQCGEN FMDMECFMIL TPSQQLAVAV
     LSLTLGTFTV LENLVVLCVI FQSRTLRCRP SYHFIGSLAV ADLLGSVIFV YSFLDFHVFH
     KKDSPNVFLF KLGGVTASFT ASVGSLFLTA IDRYISIHRP LAYRRIVTRT KAVIAFCMMW
     TISIIIAVLP LLGWNCKRLN SVCSDIFPLI DENYLMFWIG VTSVLVLFII YAYIYILWKA
     HHHAVRMLSR TSQKSLVVYS AEGTKVQTTR PEQTRMDIRL AKTLVLILAV LVICWGPLLA
     IMVYDLFWKM DDNIKTVFAF CSMLCLLNST VNPIIYALRS RDLRHAFLSS CHACRGSAQQ
     LDNSLESDCQ NRNVNISANR AAESCVKTTV KIAKVTMSVS TETSAEAV
//
ID   CNR1B_TAKRU             Reviewed;         470 AA.
AC   Q98895;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-MAY-2012, entry version 72.
DE   RecName: Full=Cannabinoid receptor type 1B;
GN   Name=cnr1b; Synonyms=cb1b;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=97001167; PubMed=8812500; DOI=10.1006/geno.1996.0406;
RA   Yamaguchi F., Macrae A., Brenner S.;
RT   "Molecular cloning of two cannabinoid type 1-like receptor genes from
RT   the puffer fish Fugu rubripes.";
RL   Genomics 35:603-605(1996).
CC   -!- FUNCTION: Involved in cannabinoid-induced CNS effects (Potential).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X94402; CAA64175.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q98895; -.
DR   eggNOG; NOG308746; -.
DR   InParanoid; Q98895; -.
DR   OrthoDB; EOG4J3WH0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004949; F:cannabinoid receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR002230; Cnbnoid_rcpt.
DR   InterPro; IPR000810; Cnoid_rcpt_1.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   PANTHER; PTHR22750:SF10; Cnoid_rcpt_1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PIRSF; PIRSF037995; Cnoid_rcpt_1; 1.
DR   PRINTS; PR00522; CANABINOID1R.
DR   PRINTS; PR00362; CANNABINOIDR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    470       Cannabinoid receptor type 1B.
FT                                /FTId=PRO_0000069321.
FT   TOPO_DOM      1    113       Extracellular (Potential).
FT   TRANSMEM    114    139       Helical; Name=1; (Potential).
FT   TOPO_DOM    140    151       Cytoplasmic (Potential).
FT   TRANSMEM    152    172       Helical; Name=2; (Potential).
FT   TOPO_DOM    173    184       Extracellular (Potential).
FT   TRANSMEM    185    209       Helical; Name=3; (Potential).
FT   TOPO_DOM    210    229       Cytoplasmic (Potential).
FT   TRANSMEM    230    252       Helical; Name=4; (Potential).
FT   TOPO_DOM    253    270       Extracellular (Potential).
FT   TRANSMEM    271    296       Helical; Name=5; (Potential).
FT   TOPO_DOM    297    341       Cytoplasmic (Potential).
FT   TRANSMEM    342    362       Helical; Name=6; (Potential).
FT   TOPO_DOM    363    374       Extracellular (Potential).
FT   TRANSMEM    375    396       Helical; Name=7; (Potential).
FT   TOPO_DOM    397    470       Cytoplasmic (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   470 AA;  52081 MW;  CEE87CD37FDF9192 CRC64;
     MKLALHRIAG ATMAALTTEV QYLGSNDASY EDPQADAALM KSRFNFEKPY SASSSLHRLI
     PGNKELIYGG LSTILPTNAS DFPLSNGSGE ATQCGEDIVD NMECFMILTP AQQLVIVILA
     ITLGTFTVLE NFVVLCVILH SHTLRSRPSY HFIGSLAVAD LIGSIIFVYS FLDFHVLHRK
     DSPSIFLFKL AGVIASFTAS VGSLFLTAID RYVSIHRPMA YKRIITKTKA VIAFSVMWAI
     SIEFSLLPLL GWNCKRLHSV CSDIFPLIDE KYLMFWIGMT TVLLLFIIYA YMFILWKSHH
     HAVRMLSRSS QRSIIVYTSE GTKVQTVRPE QARMDLRLAK TLVLILVALI ICWGPLLAIM
     VYDLFGRVND FIKTVFAFCS MLCLLNSTIN PVIYAMRSKD LRRAFVNICH MCRGTTQSLD
     SSAESDWNSR SVRSTGGRAG KDRSVGGKPQ VKVAQVTVSG VTASSPAEAV
//
ID   CO9_TAKRU               Reviewed;         586 AA.
AC   P79755;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   16-MAY-2012, entry version 77.
DE   RecName: Full=Complement component C9;
DE   Flags: Precursor;
GN   Name=c9;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98038993; PubMed=9373156; DOI=10.1016/S0378-1119(97)00423-X;
RA   Yeo G.S.H., Elgar G., Sandford R., Brenner S.;
RT   "Cloning and sequencing of complement component C9 and its linkage to
RT   DOC-2 in the pufferfish Fugu rubripes.";
RL   Gene 200:203-211(1997).
CC   -!- FUNCTION: C9 is the final component of the complement system to be
CC       added in the assembly of the membrane attack complex. It is able
CC       to enter lipid bilayers, forming transmembrane channels (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted. Cell membrane; Multi-pass membrane
CC       protein (By similarity). Note=Secreted as soluble monomer.
CC       Oligomerizes at target membranes, forming a pre-pore. A
CC       conformation change then leads to the formation of a pore (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 LDL-receptor class A domain.
CC   -!- SIMILARITY: Contains 1 MACPF domain.
CC   -!- SIMILARITY: Contains 2 TSP type-1 domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U87241; AAC60288.1; -; Genomic_DNA.
DR   ProteinModelPortal; P79755; -.
DR   TCDB; 1.C.39.1.2; membrane attack complex/perforin (MACPF) family.
DR   eggNOG; NOG46204; -.
DR   InParanoid; P79755; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005579; C:membrane attack complex; IEA:UniProtKB-KW.
DR   GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 1.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR001862; MAC_perforin.
DR   InterPro; IPR020864; MACPF.
DR   InterPro; IPR020863; MACPF_CS.
DR   InterPro; IPR000884; Thrombospondin_1_rpt.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   PRINTS; PR00764; COMPLEMENTC9.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00209; TSP1; 1.
DR   SUPFAM; SSF57424; LDL_rcpt_classA_cys-rich; 1.
DR   SUPFAM; SSF82895; TSP1; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS00279; MACPF_1; 1.
DR   PROSITE; PS51412; MACPF_2; 1.
DR   PROSITE; PS50092; TSP1; 2.
PE   3: Inferred from homology;
KW   Cell membrane; Complement alternate pathway; Complement pathway;
KW   Complete proteome; Cytolysis; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Immunity; Innate immunity; Membrane;
KW   Membrane attack complex; Reference proteome; Repeat; Secreted; Signal;
KW   Transmembrane; Transmembrane beta strand.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    586       Complement component C9.
FT                                /FTId=PRO_0000023608.
FT   DOMAIN       36     89       TSP type-1 1.
FT   DOMAIN       94    131       LDL-receptor class A.
FT   DOMAIN      132    493       MACPF.
FT   DOMAIN      494    524       EGF-like.
FT   DOMAIN      543    585       TSP type-1 2.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    274    274       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    354    354       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    545    545       N-linked (GlcNAc...) (Potential).
FT   DISULFID     37     72       By similarity.
FT   DISULFID     48     51       By similarity.
FT   DISULFID     82     88       By similarity.
FT   DISULFID     96    108       By similarity.
FT   DISULFID    103    121       By similarity.
FT   DISULFID    115    129       By similarity.
FT   DISULFID    136    175       By similarity.
FT   DISULFID    363    389       By similarity.
FT   DISULFID    494    510       By similarity.
FT   DISULFID    497    512       By similarity.
FT   DISULFID    514    523       By similarity.
SQ   SEQUENCE   586 AA;  65198 MW;  8466EB7B8B8FDC18 CRC64;
     MRTEAALQLG FCALCVMLAL LGEGMGRELP DPPAVNCVWS RWAPWSSCDP CTNTRRRSRG
     VEVFGQFAGI ACQGSVGDRE YCITNAKCNL PPPRECSDSE FQCESGSCIK LRLKCNGDYD
     CEDGSDEDCE PLRKTCPPTV LDTNEQGRTA GYGINILGAD PRMNPFNNDF FNGRCDKVRN
     PNTLQLDRLP WNIGVLNYQT LVEETASREI YEDSYSLLRE MLKEMSIKVD AGLSFKFKST
     EPSMSNNSLK LDASLEYEKK TMIKDVSELT NIKNKSFMRV KGRLQLSTYR MRSHQLQVAD
     EFVAHVKSLP LEYEKGIYYA FLEDYGTHYT KNGKSGGEYE LVYVLNQDTI KAKNLTERKI
     QECLKIGIEA EFATTSVQDG KAHAKLNKCD DVTTKSQGDV EGKAVVDNVM TSVKGGSLES
     AVTMRAKLNK EGVMDIATYQ NWARTIASAP ALINSEPEPI YMLIPTDIPG ANSRIANLKQ
     ATADYVAEYN VCKCRPCHNG GTLALLDGKC ICMCSNLFEG LGCQNFKGDK ARVPAARPAV
     TQEGNWSCWS SWSNCQGQKR SRTRYCNTEG VLGAECRGEI RSEEYC
//
ID   DRD1L_TAKRU             Reviewed;         459 AA.
AC   P53452;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 70.
DE   RecName: Full=D(1)-like dopamine receptor;
GN   Name=d14;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M;
RA   Machae A.D., Brenner S.;
RT   "Analysis of the dopamine receptor family in the compact genome of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 25:436-446(1995).
CC   -!- FUNCTION: Receptor for dopamine.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80174; CAA56455.1; -; Genomic_DNA.
DR   PIR; A56849; A56849.
DR   ProteinModelPortal; P53452; -.
DR   eggNOG; NOG262978; -.
DR   InParanoid; P53452; -.
DR   OrthoDB; EOG4BG8W3; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004952; F:dopamine receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001413; Dopa_1A_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00565; DOPAMINED1AR.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    459       D(1)-like dopamine receptor.
FT                                /FTId=PRO_0000069382.
FT   TOPO_DOM      1     23       Extracellular (Potential).
FT   TRANSMEM     24     49       Helical; Name=1; (Potential).
FT   TOPO_DOM     50     60       Cytoplasmic (Potential).
FT   TRANSMEM     61     87       Helical; Name=2; (Potential).
FT   TOPO_DOM     88     96       Extracellular (Potential).
FT   TRANSMEM     97    119       Helical; Name=3; (Potential).
FT   TOPO_DOM    120    138       Cytoplasmic (Potential).
FT   TRANSMEM    139    164       Helical; Name=4; (Potential).
FT   TOPO_DOM    165    191       Extracellular (Potential).
FT   TRANSMEM    192    216       Helical; Name=5; (Potential).
FT   TOPO_DOM    217    269       Cytoplasmic (Potential).
FT   TRANSMEM    270    297       Helical; Name=6; (Potential).
FT   TOPO_DOM    298    311       Extracellular (Potential).
FT   TRANSMEM    312    333       Helical; Name=7; (Potential).
FT   TOPO_DOM    334    459       Cytoplasmic (Potential).
FT   CARBOHYD      4      4       N-linked (GlcNAc...) (Potential).
FT   DISULFID     96    187       By similarity.
SQ   SEQUENCE   459 AA;  51080 MW;  B69857A3A4E4E10B CRC64;
     MAQNFSTVGD GKQMLLERDS SKRVLTGCFL SLLIFTTLLG NTLVCVAVTK FRHLRSKVTN
     FFVISLAISD LLVAILVMPW KAATEIMGFW PFGEFCNIWV AFDIMCSTAS ILNLCVISVD
     RYWAISSPFR YERKMTPKVA CLMISVAWTL SVLISFIPVQ LNWHKAQTAS YVELNGTYAG
     DLPPDNCDSS LNRTYAISSS LISFYIPVAI MIVTYTRIYR IAQKQIRRIS ALERAAESAQ
     NRHSSMGNSL SMESECSFKM SFKRETKVLK TLSVIMGVFV CCWLPFFILN CMVPFCEADD
     TTDFPCISST TFDVFVWFGW ANSSLNPIIY AFNADFRKAF SILLGCHRLC PGNSAIEIVS
     INNTGAPLSN PSCQYQPKSH IPKEGNHSSS YVIPHSILCQ EEELQKKDGF GGEMEVGLVN
     NAMEKVSPAI SGNFDSDAAV TLETINPITQ NGQHKSMSC
//
ID   DRD2L_TAKRU             Reviewed;         463 AA.
AC   P53453;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 68.
DE   RecName: Full=D(2)-like dopamine receptor;
GN   Name=d215;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M;
RA   Machae A.D., Brenner S.;
RT   "Analysis of the dopamine receptor family in the compact genome of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 25:436-446(1995).
CC   -!- FUNCTION: Receptor for dopamine.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80175; CAA56456.1; -; Genomic_DNA.
DR   ProteinModelPortal; P53453; -.
DR   eggNOG; NOG309657; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004952; F:dopamine receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001922; Dopa_D2_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00567; DOPAMINED2R.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    463       D(2)-like dopamine receptor.
FT                                /FTId=PRO_0000069392.
FT   TOPO_DOM      1     35       Extracellular (By similarity).
FT   TRANSMEM     36     58       Helical; Name=1; (By similarity).
FT   TOPO_DOM     59     68       Cytoplasmic (By similarity).
FT   TRANSMEM     69     91       Helical; Name=2; (By similarity).
FT   TOPO_DOM     92    106       Extracellular (By similarity).
FT   TRANSMEM    107    128       Helical; Name=3; (By similarity).
FT   TOPO_DOM    129    149       Cytoplasmic (By similarity).
FT   TRANSMEM    150    170       Helical; Name=4; (By similarity).
FT   TOPO_DOM    171    189       Extracellular (By similarity).
FT   TRANSMEM    190    214       Helical; Name=5; (By similarity).
FT   TOPO_DOM    215    392       Cytoplasmic (By similarity).
FT   TRANSMEM    393    414       Helical; Name=6; (By similarity).
FT   TOPO_DOM    415    429       Extracellular (By similarity).
FT   TRANSMEM    430    451       Helical; Name=7; (By similarity).
FT   TOPO_DOM    452    463       Cytoplasmic (By similarity).
FT   REGION      191    198       Agonist binding (By similarity).
FT   REGION      405    413       Agonist binding (By similarity).
FT   BINDING     112    112       Agonist (By similarity).
FT   CARBOHYD     10     10       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     16     16       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     22     22       N-linked (GlcNAc...) (Potential).
FT   DISULFID    105    183       By similarity.
FT   DISULFID    418    421       By similarity.
SQ   SEQUENCE   463 AA;  52120 MW;  A54B178D7718AF6B CRC64;
     MDVFTQYAYN DSIFDNGTWS ANETTKDETH PYNYYAMLLT LLIFVIVFGN VLVCMAVSRE
     KALQTTTNYL IVSLAVADLL VATLVMPWVV YLEVVGEWRF SKIHCDIFVT LDVMMCTASI
     LNLCAISIDR YTAVAMPMLY NTRYSSRRRV TVMISVVWVL SFAISCPLLF GLNNTATRDQ
     SLCFIANPAF VVYSSIVSFY VPFIVTLLVY VQIYVVLRKR RKRVNTKPKQ RLCQAADPDI
     PTSLKDKCTH PEDVRLCTMI VKSNGSFPVN KKKVIFIKDG VNEVEGLELD ELNYCGGSHK
     QPPPQQQPRA LGDTPATSHQ LLMSTKANAS PTSTPPTPPE EGQRTEKNGD PTKEAQGNPA
     PVVALRNGKT QTSLKTLSKR KISQQKEKKA TQMLAIVLGV FIICWLPFFI THILNTHCTR
     CKVPAEMYNA FTWLGYVNSA VNPIIYTTFN VEFRKAFIKI LHC
//
ID   DRD5L_TAKRU             Reviewed;         463 AA.
AC   P53454;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 70.
DE   RecName: Full=D(5)-like dopamine receptor;
GN   Name=dl;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M;
RA   Machae A.D., Brenner S.;
RT   "Analysis of the dopamine receptor family in the compact genome of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 25:436-446(1995).
CC   -!- FUNCTION: Receptor for dopamine.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80177; CAA56457.1; -; Genomic_DNA.
DR   PIR; B56849; B56849.
DR   ProteinModelPortal; P53454; -.
DR   eggNOG; NOG262978; -.
DR   InParanoid; P53454; -.
DR   OrthoDB; EOG4PVNZH; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004952; F:dopamine receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    463       D(5)-like dopamine receptor.
FT                                /FTId=PRO_0000069409.
FT   TOPO_DOM      1     39       Extracellular (Potential).
FT   TRANSMEM     40     65       Helical; Name=1; (Potential).
FT   TOPO_DOM     66     76       Cytoplasmic (Potential).
FT   TRANSMEM     77    103       Helical; Name=2; (Potential).
FT   TOPO_DOM    104    112       Extracellular (Potential).
FT   TRANSMEM    113    135       Helical; Name=3; (Potential).
FT   TOPO_DOM    136    154       Cytoplasmic (Potential).
FT   TRANSMEM    155    180       Helical; Name=4; (Potential).
FT   TOPO_DOM    181    198       Extracellular (Potential).
FT   TRANSMEM    199    223       Helical; Name=5; (Potential).
FT   TOPO_DOM    224    273       Cytoplasmic (Potential).
FT   TRANSMEM    274    301       Helical; Name=6; (Potential).
FT   TOPO_DOM    302    315       Extracellular (Potential).
FT   TRANSMEM    316    337       Helical; Name=7; (Potential).
FT   TOPO_DOM    338    463       Cytoplasmic (Potential).
FT   CARBOHYD      6      6       N-linked (GlcNAc...) (Potential).
FT   DISULFID    112    194       By similarity.
SQ   SEQUENCE   463 AA;  51096 MW;  7FD627F69A699F6B CRC64;
     MENFYNETEP TEPRGGVDPL RVVTAAEDVP APVGGVSVRA LTGCVLCALI VSTLLGNTLV
     CAAVIKFRHL RSKVTNAFVV SLAVSDLFVA VLVMPWRAVS EVAGVWLFGR FCDTWVAFDI
     MCSTASILNL CVISMDRYWA ISNPFRYERR MTRRFAFLMI AVAWTLSVLI SFIPVQLNWH
     RADNNSSAHE QGDCNASLNR TYAISSSLIS FYIPVLIMVG TYTRIFRIAQ TQIRRISSLE
     RAAGQRAQNQ SHRASTHDES ALKTSFKRET KVLKTLSVIM GVFVFCWLPF FVLNCVVPFC
     DVDKVGEPPC VSDTTFNIFV WFGWANSSLN PVIYAFNADF RKAFTTILGC SKFCSSSAVQ
     AVDFSNELVS YHHDTTLQKE PVPGPGAHRL VAPLPQNRGD AGPNFDKVSV VSDDSRADRN
     LLLPAILQCD CEAEISLDMV PFGSSGPADS FLIPGQIQDL GDL
//
ID   EI2BB_TAKRU             Reviewed;         355 AA.
AC   Q90511;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-MAY-2012, entry version 58.
DE   RecName: Full=Translation initiation factor eIF-2B subunit beta;
DE   AltName: Full=S20I15;
DE   AltName: Full=eIF-2B GDP-GTP exchange factor subunit beta;
GN   Name=eif2b2; Synonyms=eif2bb;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96202283; PubMed=8643637; DOI=10.1073/pnas.93.4.1366;
RA   Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J.,
RA   Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R.,
RA   Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.;
RT   "Conservation of synteny between the genome of the pufferfish (Fugu
RT   rubripes) and the region on human chromosome 14 (14q24.3) associated
RT   with familial Alzheimer disease (AD3 locus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996).
CC   -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor
CC       2-bound GDP for GTP (By similarity).
CC   -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma,
CC       delta and epsilon (By similarity).
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits
CC       family.
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DR   EMBL; U40756; AAC59777.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q90511; -.
DR   STRING; Q90511; -.
DR   Ensembl; ENSTRUT00000027526; ENSTRUP00000027417; ENSTRUG00000010849.
DR   eggNOG; COG1184; -.
DR   GeneTree; ENSGT00550000074908; -.
DR   InParanoid; Q90511; -.
DR   OMA; RRSSEDM; -.
DR   OrthoDB; EOG4JT05R; -.
DR   GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:RefGenome.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:RefGenome.
DR   GO; GO:0051716; P:cellular response to stimulus; ISS:UniProtKB.
DR   GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR   GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; ISS:RefGenome.
DR   InterPro; IPR000649; IF-2B-related.
DR   PANTHER; PTHR10233; IF-2B_related; 1.
DR   Pfam; PF01008; IF-2B; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Initiation factor; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    355       Translation initiation factor eIF-2B
FT                                subunit beta.
FT                                /FTId=PRO_0000156065.
SQ   SEQUENCE   355 AA;  39130 MW;  4375743877F6B132 CRC64;
     MPGADKEVDL TERIEAFLSD LKRGGSGTGP LRGSSETARE TTALLRRITA QARWSSAGDL
     MEIIRKEGRR LIAAQPSETT VGNMIRRVLK IIREEYARSR GSSEEADQQE SLHKLLTSGG
     LSEENFRQHF AALRANVIEA INELLTELEG TTDNIAMQAL EHIHSNEVIM TVGRSRTVEA
     FLKDAARKRK FHVIVAECAP FCQGHKMATS LSTAGIETTV IADAAIFAVM SRVNKVIIGT
     QTVLANGGLR AVNGTHTLAL AAKHHSTPLI VCAPMFKLSP QFPNEEDTFH KFVSPHEVLP
     FTEGEILSKV NVHCPVFDYV PPELITLFIS NIGGHAPSYI YRLMSELYHP EDHEL
//
ID   EM55_TAKRU              Reviewed;         467 AA.
AC   P49697;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-MAY-2012, entry version 75.
DE   RecName: Full=55 kDa erythrocyte membrane protein;
DE            Short=p55;
DE   AltName: Full=Membrane protein, palmitoylated 1;
GN   Name=mpp1;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=96047329; PubMed=7558025; DOI=10.1006/geno.1995.1075;
RA   Elgar G.S., Rattray F.M., Greystrong J.S., Brenner S.;
RT   "Genomic structure and nucleotide sequence of the p55 gene of the
RT   puffer fish Fugu rubripes.";
RL   Genomics 27:442-446(1995).
CC   -!- FUNCTION: May play a role in the regulation of neutrophil
CC       polarization (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- PTM: Extensively palmitoylated (By similarity).
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; X81359; CAA57127.1; -; Genomic_DNA.
DR   PIR; A57627; A57627.
DR   ProteinModelPortal; P49697; -.
DR   SMR; P49697; 71-155.
DR   eggNOG; COG0194; -.
DR   InParanoid; P49697; -.
DR   OrthoDB; EOG46HG9K; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; SH3 domain.
FT   CHAIN         1    467       55 kDa erythrocyte membrane protein.
FT                                /FTId=PRO_0000094567.
FT   DOMAIN       73    154       PDZ.
FT   DOMAIN      160    230       SH3.
FT   DOMAIN      283    452       Guanylate kinase-like.
SQ   SEQUENCE   467 AA;  52609 MW;  48BA1CE3ED524EDC CRC64;
     MTLKSNKNEP ALILDSVTSV RTALSDLYLE QLLQNKPTDK QAAMQTYENK GAEVFSNGSA
     GHINGAELSR MREVAFEKNQ SEPLGVTLKL NDKQRCSVAR ILHGGMIHRQ GSLHEGDEIA
     EINGKSVANQ TVDQLQKILK ETNGVVTMKI IPRPQSRSKP CEMYMRGQFD YDPAMDDLIP
     CKEAGLKFQT GDIIQIINKQ DPNWWQGRVE NNAANFAGLI PSPELQEWRA ASKSKAREGS
     QSCSPFGKKK KCKDKYLAKH SSIFDQLDVI SYEEVVRLPA FKRKTLVLIG APGVGRRHIK
     NVLLTKYPEK FSYPVPHTTR PQRKGDANGE EYFFISNEAM TKCISANELL EYGSFQGYMF
     GTITETIQKI HEQDKIALLD VEPQTMKVLR TADFGPLMVF IAPTDTAAQT ENLQMIQKES
     ETILNTYRQY FDVVLVNNDV NESVKIVEEA LEHATTTPQW VPVSWVY
//
ID   FLAV_ANASO              Reviewed;         170 AA.
AC   P0A3E0; P11241;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   18-APR-2012, entry version 40.
DE   RecName: Full=Flavodoxin;
GN   Name=isiB;
OS   Anabaena sp. (strain PCC 7119).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=1168;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92074973; PubMed=1720613;
RA   Fillat M.F., Borrias W.E., Weisbeek P.J.;
RT   "Isolation and overexpression in Escherichia coli of the flavodoxin
RT   gene from Anabaena PCC 7119.";
RL   Biochem. J. 280:187-191(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-37.
RX   MEDLINE=90381288; PubMed=2119231; DOI=10.1016/0167-4838(90)90091-S;
RA   Fillat M.F., Edmondson D.E., Gomez-Moreno C.;
RT   "Structural and chemical properties of a flavodoxin from Anabaena PCC
RT   7119.";
RL   Biochim. Biophys. Acta 1040:301-307(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=99318886; PubMed=10388575; DOI=10.1006/jmbi.1999.2863;
RA   Fernandez-Recio J., Romero A., Sancho J.;
RT   "Energetics of a hydrogen bond (charged and neutral) and of a cation-
RT   pi interaction in apoflavodoxin.";
RL   J. Mol. Biol. 290:319-330(1999).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- INTERACTION:
CC       P08165:FDXR (xeno); NbExp=3; IntAct=EBI-593907, EBI-593948;
CC       P21890:petH; NbExp=5; IntAct=EBI-593907, EBI-593915;
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; S68006; AAB20462.1; -; Genomic_DNA.
DR   PDB; 1DX9; X-ray; 2.05 A; A/B/C/D=2-170.
DR   PDB; 1FTG; X-ray; 2.00 A; A=3-169.
DR   PDB; 1OBO; X-ray; 1.20 A; A/B=3-170.
DR   PDB; 1OBV; X-ray; 2.10 A; A=3-170.
DR   PDB; 1QHE; X-ray; 2.00 A; A=3-170.
DR   PDB; 2KQU; NMR; -; A=3-170.
DR   PDB; 2V5U; X-ray; 1.99 A; A/B=3-169.
DR   PDB; 2V5V; X-ray; 1.88 A; A/B=3-170.
DR   PDB; 3ESX; X-ray; 2.31 A; A/B=2-170.
DR   PDB; 3ESY; X-ray; 2.39 A; A/B/C/D=2-170.
DR   PDB; 3ESZ; X-ray; 1.94 A; A/B=5-170.
DR   PDBsum; 1DX9; -.
DR   PDBsum; 1FTG; -.
DR   PDBsum; 1OBO; -.
DR   PDBsum; 1OBV; -.
DR   PDBsum; 1QHE; -.
DR   PDBsum; 2KQU; -.
DR   PDBsum; 2V5U; -.
DR   PDBsum; 2V5V; -.
DR   PDBsum; 3ESX; -.
DR   PDBsum; 3ESY; -.
DR   PDBsum; 3ESZ; -.
DR   ProteinModelPortal; P0A3E0; -.
DR   SMR; P0A3E0; 2-170.
DR   IntAct; P0A3E0; 3.
DR   EvolutionaryTrace; P0A3E0; -.
DR   GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB.
DR   GO; GO:0010181; F:FMN binding; TAS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0010106; P:cellular response to iron ion starvation; TAS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    170       Flavodoxin.
FT                                /FTId=PRO_0000171600.
FT   DOMAIN        5    165       Flavodoxin-like.
FT   STRAND        4      9
FT   STRAND       12     14
FT   HELIX        15     27
FT   TURN         29     31
FT   STRAND       32     36
FT   TURN         37     39
FT   HELIX        42     47
FT   STRAND       49     58
FT   TURN         59     61
FT   HELIX        65     71
FT   HELIX        72     76
FT   STRAND       83     89
FT   TURN         92     97
FT   HELIX       101    112
FT   STRAND      138    144
FT   TURN        146    148
FT   HELIX       150    152
FT   HELIX       153    168
SQ   SEQUENCE   170 AA;  18964 MW;  069E8DEBA9E33302 CRC64;
     MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI
     GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY
     WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL
//
ID   FLAV_NOSS1              Reviewed;         170 AA.
AC   P0A3D9; P11241;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 55.
DE   RecName: Full=Flavodoxin;
GN   Name=isiB; OrderedLocusNames=alr2405;
OS   Nostoc sp. (strain PCC 7120 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89296496; PubMed=2500643; DOI=10.1093/nar/17.11.4384;
RA   Leonhardt K.G., Straus N.A.;
RT   "Sequence of the flavodoxin gene from Anabaena variabilis 7120.";
RL   Nucleic Acids Res. 17:4384-4384(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / UTEX 2576;
RX   MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
RN   [3]
RP   STRUCTURE BY NMR.
RX   MEDLINE=91104858; PubMed=2125478; DOI=10.1021/bi00493a014;
RA   Stockman B.J., Krezel A.M., Markley J.L., Leonhardt K.G., Straus N.A.;
RT   "Hydrogen-1, carbon-13, and nitrogen-15 NMR spectroscopy of Anabaena
RT   7120 flavodoxin: assignment of beta-sheet and flavin binding site
RT   resonances and analysis of protein-flavin interactions.";
RL   Biochemistry 29:9600-9609(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=93271891; PubMed=1303762;
RA   Rao S.T., Shaffie F., Yu C., Satyshur K.A., Stockman B.J.,
RA   Markley J.L., Sundaralingam M.;
RT   "Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at
RT   2-A resolution.";
RL   Protein Sci. 1:1413-1427(1992).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX   PubMed=15299298; DOI=10.1107/S0907444994011716;
RA   Burkhart B.M., Ramakrishnan B., Yan H., Reedstrom R.J., Markley J.L.,
RA   Straus N.A., Sundaralingam M.;
RT   "Structure of the trigonal form of recombinant oxidized flavodoxin
RT   from Anabaena 7120 at 1.40-A resolution.";
RL   Acta Crystallogr. D 51:318-330(1995).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; X14577; CAA32720.1; -; Genomic_DNA.
DR   EMBL; BA000019; BAB74104.1; -; Genomic_DNA.
DR   PIR; AF2106; AF2106.
DR   RefSeq; NP_486445.1; NC_003272.1.
DR   PDB; 1FLV; X-ray; 2.00 A; A=2-170.
DR   PDB; 1RCF; X-ray; 1.40 A; A=2-170.
DR   PDBsum; 1FLV; -.
DR   PDBsum; 1RCF; -.
DR   ProteinModelPortal; P0A3D9; -.
DR   SMR; P0A3D9; 2-170.
DR   STRING; P0A3D9; -.
DR   GeneID; 1106002; -.
DR   GenomeReviews; BA000019_GR; alr2405.
DR   KEGG; ana:alr2405; -.
DR   PATRIC; 22774998; VBINosSp37423_2965.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   OMA; DDKHFVG; -.
DR   ProtClustDB; PRK09267; -.
DR   BioCyc; NSP103690:ALR2405-MONOMER; -.
DR   EvolutionaryTrace; P0A3D9; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Electron transport; Flavoprotein;
KW   FMN; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    170       Flavodoxin.
FT                                /FTId=PRO_0000171601.
FT   DOMAIN        5    165       Flavodoxin-like.
FT   STRAND        5      9
FT   STRAND       12     14
FT   HELIX        15     26
FT   TURN         27     29
FT   STRAND       32     36
FT   HELIX        42     47
FT   STRAND       49     54
FT   TURN         59     61
FT   HELIX        65     71
FT   HELIX        72     76
FT   STRAND       83     89
FT   TURN         92     97
FT   HELIX       101    112
FT   STRAND      138    144
FT   TURN        146    148
FT   HELIX       150    152
FT   HELIX       153    167
SQ   SEQUENCE   170 AA;  18964 MW;  069E8DEBA9E33302 CRC64;
     MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI
     GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY
     WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL
//
ID   FLAV_AQUAE              Reviewed;         185 AA.
AC   O67866;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-MAY-2012, entry version 71.
DE   RecName: Full=Flavodoxin;
GN   Name=fldA; Synonyms=floX; OrderedLocusNames=aq_2096;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AE000657; AAC07825.1; -; Genomic_DNA.
DR   PIR; F70479; F70479.
DR   RefSeq; NP_214435.1; NC_000918.1.
DR   PDB; 2ARK; X-ray; 2.40 A; A/B/C/D/E/F=1-185.
DR   PDBsum; 2ARK; -.
DR   ProteinModelPortal; O67866; -.
DR   SMR; O67866; 1-185.
DR   GeneID; 1193855; -.
DR   GenomeReviews; AE000657_GR; aq_2096.
DR   KEGG; aae:aq_2096; -.
DR   PATRIC; 20961048; VBIAquAeo85532_1617.
DR   eggNOG; COG0655; -.
DR   HOGENOM; HOG000030539; -.
DR   OMA; WEEGSLA; -.
DR   ProtClustDB; CLSK230748; -.
DR   BioCyc; AAEO224324:AQ_2096-MONOMER; -.
DR   EvolutionaryTrace; O67866; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Electron transport; Flavoprotein;
KW   FMN; Reference proteome; Transport.
FT   CHAIN         1    185       Flavodoxin.
FT                                /FTId=PRO_0000171602.
FT   DOMAIN        4    159       Flavodoxin-like.
FT   STRAND        2      8
FT   STRAND       11     13
FT   HELIX        14     27
FT   STRAND       32     38
FT   TURN         39     41
FT   HELIX        44     49
FT   STRAND       51     58
FT   HELIX        66     74
FT   HELIX        76     78
FT   TURN         79     81
FT   STRAND       87     97
FT   HELIX       101    114
FT   STRAND      122    127
FT   STRAND      130    141
FT   HELIX       145    165
FT   HELIX       172    178
FT   HELIX       180    182
SQ   SEQUENCE   185 AA;  20444 MW;  7C138666D5B89281 CRC64;
     MGKVLVIYDT RTGNTKKMAE LVAEGARSLE GTEVRLKHVD EATKEDVLWA DGLAVGSPTN
     MGLVSWKMKR FFDDVLGDLW GEIDGKIACA FSSSGGWGGG NEVACMSILT MLMNFGFLVF
     GVTDYVGKKF TLHYGAVVAG EPRSEEEKEA CRRLGRRLAE WVAIFVDGRK ELLEKIRKDP
     ARFVD
//
ID   FLAV_AZOCH              Reviewed;         180 AA.
AC   P23001; P35708;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   31-MAY-2011, entry version 62.
DE   RecName: Full=Flavodoxin-B;
DE            Short=FldB;
GN   Name=nifF;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8765738; DOI=10.1007/BF00200433;
RA   Peelen S., Wijmenga S., Erbel P.J., Robson R.L., Eady R.R.,
RA   Vervoort J.;
RT   "Possible role of a short extra loop of the long-chain flavodoxin from
RT   Azotobacter chroococcum in electron transfer to nitrogenase: complete
RT   1H, 15N and 13C backbone assignments and secondary solution structure
RT   of the flavodoxin.";
RL   J. Biomol. NMR 7:315-330(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=MCD 1155;
RX   MEDLINE=91315397; PubMed=1859358;
RA   Bagby S., Barker P.D., Hill H.A.O., Sanghera G.S., Dunbar B.,
RA   Ashby G.A., Eady R.R., Thorneley R.N.F.;
RT   "Direct electrochemistry of two genetically distinct flavodoxins
RT   isolated from Azotobacter chroococcum grown under nitrogen-fixing
RT   conditions.";
RL   Biochem. J. 277:313-319(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M73019; AAB36613.1; -; Genomic_DNA.
DR   ProteinModelPortal; P23001; -.
DR   SMR; P23001; 2-180.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Flavoprotein; FMN;
KW   Nitrogen fixation; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    180       Flavodoxin-B.
FT                                /FTId=PRO_0000171603.
FT   DOMAIN        4    173       Flavodoxin-like.
SQ   SEQUENCE   180 AA;  19524 MW;  A19BE720B93F551D CRC64;
     MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDAVNVNRV SAEDFAQYQF LILGTPTLGE
     GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENFLDA MGELHSFFTE
     RGAKVVGAWS TDGYEFEGST AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL
//
ID   FLAV_AZOVI              Reviewed;         180 AA.
AC   P00324;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   18-APR-2012, entry version 82.
DE   RecName: Full=Flavodoxin-2;
GN   Name=nifF;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89123097; PubMed=2644218;
RA   Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A.,
RA   Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT   "Physical and genetic map of the major nif gene cluster from
RT   Azotobacter vinelandii.";
RL   J. Bacteriol. 171:1017-1027(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88087273; PubMed=3121629;
RA   Bennett L., Jacobson M., Dean D.R.;
RT   "Isolation, sequencing, and mutagenesis of the nifF gene encoding
RT   flavodoxin from Azotobacter vinelandii.";
RL   J. Biol. Chem. 263:1364-1369(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-180.
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW;
RX   MEDLINE=77242321; PubMed=889809; DOI=10.1021/bi00635a005;
RA   Tanaka M., Haniu M., Yasunobu K.T., Yoch D.C.;
RT   "Complete amino acid sequence of azotoflavin, a flavodoxin from
RT   Azotobacter vinelandii.";
RL   Biochemistry 16:3525-3537(1977).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-21, AND MASS SPECTROMETRY.
RC   STRAIN=OP / UW136;
RX   MEDLINE=96276406; PubMed=8694750;
RA   Gangeswaran R., Eady R.R.;
RT   "Flavodoxin 1 of Azotobacter vinelandii: characterization and role in
RT   electron donation to purified assimilatory nitrate reductase.";
RL   Biochem. J. 317:103-108(1996).
RN   [5]
RP   STRUCTURE BY NMR.
RC   STRAIN=ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617;
RX   MEDLINE=98180401; PubMed=9521106;
RA   Steensma E., Nijman M.J.M., Bollen Y.J.M., de Jager P.A.,
RA   van den Berg W.A.M., van Dongen W.M.A.M., van Mierlo C.P.M.;
RT   "Apparent local stability of the secondary structure of Azotobacter
RT   vinelandii holoflavodoxin II as probed by hydrogen exchange:
RT   implications for redox potential regulation and flavodoxin folding.";
RL   Protein Sci. 7:306-317(1998).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR: FMN.
CC   -!- SUBUNIT: Monomer.
CC   -!- MASS SPECTROMETRY: Mass=19533; Mass_error=5; Method=Electrospray;
CC       Range=2-180; Source=PubMed:8694750;
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M20568; AAA64735.1; -; Genomic_DNA.
DR   EMBL; J03519; AAA22154.1; -; Genomic_DNA.
DR   PIR; A29935; FXAVEP.
DR   PDB; 1YOB; X-ray; 2.25 A; A/B=2-179.
DR   PDBsum; 1YOB; -.
DR   ProteinModelPortal; P00324; -.
DR   SMR; P00324; 2-180.
DR   EvolutionaryTrace; P00324; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Nitrogen fixation; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    180       Flavodoxin-2.
FT                                /FTId=PRO_0000171605.
FT   DOMAIN        4    173       Flavodoxin-like.
FT   STRAND        4      8
FT   STRAND       11     13
FT   HELIX        14     23
FT   TURN         28     30
FT   HELIX        37     39
FT   HELIX        42     46
FT   STRAND       49     56
FT   TURN         59     61
FT   HELIX        66     68
FT   HELIX        75     82
FT   STRAND       91     97
FT   TURN        100    102
FT   TURN        104    108
FT   HELIX       109    119
FT   TURN        120    122
FT   STRAND      124    126
FT   STRAND      142    152
FT   TURN        154    156
FT   HELIX       158    160
FT   HELIX       161    172
FT   HELIX       173    176
SQ   SEQUENCE   180 AA;  19663 MW;  8B1B43F23AB5E8B4 CRC64;
     MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDALNVNRV SAEDFAQYQF LILGTPTLGE
     GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENYLDA LGELYSFFKD
     RGAKIVGSWS TDGYEFESSE AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL
//
ID   FLAV_BACSU              Reviewed;         158 AA.
AC   O34737;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-MAY-2012, entry version 82.
DE   RecName: Full=Probable flavodoxin-1;
GN   Name=ykuN; OrderedLocusNames=BSU14150;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Scanlan E., Devine K.M.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (Potential).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AJ222587; CAA10877.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13288.1; -; Genomic_DNA.
DR   PIR; C69866; C69866.
DR   RefSeq; NP_389298.1; NC_000964.3.
DR   ProteinModelPortal; O34737; -.
DR   SMR; O34737; 2-146.
DR   EnsemblBacteria; EBBACT00000000146; EBBACP00000000146; EBBACG00000000146.
DR   GeneID; 939194; -.
DR   GenomeReviews; AL009126_GR; BSU14150.
DR   KEGG; bsu:BSU14150; -.
DR   PATRIC; 18974619; VBIBacSub10457_1501.
DR   GenoList; BSU14150; -.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030540; -.
DR   KO; K03839; -.
DR   OMA; ATKGADS; -.
DR   ProtClustDB; PRK06703; -.
DR   BioCyc; BSUB:BSU14150-MONOMER; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; FALSE_NEG.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Electron transport; Flavoprotein; FMN;
KW   Reference proteome; Transport.
FT   CHAIN         1    158       Probable flavodoxin-1.
FT                                /FTId=PRO_0000171607.
FT   DOMAIN        4    144       Flavodoxin-like.
SQ   SEQUENCE   158 AA;  17793 MW;  FECE71BF6E552D3F CRC64;
     MAKALITYAS MSGNTEDIAF IIKDTLQEYE LDIDCVEIND MDASCLTSYD YVLIGTYTWG
     DGDLPYEAED FFEEVKQIQL NGLKTACFGS GDYSYPKFCE AVNLFNVMLQ EAGAAVYQET
     LKIELAPETD EDVESCRAFA RGFLAWADYM NKEKIHVS
//
ID   FLAV_CHOCR              Reviewed;         173 AA.
AC   P14070;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   18-APR-2012, entry version 72.
DE   RecName: Full=Flavodoxin;
OS   Chondrus crispus (Carragheen moss) (Irish moss).
OC   Eukaryota; Rhodophyta; Florideophyceae; Gigartinales; Gigartinaceae;
OC   Chondrus.
OX   NCBI_TaxID=2769;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=90088453; PubMed=2597140;
RA   Wakabayashi S., Kimura K., Matsubara H., Rogers L.J.;
RT   "The amino acid sequence of a flavodoxin from the eukaryotic red alga
RT   Chondrus crispus.";
RL   Biochem. J. 263:981-984(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-34.
RA   Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.;
RT   "N-terminal amino acid sequences of flavodoxins from Chondrus crispus
RT   and Nostoc strain MAC.";
RL   Phytochemistry 25:2113-2115(1986).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
RX   MEDLINE=90368796; PubMed=2394748;
RA   Fukuyama K., Wakabayashi S., Matsubara H., Rogers L.J.;
RT   "Tertiary structure of oxidized flavodoxin from an eukaryotic red alga
RT   Chondrus crispus at 2.35-A resolution. Localization of charged
RT   residues and implication for interaction with electron transfer
RT   partners.";
RL   J. Biol. Chem. 265:15804-15812(1990).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=92292160; PubMed=1602481; DOI=10.1016/0022-2836(92)90400-E;
RA   Fukuyama K., Matsubara H., Rogers L.J.;
RT   "Crystal structure of oxidized flavodoxin from a red alga Chondrus
RT   crispus refined at 1.8-A resolution. Description of the flavin
RT   mononucleotide binding site.";
RL   J. Mol. Biol. 225:775-789(1992).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   PIR; S06648; S06648.
DR   PDB; 2FCR; X-ray; 1.80 A; A=1-173.
DR   PDBsum; 2FCR; -.
DR   ProteinModelPortal; P14070; -.
DR   SMR; P14070; 1-173.
DR   EvolutionaryTrace; P14070; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   CHAIN         1    173       Flavodoxin.
FT                                /FTId=PRO_0000171612.
FT   DOMAIN        2    168       Flavodoxin-like.
FT   CONFLICT     29     29       D -> S (in Ref. 2; AA sequence).
FT   CONFLICT     33     33       D -> S (in Ref. 2; AA sequence).
FT   STRAND        2      6
FT   STRAND        9     11
FT   HELIX        12     24
FT   HELIX        25     27
FT   HELIX        34     36
FT   HELIX        40     45
FT   STRAND       47     54
FT   HELIX        69     75
FT   HELIX        77     79
FT   STRAND       86     93
FT   TURN         95     97
FT   TURN        102    104
FT   HELIX       105    115
FT   STRAND      119    121
FT   HELIX       126    128
FT   STRAND      141    148
FT   TURN        149    151
FT   HELIX       156    171
SQ   SEQUENCE   173 AA;  18871 MW;  EF1F3A3554CA4166 CRC64;
     KIGIFFSTST GNTTEVADFI GKTLGAKADA PIDVDDVTDP QALKDYDLLF LGAPTWNTGA
     DTERSGTSWD EFLYDKLPEV DMKDLPVAIF GLGDAEGYPD NFCDAIEEIH DCFAKQGAKP
     VGFSNPDDYD YEESKSVRDG KFLGLPLDMV NDQIPMEKRV AGWVEAVVSE TGV
//
ID   FLAV_CLOBE              Reviewed;         138 AA.
AC   P00322;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   18-APR-2012, entry version 75.
DE   RecName: Full=Flavodoxin;
OS   Clostridium beijerinckii (Clostridium MP).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1520;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=74277392; PubMed=4843142;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G.;
RT   "The amino acid sequence of the Clostridium MP flavodoxin.";
RL   J. Biol. Chem. 249:4393-4396(1974).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF OXIDIZED FORM.
RX   MEDLINE=74277391; PubMed=4843141;
RA   Burnett R.M., Darling G.D., Kendall D.S., Lequesne M.E., Mayhew S.G.,
RA   Smith W.W., Ludwig M.L.;
RT   "The structure of the oxidized form of clostridial flavodoxin at 1.9-A
RT   resolution.";
RL   J. Biol. Chem. 249:4383-4392(1974).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=97178811; PubMed=9063874; DOI=10.1021/bi962180o;
RA   Ludwig M.L., Pattridge K.A., Metzger A.L., Dixon M.M., Eren M.,
RA   Feng Y., Swenson R.P.;
RT   "Control of oxidation-reduction potentials in flavodoxin from
RT   Clostridium beijerinckii: the role of conformation changes.";
RL   Biochemistry 36:1259-1280(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   PDB; 1FLA; X-ray; 1.90 A; A=1-138.
DR   PDB; 1FLD; X-ray; 1.80 A; A=1-138.
DR   PDB; 1FLN; X-ray; 1.90 A; A=1-138.
DR   PDB; 1FVX; X-ray; 1.90 A; A=1-138.
DR   PDB; 2FAX; X-ray; 1.80 A; A=1-136.
DR   PDB; 2FDX; X-ray; 1.65 A; A=1-136.
DR   PDB; 2FLV; X-ray; 1.80 A; A=1-138.
DR   PDB; 2FOX; X-ray; 1.80 A; A=1-138.
DR   PDB; 2FVX; X-ray; 1.80 A; A=1-138.
DR   PDB; 3NLL; X-ray; 2.40 A; A=1-138.
DR   PDB; 4NLL; X-ray; 1.90 A; A=1-138.
DR   PDB; 4NUL; X-ray; 1.90 A; A=1-138.
DR   PDB; 5NLL; X-ray; 1.75 A; A=1-138.
DR   PDB; 5NUL; X-ray; 1.60 A; A=1-138.
DR   PDB; 5ULL; X-ray; 1.80 A; A=1-138.
DR   PDB; 6NUL; X-ray; 1.80 A; A=1-136.
DR   PDBsum; 1FLA; -.
DR   PDBsum; 1FLD; -.
DR   PDBsum; 1FLN; -.
DR   PDBsum; 1FVX; -.
DR   PDBsum; 2FAX; -.
DR   PDBsum; 2FDX; -.
DR   PDBsum; 2FLV; -.
DR   PDBsum; 2FOX; -.
DR   PDBsum; 2FVX; -.
DR   PDBsum; 3NLL; -.
DR   PDBsum; 4NLL; -.
DR   PDBsum; 4NUL; -.
DR   PDBsum; 5NLL; -.
DR   PDBsum; 5NUL; -.
DR   PDBsum; 5ULL; -.
DR   PDBsum; 6NUL; -.
DR   ProteinModelPortal; P00322; -.
DR   SMR; P00322; 1-138.
DR   EvolutionaryTrace; P00322; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   CHAIN         1    138       Flavodoxin.
FT                                /FTId=PRO_0000171613.
FT   DOMAIN        1    136       Flavodoxin-like.
FT   STRAND        2      6
FT   STRAND        8     10
FT   HELIX        11     25
FT   STRAND       31     34
FT   HELIX        35     37
FT   HELIX        40     43
FT   STRAND       47     53
FT   TURN         57     59
FT   TURN         63     65
FT   HELIX        66     73
FT   HELIX        74     76
FT   STRAND       81     93
FT   HELIX        94    105
FT   STRAND      115    120
FT   HELIX       122    124
FT   HELIX       125    136
SQ   SEQUENCE   138 AA;  15332 MW;  98BE3746EC000FF1 CRC64;
     MKIVYWSGTG NTEKMAELIA KGIIESGKDV NTINVSDVNI DELLNEDILI LGCSAMGDEV
     LEESEFEPFI EEISTKISGK KVALFGSYGW GDGKWMRDFE ERMNGYGCVV VETPLIVQNE
     PDEAEQDCIE FGKKIANI
//
ID   FLAV_CLOSA              Reviewed;         160 AA.
AC   P18855;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   21-SEP-2011, entry version 50.
DE   RecName: Full=Flavodoxin;
GN   Name=floX;
OS   Clostridium saccharobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=169679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91123180; PubMed=1991710;
RA   Santangelo J.D., Jones D.T., Woods D.R.;
RT   "Metronidazole activation and isolation of Clostridium acetobutylicum
RT   electron transport genes.";
RL   J. Bacteriol. 173:1088-1095(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -!- CAUTION: Was originally thought to originate from
CC       C.acetobutylicum.
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DR   EMBL; M36770; AAA23238.1; -; Genomic_DNA.
DR   ProteinModelPortal; P18855; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    160       Flavodoxin.
FT                                /FTId=PRO_0000171614.
FT   DOMAIN        3    153       Flavodoxin-like.
SQ   SEQUENCE   160 AA;  17763 MW;  6153F8A1F0BCDC8D CRC64;
     MKISILYSSK TGKTERVAKL IEEGVKRSGN IEVKTMNLDA VDKKFLQESE GIIFGTPTYY
     ANISWEMKKW IDESSEFNLE GKLGAAFSTA NSIAGGSDIA LLTILNHLMV KGMLVYSGGV
     AFGKPKTHLG YVHINEIQEN EDENARIFGE RIANKVKQIF
//
ID   FLAV_DESDE              Reviewed;         148 AA.
AC   P26492;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   18-APR-2012, entry version 53.
DE   RecName: Full=Flavodoxin;
OS   Desulfovibrio desulfuricans.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=876;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 29577 / CIP 107039 / LMG 7529 / NCIB 8307 / VKM B-1799;
RX   MEDLINE=91316149; PubMed=1859847; DOI=10.1016/0167-4781(91)90190-W;
RA   Helms L.R., Swenson R.P.;
RT   "Cloning and characterization of the flavodoxin gene from
RT   Desulfovibrio desulfuricans.";
RL   Biochim. Biophys. Acta 1089:417-419(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; X59438; CAA42064.1; -; mRNA.
DR   PIR; S17000; FXDVD.
DR   PDB; 3F6R; X-ray; 2.00 A; A/B/C/D=1-148.
DR   PDB; 3F6S; X-ray; 2.50 A; A/B/D/E/F/G/H/I=1-148.
DR   PDB; 3F90; X-ray; 2.50 A; A/B/D/E/F/G/H/I=1-148.
DR   PDBsum; 3F6R; -.
DR   PDBsum; 3F6S; -.
DR   PDBsum; 3F90; -.
DR   ProteinModelPortal; P26492; -.
DR   EvolutionaryTrace; P26492; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    148       Flavodoxin.
FT                                /FTId=PRO_0000171615.
FT   DOMAIN        4    145       Flavodoxin-like.
FT   STRAND        3      8
FT   HELIX        15     27
FT   STRAND       32     37
FT   TURN         38     40
FT   TURN         44     47
FT   STRAND       52     55
FT   HELIX        69     75
FT   HELIX        76     80
FT   STRAND       87     90
FT   STRAND       98    100
FT   HELIX       105    114
FT   HELIX       130    132
FT   HELIX       134    146
SQ   SEQUENCE   148 AA;  15694 MW;  1CE35B4B79817459 CRC64;
     MSKVLIVFGS STGNTESIAQ KLEELIAAGG HEVTLLNAAD ASAENLADGY DAVLFGCSAW
     GMEDLEMQDD FLSLFEEFNR IGLAGRKVAA FASGDQEYEH FCGAVPAIEE RAKELGATII
     AEGLKMEGDA SNDPEAVASF AEDVLKQL
//
ID   FLAV_DESGI              Reviewed;         146 AA.
AC   Q01095;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   31-MAY-2011, entry version 56.
DE   RecName: Full=Flavodoxin;
OS   Desulfovibrio gigas.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759;
RX   MEDLINE=92329549; PubMed=1627649; DOI=10.1016/0167-4781(92)90034-W;
RA   Helms L.R., Swenson R.P.;
RT   "The primary structures of the flavodoxins from two strains of
RT   Desulfovibrio gigas. Cloning and nucleotide sequence of the structural
RT   genes.";
RL   Biochim. Biophys. Acta 1131:325-328(1992).
CC   -!- FUNCTION: Electron-transfer proteins that function in various
CC       electron transport systems in micro-organisms. Functionally
CC       interchangeable with ferredoxin.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; X64766; CAA46013.1; -; Genomic_DNA.
DR   PIR; S24311; S24311.
DR   ProteinModelPortal; Q01095; -.
DR   SMR; Q01095; 2-146.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    146       Flavodoxin.
FT                                /FTId=PRO_0000171617.
FT   DOMAIN        4    143       Flavodoxin-like.
SQ   SEQUENCE   146 AA;  15470 MW;  95D9E73B1FCF1403 CRC64;
     MPKALIVYGS TTGNTEGVAE AIAKTLNSEG METTVVNVAD VTAPGLAEGY DVVLLGCSTW
     GDDEIELQED FVPLYEDLDR AGLKDKKVGV FGCGDSSYTY FCGAVDVIEK KAEELGATLV
     ASSLKIDGEP DSAEVLDWAR EVLARV
//
ID   FLAV_DESAD              Reviewed;         146 AA.
AC   P18086; C6BZ47;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   16-MAY-2012, entry version 64.
DE   RecName: Full=Flavodoxin;
GN   OrderedLocusNames=Desal_0805;
OS   Desulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 /
OS   VKM B-1763).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=526222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90241257; PubMed=2334437; DOI=10.1016/0006-291X(90)92393-E;
RA   Helms L.R., Krey G.D., Swenson R.P.;
RT   "Identification, sequence determination, and expression of the
RT   flavodoxin gene from Desulfovibrio salexigens.";
RL   Biochem. Biophys. Res. Commun. 168:809-817(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I., Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B.,
RA   Hazen T.C.;
RT   "Complete sequence of Desulfovibrio salexigens DSM 2638.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M35475; AAA23368.1; -; Genomic_DNA.
DR   EMBL; CP001649; ACS78871.1; -; Genomic_DNA.
DR   PIR; A34640; A34640.
DR   RefSeq; YP_002990410.1; NC_012881.1.
DR   ProteinModelPortal; P18086; -.
DR   SMR; P18086; 2-146.
DR   STRING; P18086; -.
DR   GeneID; 8091789; -.
DR   GenomeReviews; CP001649_GR; Desal_0805.
DR   KEGG; dsa:Desal_0805; -.
DR   PATRIC; 21757061; VBIDesSal121003_0807.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030540; -.
DR   ProtClustDB; CLSK634549; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    146       Flavodoxin.
FT                                /FTId=PRO_0000171619.
FT   DOMAIN        4    143       Flavodoxin-like.
SQ   SEQUENCE   146 AA;  15812 MW;  BDE3651310E1F780 CRC64;
     MSKSLIVYGS TTGNTETAAE YVAEAFENKE IDVELKNVTD VSVADLGNGY DIVLFGCSTW
     GEEEIELQDD FIPLYDSLEN ADLKGKKVSV FGCGDSDYTY FCGAVDAIEE KLEKMGAVVI
     GDSLKIDGDP ERDEIVSWGS GIADKI
//
ID   FLAV_DESVH              Reviewed;         148 AA.
AC   P00323;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   16-MAY-2012, entry version 100.
DE   RecName: Full=Flavodoxin;
GN   OrderedLocusNames=DVU_2680;
OS   Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB
OS   8303).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89008444; PubMed=3170590;
RA   Krey G.D., Vanin E.F., Swenson R.P.;
RT   "Cloning, nucleotide sequence, and expression of the flavodoxin gene
RT   from Desulfovibrio vulgaris (Hildenborough).";
RL   J. Biol. Chem. 263:15436-15443(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Curley G.P., Voordouw G.;
RT   "Cloning and sequencing of the gene encoding flavodoxin from
RT   Desulfovibrio vulgaris Hildenborough.";
RL   FEMS Microbiol. Lett. 49:295-299(1988).
RN   [3]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=77118626; PubMed=402366;
RA   Dubourdieu M., Fox J.L.;
RT   "Amino acid sequence of Desulfovibrio vulgaris flavodoxin.";
RL   J. Biol. Chem. 252:1453-1463(1977).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hildenborough / ATCC 29579 / NCIMB 8303;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D.,
RA   Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R.,
RA   Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=91162643; PubMed=2002503; DOI=10.1016/0022-2836(91)90884-9;
RA   Warr W., Tulinsky A., Swenson R.P., Watenpaugh K.D.;
RT   "Comparison of the crystal structures of a flavodoxin in its three
RT   oxidation states at cryogenic temperatures.";
RL   J. Mol. Biol. 218:195-208(1991).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   MEDLINE=74087652; PubMed=4521211; DOI=10.1073/pnas.70.12.3857;
RA   Watenpaugh K.D., Sieker L.C., Jensen L.H.;
RT   "The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin
RT   at 2.0-A resolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:3857-3860(1973).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=73044810; PubMed=4508313; DOI=10.1073/pnas.69.11.3185;
RA   Watenpaugh K.D., Sieker L.C., Jensen L.H., Legall J., Dubourdieu M.;
RT   "Structure of the oxidized form of a flavodoxin at 2.5-A resolution:
RT   resolution of the phase ambiguity by anomalous scattering.";
RL   Proc. Natl. Acad. Sci. U.S.A. 69:3185-3188(1972).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=99089597; PubMed=9874201;
RX   DOI=10.1046/j.1432-1327.1998.2580362.x;
RA   Walsh M.A., McCarthy A., O'Farrell P.A., McArdle P., Cunningham P.D.,
RA   Mayhew S.G., Higgins T.M.;
RT   "X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough)
RT   apoflavodoxin-riboflavin complex.";
RL   Eur. J. Biochem. 258:362-371(1998).
RN   [9]
RP   STRUCTURE BY NMR.
RX   MEDLINE=93238683; PubMed=8477691;
RX   DOI=10.1111/j.1432-1033.1993.tb17746.x;
RA   Knauf M.A., Loehr F., Curley G.P., O'Farrell P., Mayhew S.G.,
RA   Mueller F., Rueterjans H.;
RT   "Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio
RT   vulgaris flavodoxin. Sequential assignments and identification of
RT   secondary structure elements.";
RL   Eur. J. Biochem. 213:167-184(1993).
RN   [10]
RP   STRUCTURE BY NMR.
RX   MEDLINE=96283837; PubMed=8681954;
RX   DOI=10.1111/j.1432-1033.1996.0423z.x;
RA   Knauf M.A., Loehr F., Bluemel M., Mayhew S.G., Rueterjans H.;
RT   "NMR investigation of the solution conformation of oxidized flavodoxin
RT   from Desulfovibrio vulgaris. Determination of the tertiary structure
RT   and detection of protein-bound water molecules.";
RL   Eur. J. Biochem. 238:423-434(1996).
RN   [11]
RP   STRUCTURE BY NMR.
RX   MEDLINE=93237739; PubMed=8477184; DOI=10.1007/BF00178258;
RA   Stockman B.J., Euvrard A., Kloosterman D.A., Scahill T.A.,
RA   Swenson R.P.;
RT   "1H and 15N resonance assignments and solution secondary structure of
RT   oxidized Desulfovibrio vulgaris flavodoxin determined by heteronuclear
RT   three-dimensional NMR spectroscopy.";
RL   J. Biomol. NMR 3:133-149(1993).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; J04033; AAA23367.1; -; Genomic_DNA.
DR   EMBL; AE017285; AAS97152.1; -; Genomic_DNA.
DR   PIR; A31991; FXDV.
DR   RefSeq; YP_011892.1; NC_002937.3.
DR   PDB; 1AKQ; X-ray; 1.90 A; A=2-148.
DR   PDB; 1AKR; X-ray; 1.58 A; A=2-148.
DR   PDB; 1AKT; X-ray; 1.80 A; A=2-148.
DR   PDB; 1AKU; X-ray; 1.90 A; A=2-148.
DR   PDB; 1AKV; X-ray; 2.00 A; A=2-148.
DR   PDB; 1AKW; X-ray; 1.75 A; A=2-148.
DR   PDB; 1AZL; X-ray; 1.80 A; A=2-148.
DR   PDB; 1BU5; X-ray; 1.83 A; A/B=2-148.
DR   PDB; 1C7E; X-ray; 2.25 A; A/B=2-148.
DR   PDB; 1C7F; X-ray; 2.00 A; A/B=2-148.
DR   PDB; 1F4P; X-ray; 1.30 A; A=2-148.
DR   PDB; 1FX1; X-ray; 2.00 A; A=1-148.
DR   PDB; 1I1O; X-ray; 2.00 A; A=3-148.
DR   PDB; 1J8Q; X-ray; 1.35 A; A=3-148.
DR   PDB; 1J9E; X-ray; 1.44 A; A=3-148.
DR   PDB; 1J9G; X-ray; 2.40 A; A=3-148.
DR   PDB; 1WSB; X-ray; 1.80 A; A=3-148.
DR   PDB; 1WSW; X-ray; 1.69 A; A=3-148.
DR   PDB; 1XT6; X-ray; 1.80 A; A=3-148.
DR   PDB; 1XYV; X-ray; 1.79 A; A=3-148.
DR   PDB; 1XYY; X-ray; 1.70 A; A=3-148.
DR   PDB; 2FX2; X-ray; 1.90 A; A=3-148.
DR   PDB; 3FX2; X-ray; 1.90 A; A=3-148.
DR   PDB; 4FX2; X-ray; 1.90 A; A=3-148.
DR   PDB; 5FX2; X-ray; 1.90 A; A=3-148.
DR   PDBsum; 1AKQ; -.
DR   PDBsum; 1AKR; -.
DR   PDBsum; 1AKT; -.
DR   PDBsum; 1AKU; -.
DR   PDBsum; 1AKV; -.
DR   PDBsum; 1AKW; -.
DR   PDBsum; 1AZL; -.
DR   PDBsum; 1BU5; -.
DR   PDBsum; 1C7E; -.
DR   PDBsum; 1C7F; -.
DR   PDBsum; 1F4P; -.
DR   PDBsum; 1FX1; -.
DR   PDBsum; 1I1O; -.
DR   PDBsum; 1J8Q; -.
DR   PDBsum; 1J9E; -.
DR   PDBsum; 1J9G; -.
DR   PDBsum; 1WSB; -.
DR   PDBsum; 1WSW; -.
DR   PDBsum; 1XT6; -.
DR   PDBsum; 1XYV; -.
DR   PDBsum; 1XYY; -.
DR   PDBsum; 2FX2; -.
DR   PDBsum; 3FX2; -.
DR   PDBsum; 4FX2; -.
DR   PDBsum; 5FX2; -.
DR   ProteinModelPortal; P00323; -.
DR   SMR; P00323; 2-148.
DR   STRING; P00323; -.
DR   GeneID; 2795051; -.
DR   GenomeReviews; AE017285_GR; DVU_2680.
DR   KEGG; dvu:DVU2680; -.
DR   PATRIC; 32064950; VBIDesVul119526_2425.
DR   TIGR; DVU_2680; -.
DR   eggNOG; COG0716; -.
DR   OMA; HFCGAVD; -.
DR   ProtClustDB; CLSK634549; -.
DR   BioCyc; DVUL882:DVU_2680-MONOMER; -.
DR   DrugBank; DB00140; Riboflavin.
DR   EvolutionaryTrace; P00323; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Electron transport; Flavoprotein; FMN; Reference proteome; Transport.
FT   CHAIN         1    148       Flavodoxin.
FT                                /FTId=PRO_0000171620.
FT   DOMAIN        4    145       Flavodoxin-like.
FT   CONFLICT     28     28       D -> N (in Ref. 2).
FT   STRAND        3      9
FT   STRAND       11     13
FT   HELIX        14     29
FT   STRAND       32     37
FT   HELIX        38     40
FT   TURN         44     49
FT   STRAND       51     57
FT   STRAND       62     64
FT   TURN         69     71
FT   HELIX        72     76
FT   HELIX        78     80
FT   STRAND       87     94
FT   STRAND       98    100
FT   HELIX       103    114
FT   STRAND      124    128
FT   HELIX       130    133
FT   HELIX       134    145
SQ   SEQUENCE   148 AA;  15823 MW;  E07630E7047ABD3F CRC64;
     MPKALIVYGS TTGNTEYTAE TIARELADAG YEVDSRDAAS VEAGGLFEGF DLVLLGCSTW
     GDDSIELQDD FIPLFDSLEE TGAQGRKVAC FGCGDSSYEY FCGAVDAIEE KLKNLGAEIV
     QDGLRIDGDP RAARDDIVGW AHDVRGAI
//
ID   FLAV_DESVM              Reviewed;         148 AA.
AC   P71165; B8DKD5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   16-MAY-2012, entry version 61.
DE   RecName: Full=Flavodoxin;
GN   OrderedLocusNames=DvMF_1143;
OS   Desulfovibrio vulgaris (strain Miyazaki F / DSM 19637).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=Isolate F;
RX   MEDLINE=98230696; PubMed=9562622;
RA   Kitamura M., Sagara T., Taniguchi M., Ashida M., Ezoe K., Kohno K.,
RA   Kojima S., Ozawa K., Akutsu H., Kumagai I., Nakaya T.;
RT   "Cloning and expression of the gene encoding flavodoxin from
RT   Desulfovibrio vulgaris (Miyazaki F).";
RL   J. Biochem. 123:891-898(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Miyazaki F / DSM 19637;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Hazen T.C., Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; D88493; BAA13628.1; -; Genomic_DNA.
DR   EMBL; CP001197; ACL08097.1; -; Genomic_DNA.
DR   RefSeq; YP_002435565.1; NC_011769.1.
DR   ProteinModelPortal; P71165; -.
DR   STRING; P71165; -.
DR   GeneID; 7173044; -.
DR   GenomeReviews; CP001197_GR; DvMF_1143.
DR   KEGG; dvm:DvMF_1143; -.
DR   PATRIC; 21772357; VBIDesVul86729_1215.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030540; -.
DR   OMA; ARIICDS; -.
DR   ProtClustDB; CLSK634549; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    148       Flavodoxin.
FT                                /FTId=PRO_0000171621.
FT   DOMAIN        4    145       Flavodoxin-like.
FT   CONFLICT    104    104       A -> P (in Ref. 1; BAA13628).
SQ   SEQUENCE   148 AA;  15630 MW;  9D321268C4089DF1 CRC64;
     MANVLIVYGS TTGNTAWVAE TVGRDIAEAG HSVEIRDAGQ VEAEGLCEGR DLVLFGCSTW
     GDDEIELQDD FIHLYESLEA TGAGKGRAAC FGCGDSSYTY FCGAVDAIEE RLSGLGADIV
     ADSLKIDGDP RTMRDDVSAW AGRVVTAL
//
ID   FLAV_ECO57              Reviewed;         176 AA.
AC   P61951; P23243;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 51.
DE   RecName: Full=Flavodoxin-1;
GN   Name=fldA; OrderedLocusNames=Z0832, ECs0715;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (Potential). Involved in the reactivation of inactive
CC       cob(II)alamin in methionine synthase (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AE005174; AAG55007.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34138.1; -; Genomic_DNA.
DR   PIR; C85568; C85568.
DR   PIR; C90718; C90718.
DR   RefSeq; NP_286399.1; NC_002655.2.
DR   RefSeq; NP_308742.1; NC_002695.1.
DR   ProteinModelPortal; P61951; -.
DR   SMR; P61951; 2-176.
DR   EnsemblBacteria; EBESCT00000027406; EBESCP00000026299; EBESCG00000026458.
DR   EnsemblBacteria; EBESCT00000055801; EBESCP00000053629; EBESCG00000054849.
DR   GeneID; 917084; -.
DR   GeneID; 957759; -.
DR   GenomeReviews; AE005174_GR; Z0832.
DR   GenomeReviews; BA000007_GR; ECs0715.
DR   KEGG; ece:Z0832; -.
DR   KEGG; ecs:ECs0715; -.
DR   PATRIC; 18350446; VBIEscCol44059_0734.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   OMA; DDKHFVG; -.
DR   ProtClustDB; PRK09267; -.
DR   BioCyc; ECOL83334:ECS0715-MONOMER; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    176       Flavodoxin-1.
FT                                /FTId=PRO_0000171624.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   176 AA;  19737 MW;  8878DA1A8EAA55BD CRC64;
     MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA
//
ID   FLAV_ECOL6              Reviewed;         176 AA.
AC   P61950; P23243;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 51.
DE   RecName: Full=Flavodoxin-1;
GN   Name=fldA; OrderedLocusNames=c0771;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (Potential). Involved in the reactivation of inactive
CC       cob(II)alamin in methionine synthase (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79244.1; Type=Erroneous initiation;
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DR   EMBL; AE014075; AAN79244.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_752701.2; NC_004431.1.
DR   ProteinModelPortal; P61950; -.
DR   SMR; P61950; 2-176.
DR   EnsemblBacteria; EBESCT00000041388; EBESCP00000039737; EBESCG00000040438.
DR   GeneID; 1035998; -.
DR   GenomeReviews; AE014075_GR; c0771.
DR   KEGG; ecc:c0771; -.
DR   PATRIC; 18279597; VBIEscCol75197_0735.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   OMA; DDKHFVG; -.
DR   ProtClustDB; PRK09267; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    176       Flavodoxin-1.
FT                                /FTId=PRO_0000171623.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   176 AA;  19737 MW;  8878DA1A8EAA55BD CRC64;
     MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA
//
ID   FLAV_ECOLI              Reviewed;         176 AA.
AC   P61949; P23243;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 81.
DE   RecName: Full=Flavodoxin-1;
GN   Name=fldA; OrderedLocusNames=b0684, JW0671;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15.
RX   MEDLINE=91154129; PubMed=1999390;
RA   Osborne C., Chen L.-M., Matthews R.G.;
RT   "Isolation, cloning, mapping, and nucleotide sequencing of the gene
RT   encoding flavodoxin in Escherichia coli.";
RL   J. Bacteriol. 173:1729-1737(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11.
RX   MEDLINE=95050480; PubMed=7961651;
RA   Jenkins C.M., Waterman M.R.;
RT   "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli
RT   support bovine cytochrome P450c17 hydroxylase activities.";
RL   J. Biol. Chem. 269:27401-27408(1994).
RN   [6]
RP   FUNCTION IN COBALT REDUCTION OF COB(II)ALAMIN.
RX   PubMed=9730838; DOI=10.1021/bi9808565;
RA   Jarrett J.T., Hoover D.M., Ludwig M.L., Matthews R.G.;
RT   "The mechanism of adenosylmethionine-dependent activation of
RT   methionine synthase: a rapid kinetic analysis of intermediates in
RT   reductive methylation of Cob(II)alamin enzyme.";
RL   Biochemistry 37:12649-12658(1998).
RN   [7]
RP   STRUCTURE BY NMR.
RX   MEDLINE=97234567; PubMed=9119004;
RX   DOI=10.1111/j.1432-1033.1997.00384.x;
RA   Ponstingl H., Otting G.;
RT   "NMR assignments, secondary structure and hydration of oxidized
RT   Escherichia coli flavodoxin.";
RL   Eur. J. Biochem. 244:384-399(1997).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=98078562; PubMed=9416602;
RA   Hoover D.M., Ludwig M.L.;
RT   "A flavodoxin that is required for enzyme activation: the structure of
RT   oxidized flavodoxin from Escherichia coli at 1.8-A resolution.";
RL   Protein Sci. 6:2525-2537(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (Potential). Involved in the reactivation of inactive
CC       cob(II)alamin in methionine synthase.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M59426; AAA23789.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73778.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35333.1; -; Genomic_DNA.
DR   PIR; A37319; A37319.
DR   RefSeq; NP_415210.1; NC_000913.2.
DR   PDB; 1AG9; X-ray; 1.80 A; A/B=2-176.
DR   PDB; 1AHN; X-ray; 2.60 A; A=2-176.
DR   PDBsum; 1AG9; -.
DR   PDBsum; 1AHN; -.
DR   ProteinModelPortal; P61949; -.
DR   SMR; P61949; 2-176.
DR   DIP; DIP-48242N; -.
DR   IntAct; P61949; 19.
DR   MINT; MINT-1239730; -.
DR   ECO2DBASE; A019.0; 6TH EDITION.
DR   EnsemblBacteria; EBESCT00000004622; EBESCP00000004622; EBESCG00000003770.
DR   EnsemblBacteria; EBESCT00000015811; EBESCP00000015102; EBESCG00000014871.
DR   GeneID; 945293; -.
DR   GenomeReviews; AP009048_GR; JW0671.
DR   GenomeReviews; U00096_GR; b0684.
DR   KEGG; eco:b0684; -.
DR   PATRIC; 32116561; VBIEscCol129921_0713.
DR   EchoBASE; EB0314; -.
DR   EcoGene; EG10318; fldA.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   OMA; DDKHFVG; -.
DR   ProtClustDB; PRK09267; -.
DR   BioCyc; EcoCyc:FLAVODOXIN1-MONOMER; -.
DR   EvolutionaryTrace; P61949; -.
DR   Genevestigator; P61949; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Electron transport; Flavoprotein; FMN; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    176       Flavodoxin-1.
FT                                /FTId=PRO_0000171622.
FT   DOMAIN        4    165       Flavodoxin-like.
FT   STRAND        4      8
FT   STRAND       11     13
FT   HELIX        14     26
FT   TURN         28     30
FT   STRAND       31     35
FT   HELIX        36     38
FT   HELIX        41     45
FT   STRAND       48     53
FT   TURN         58     60
FT   HELIX        64     73
FT   STRAND       82     88
FT   TURN         91     96
FT   HELIX       100    109
FT   TURN        110    113
FT   STRAND      133    135
FT   STRAND      138    144
FT   TURN        146    148
FT   TURN        150    152
FT   HELIX       153    168
FT   HELIX       170    173
SQ   SEQUENCE   176 AA;  19737 MW;  8878DA1A8EAA55BD CRC64;
     MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA
//
ID   FLAV_ENTAG              Reviewed;         177 AA.
AC   P28579;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   21-SEP-2011, entry version 56.
DE   RecName: Full=Flavodoxin;
GN   Name=nifF;
OS   Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OG   Plasmid pEA3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Pantoea.
OX   NCBI_TaxID=549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=333;
RX   MEDLINE=91217003; PubMed=1708766;
RA   Kreutzer R., Dayananda S., Klingmueller W.;
RT   "Cotranscription of the electron transport protein genes nifJ and nifF
RT   in Enterobacter agglomerans 333.";
RL   J. Bacteriol. 173:3252-3256(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RC   STRAIN=333;
RA   Schwickerath O.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M38221; AAA23385.1; -; Genomic_DNA.
DR   EMBL; X99694; CAA68010.1; -; Genomic_DNA.
DR   EMBL; X78558; CAA55301.1; -; Genomic_DNA.
DR   PIR; A39414; A39414.
DR   ProteinModelPortal; P28579; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Electron transport; Flavoprotein; FMN; Nitrogen fixation; Plasmid;
KW   Transport.
FT   CHAIN         1    177       Flavodoxin.
FT                                /FTId=PRO_0000171631.
FT   DOMAIN        4    173       Flavodoxin-like.
SQ   SEQUENCE   177 AA;  19581 MW;  3D54F95F7EC60B41 CRC64;
     MATIGIFFGS DTGQTRKVAK LIHQKLDGIA DAPLDVRRAT REQFLSYPVL LLGTPTLGDG
     ELPGVEAGSQ YDSWQEFTNT LSEADLTGKT VALFGLGDQL NYSKNFVSAM RILYDLVIAR
     GACVVGNWPR EGYKFSFSAA LLENNEFVGL PLDQENQYDL TEERIDSWLE KLKPAVL
//
ID   FLAV_HAEIN              Reviewed;         174 AA.
AC   P44562;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 81.
DE   RecName: Full=Flavodoxin;
GN   Name=fldA; OrderedLocusNames=HI_0191;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   MEDLINE=95350630; PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; L42023; AAC21860.1; -; Genomic_DNA.
DR   PIR; C64053; C64053.
DR   RefSeq; NP_438360.1; NC_000907.1.
DR   ProteinModelPortal; P44562; -.
DR   SMR; P44562; 2-173.
DR   GeneID; 951101; -.
DR   GenomeReviews; L42023_GR; HI_0191.
DR   KEGG; hin:HI0191; -.
DR   PATRIC; 20188879; VBIHaeInf48452_0196.
DR   TIGR; HI_0191; -.
DR   eggNOG; COG0716; -.
DR   KO; K03839; -.
DR   OMA; DDKHFVG; -.
DR   ProtClustDB; PRK09267; -.
DR   BioCyc; HINF71421:HI_0191-MONOMER; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Electron transport; Flavoprotein; FMN;
KW   Reference proteome; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    174       Flavodoxin.
FT                                /FTId=PRO_0000171633.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   174 AA;  19627 MW;  5E95E895F04BF3F8 CRC64;
     MAIVGLFYGS DTGNTENIAK QIQKQLGSDL IDIRDIAKSS KEDIEAYDFL LFGIPTWYYG
     EAQADWDDFF PTLEEIDFTD KLVGIFGCGD QEDYADYFCD AIGTVRDIIE PHGAIVVGNW
     PTEGYNFEAS KALLEDGTFI GLCIDEDRQP ELTAERVEKW CKQIYDEMCL AELA
//
ID   FLAV_HELPY              Reviewed;         164 AA.
AC   O25776;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-MAY-2012, entry version 78.
DE   RecName: Full=Flavodoxin;
GN   Name=fldA; OrderedLocusNames=HP_1161;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter
OS   pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; AE000511; AAD08207.1; -; Genomic_DNA.
DR   PIR; A64665; A64665.
DR   RefSeq; NP_207952.1; NC_000915.1.
DR   PDB; 2BMV; X-ray; 2.11 A; A=1-164.
DR   PDB; 2W5U; X-ray; 2.62 A; A/B=1-164.
DR   PDBsum; 2BMV; -.
DR   PDBsum; 2W5U; -.
DR   ProteinModelPortal; O25776; -.
DR   SMR; O25776; 2-164.
DR   GeneID; 899921; -.
DR   GenomeReviews; AE000511_GR; HP_1161.
DR   KEGG; hpy:HP1161; -.
DR   PATRIC; 20593673; VBIHelPyl33062_1215.
DR   TIGR; HP_1161; -.
DR   eggNOG; COG0716; -.
DR   KO; K03839; -.
DR   OMA; DDKHFVG; -.
DR   ProtClustDB; PRK09267; -.
DR   EvolutionaryTrace; O25776; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; FALSE_NEG.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Electron transport; Flavoprotein;
KW   FMN; Reference proteome; Transport.
FT   CHAIN         1    164       Flavodoxin.
FT                                /FTId=PRO_0000171634.
FT   DOMAIN        4    160       Flavodoxin-like.
FT   STRAND        4      8
FT   STRAND       11     13
FT   HELIX        14     26
FT   STRAND       28     33
FT   HELIX        34     36
FT   HELIX        39     42
FT   STRAND       46     55
FT   TURN         56     58
FT   HELIX        62     68
FT   HELIX        74     77
FT   STRAND       79     86
FT   TURN         89     91
FT   TURN         96     98
FT   HELIX        99    107
FT   STRAND      110    112
FT   STRAND      116    118
FT   STRAND      133    139
FT   TURN        141    143
FT   HELIX       145    147
FT   HELIX       148    159
FT   TURN        160    162
SQ   SEQUENCE   164 AA;  17492 MW;  EBAD44D97964608C CRC64;
     MGKIGIFFGT DSGNAEAIAE KISKAIGNAE VVDVAKASKE QFNSFTKVIL VAPTAGAGDL
     QTDWEDFLGT LEASDFATKT IGLVGLGDQD TYSETFAEGI FHIYEKAKAG KVVGQTPTDG
     YHFEASKAVE GGKFVGLVID EDNQDDLTDE RISKWVEQVK GSFA
//
ID   FLAV_KLEPN              Reviewed;         176 AA.
AC   O07026;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   31-MAY-2011, entry version 47.
DE   RecName: Full=Flavodoxin;
GN   Name=fldA;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 /
RC   NCTC 9633;
RX   MEDLINE=97417492; PubMed=9272865; DOI=10.1016/S0378-1119(97)00168-6;
RA   Achenbach L.A., Genova E.G.;
RT   "Transcriptional regulation of a second flavodoxin gene from
RT   Klebsiella pneumoniae.";
RL   Gene 194:235-240(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-176.
RC   STRAIN=ATCC 13883 / DSM 30104 / JCM 1662 / NBRC 14940 / NCIMB 13281 /
RC   NCTC 9633;
RX   MEDLINE=97208874; PubMed=9055816; DOI=10.1016/S0378-1119(96)00642-7;
RA   Achenbach L.A., Yang W.;
RT   "The fur gene from Klebsiella pneumoniae: characterization, genomic
RT   organization and phylogenetic analysis.";
RL   Gene 185:201-207(1997).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- INDUCTION: By low iron conditions and by heat shock. Iron
CC       regulation is mediated through the fur protein.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; U67169; AAB65080.1; -; Genomic_DNA.
DR   EMBL; L23871; AAB51076.1; -; Genomic_DNA.
DR   ProteinModelPortal; O07026; -.
DR   SMR; O07026; 2-176.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    176       Flavodoxin.
FT                                /FTId=PRO_0000171636.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   176 AA;  19765 MW;  C40E5F80287D3636 CRC64;
     MAIIGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAHDIL LLGIPTWYYG
     EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW
     PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTNERVEKW VKQVAEELHL EEIKNA
//
ID   FLAV_MEGEL              Reviewed;         137 AA.
AC   P00321;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   18-APR-2012, entry version 66.
DE   RecName: Full=Flavodoxin;
OS   Megasphaera elsdenii.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=907;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927;
RX   MEDLINE=73197809; PubMed=4711610;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.;
RT   "The primary structure of Peptostreptococcus elsdenii flavodoxin.";
RL   J. Biol. Chem. 248:4354-4366(1973).
RN   [2]
RP   SEQUENCE REVISION TO 78-82.
RX   MEDLINE=74277393; PubMed=4843143;
RA   Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.;
RT   "Correction of the amino acid sequence of Peptostreptococcus elsdenii
RT   flavodoxin.";
RL   J. Biol. Chem. 249:4397-4397(1974).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-41 AND 136-137.
RC   STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927;
RX   MEDLINE=72062407; PubMed=5126921; DOI=10.1021/bi00792a009;
RA   Tanaka M., Haniu M., Matsueda G., Yasunobu K.T., Mayhew S., Massey V.;
RT   "Amino- and carboxyl-terminal amino acid sequences of the
RT   Peptostreptococcus eisdenii and Clostridium pasteurianum
RT   flavodoxins.";
RL   Biochemistry 10:3041-3046(1971).
RN   [4]
RP   STRUCTURE BY NMR.
RX   MEDLINE=90276429; PubMed=2161759;
RX   DOI=10.1111/j.1432-1033.1990.tb15527.x;
RA   van Mierlo C.P.M., Mueller F., Vervoort J.;
RT   "Secondary and tertiary structure characteristics of Megasphaera
RT   elsdenii flavodoxin in the reduced state as determined by two-
RT   dimensional 1H NMR.";
RL   Eur. J. Biochem. 189:589-600(1990).
RN   [5]
RP   STRUCTURE BY NMR.
RX   MEDLINE=91071190; PubMed=2253614;
RX   DOI=10.1111/j.1432-1033.1990.tb19444.x;
RA   van Mierlo C.P.M., Lijnzaad P., Vervoort J., Mueller F.,
RA   Berendsen H.J.C., de Vlieg J.;
RT   "Tertiary structure of two-electron reduced Megasphaera elsdenii
RT   flavodoxin and some implications, as determined by two-dimensional 1H-
RT   NMR and restrained molecular dynamics.";
RL   Eur. J. Biochem. 194:185-198(1990).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   PIR; A92137; FXME.
DR   PDB; 2FZ5; NMR; -; A=1-137.
DR   PDBsum; 2FZ5; -.
DR   ProteinModelPortal; P00321; -.
DR   SMR; P00321; 1-137.
DR   EvolutionaryTrace; P00321; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Transport.
FT   CHAIN         1    137       Flavodoxin.
FT                                /FTId=PRO_0000171639.
FT   DOMAIN        2    137       Flavodoxin-like.
FT   STRAND        2      6
FT   STRAND        9     11
FT   HELIX        12     26
FT   STRAND       31     35
FT   HELIX        41     45
FT   STRAND       48     53
FT   TURN         58     60
FT   HELIX        64     74
FT   HELIX        75     77
FT   STRAND       82     91
FT   HELIX        95    106
FT   STRAND      110    123
FT   HELIX       126    135
SQ   SEQUENCE   137 AA;  14550 MW;  86BD744412D6F869 CRC64;
     MVEIVYWSGT GNTEAMANEI EAAVKAAGAD VESVRFEDTN VDDVASKDVI LLGCPAMGSE
     ELEDSVVEPF FTDLAPKLKG KKVGLFGSYG WGSGEWMDAW KQRTEDTGAT VIGTAIVNEM
     PDNAPECKEL GEAAAKA
//
ID   FLAV_NOSSM              Reviewed;          35 AA.
AC   P35707;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   19-JAN-2010, entry version 39.
DE   RecName: Full=Flavodoxin;
DE   Flags: Fragment;
OS   Nostoc sp. (strain MAC).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=35822;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.;
RT   "N-terminal amino acid sequences of flavodoxins from Chondrus crispus
RT   and Nostoc strain MAC.";
RL   Phytochemistry 25:2113-2115(1986).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Flavoprotein; FMN;
KW   Transport.
FT   CHAIN         1    >35       Flavodoxin.
FT                                /FTId=PRO_0000171640.
FT   DOMAIN        4    >35       Flavodoxin-like.
FT   NON_TER      35     35
SQ   SEQUENCE   35 AA;  3820 MW;  B6EEB5CA7A45DDA6 CRC64;
     SKKIGLFYGT ZTGKTESVAE IIDEFGDEVV TLDID
//
ID   FLAV_RHOCB              Reviewed;         182 AA.
AC   P52967; D5AT59;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 3.
DT   16-MAY-2012, entry version 62.
DE   RecName: Full=Flavodoxin;
GN   Name=nifF; Synonyms=fldA; OrderedLocusNames=RCAP_rcc01421;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   MEDLINE=96272272; PubMed=8682802;
RA   Gennaro G., Huebner P., Sandmeier U., Yakunin A.F., Hallenbeck P.C.;
RT   "Cloning, characterization, and regulation of nifF from Rhodobacter
RT   capsulatus.";
RL   J. Bacteriol. 178:3949-3952(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/JB.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur
RT   bacterium Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes. NifF is the electron donor to nitrogenase.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; L42290; AAC05792.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE85166.1; -; Genomic_DNA.
DR   RefSeq; YP_003577573.1; NC_014034.1.
DR   PDB; 2WC1; X-ray; 2.17 A; A=1-182.
DR   PDBsum; 2WC1; -.
DR   ProteinModelPortal; P52967; -.
DR   GeneID; 9004244; -.
DR   KEGG; rcp:RCAP_rcc01421; -.
DR   PATRIC; 35502944; VBIRhoCap134200_1432.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   EvolutionaryTrace; P52967; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Electron transport; Flavoprotein;
KW   FMN; Nitrogen fixation; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    182       Flavodoxin.
FT                                /FTId=PRO_0000171641.
FT   DOMAIN        4    173       Flavodoxin-like.
FT   CONFLICT    124    125       KL -> NV (in Ref. 1; AAC05792).
FT   STRAND        6      8
FT   HELIX        15     23
FT   TURN         28     30
FT   STRAND       31     36
FT   HELIX        37     39
FT   HELIX        42     47
FT   STRAND       49     53
FT   HELIX        75     78
FT   HELIX        79     82
FT   STRAND       91     94
FT   TURN        100    102
FT   TURN        107    109
FT   HELIX       110    119
FT   STRAND      124    126
FT   TURN        154    156
FT   HELIX       158    160
FT   HELIX       161    165
FT   TURN        169    175
SQ   SEQUENCE   182 AA;  19848 MW;  955F326BBF27213E CRC64;
     MAKIGLFFGS DTGTTRKIAK QIKDMFDDEV MAKPLNVNRA DVADFMAYDF LILGTPTLGD
     GQLPGLSANA ASESWEEFLP RIADQDFSGK TIALFGLGDQ VTYPLEFVNA LFFLHEFFSD
     RGAKLVGRWP AKGYGFEDSL AVVEGEFLGL ALDQDNQAAL TPERLKGWLS LIAADFGLVL
     PA
//
ID   FLAV_SYNE7              Reviewed;         170 AA.
AC   P10340; Q31MZ8;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-MAY-2012, entry version 97.
DE   RecName: Full=Flavodoxin;
GN   Name=isiB; OrderedLocusNames=Synpcc7942_1541;
OS   Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=1140;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88086879; PubMed=3121586;
RA   Laudenbach D.E., Reith M.E., Straus N.A.;
RT   "Isolation, sequence analysis, and transcriptional studies of the
RT   flavodoxin gene from Anacystis nidulans R2.";
RL   J. Bacteriol. 170:258-265(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7942;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of chromosome 1 of Synechococcus elongatus PCC
RT   7942.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 2-56, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX   MEDLINE=83216115; PubMed=6406674; DOI=10.1016/S0022-2836(83)80277-0;
RA   Smith W.W., Pattridge K.A., Ludwig M.L., Petsko G.A., Tsernoglou D.,
RA   Tanaka M., Yasunobu K.T.;
RT   "Structure of oxidized flavodoxin from Anacystis nidulans.";
RL   J. Mol. Biol. 165:737-753(1983).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   MEDLINE=20079529; PubMed=10610791; DOI=10.1006/jmbi.1999.3151;
RA   Drennan C.L., Pattridge K.A., Weber C.H., Metzger A.L., Hoover D.M.,
RA   Ludwig M.L.;
RT   "Refined structures of oxidized flavodoxin from Anacystis nidulans.";
RL   J. Mol. Biol. 294:711-724(1999).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS).
RX   MEDLINE=20079530; PubMed=10610792; DOI=10.1006/jmbi.1999.3152;
RA   Hoover D.M., Drennan C.L., Metzger A.L., Osborne C., Weber C.H.,
RA   Pattridge K.A., Ludwig M.L.;
RT   "Comparisons of wild-type and mutant flavodoxins from Anacystis
RT   nidulans. Structural determinants of the redox potentials.";
RL   J. Mol. Biol. 294:725-743(1999).
RN   [6]
RP   STRUCTURE BY NMR.
RX   MEDLINE=91329335; PubMed=1907844; DOI=10.1021/bi00245a008;
RA   Clubb R.T., Thanabal V., Osborne C., Wagner G.;
RT   "1H and 15N resonance assignments of oxidized flavodoxin from
RT   Anacystis nidulans with 3D NMR.";
RL   Biochemistry 30:7718-7730(1991).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- INDUCTION: By iron stress.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M19116; AAA22050.1; -; Genomic_DNA.
DR   EMBL; CP000100; ABB57571.1; -; Genomic_DNA.
DR   RefSeq; YP_170711.1; NC_006576.1.
DR   RefSeq; YP_400558.1; NC_007604.1.
DR   PDB; 1CZH; X-ray; 1.86 A; A=2-170.
DR   PDB; 1CZK; X-ray; 1.90 A; A=2-170.
DR   PDB; 1CZL; X-ray; 1.80 A; A=2-170.
DR   PDB; 1CZN; X-ray; 1.70 A; A=2-170.
DR   PDB; 1CZO; X-ray; 1.85 A; A=2-170.
DR   PDB; 1CZR; X-ray; 1.90 A; A=2-170.
DR   PDB; 1CZU; X-ray; 2.00 A; A=2-170.
DR   PDB; 1D03; X-ray; 1.85 A; A=2-170.
DR   PDB; 1D04; X-ray; 1.85 A; A=2-170.
DR   PDB; 1OFV; X-ray; 1.70 A; A=2-170.
DR   PDBsum; 1CZH; -.
DR   PDBsum; 1CZK; -.
DR   PDBsum; 1CZL; -.
DR   PDBsum; 1CZN; -.
DR   PDBsum; 1CZO; -.
DR   PDBsum; 1CZR; -.
DR   PDBsum; 1CZU; -.
DR   PDBsum; 1D03; -.
DR   PDBsum; 1D04; -.
DR   PDBsum; 1OFV; -.
DR   ProteinModelPortal; P10340; -.
DR   SMR; P10340; 2-170.
DR   STRING; P10340; -.
DR   GeneID; 3199676; -.
DR   GeneID; 3774965; -.
DR   GenomeReviews; CP000100_GR; Synpcc7942_1541.
DR   KEGG; syc:syc0001_c; -.
DR   KEGG; syf:Synpcc7942_1541; -.
DR   PATRIC; 23788451; VBISynElo51371_1750.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   ProtClustDB; PRK09267; -.
DR   BioCyc; SYNEL:SYNPCC7942_1541-MONOMER; -.
DR   EvolutionaryTrace; P10340; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Electron transport; Flavoprotein; FMN; Stress response; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    170       Flavodoxin.
FT                                /FTId=PRO_0000171644.
FT   DOMAIN        4    165       Flavodoxin-like.
FT   CONFLICT     55     55       C -> S (in Ref. 3; AA sequence).
FT   STRAND        4      8
FT   STRAND       11     13
FT   HELIX        14     26
FT   TURN         29     31
FT   STRAND       32     36
FT   HELIX        37     39
FT   HELIX        42     47
FT   STRAND       49     54
FT   TURN         59     61
FT   HELIX        65     70
FT   HELIX        71     76
FT   STRAND       83     89
FT   TURN         92     97
FT   HELIX       101    111
FT   TURN        112    114
FT   STRAND      121    123
FT   STRAND      138    144
FT   TURN        146    148
FT   HELIX       150    152
FT   HELIX       153    168
SQ   SEQUENCE   170 AA;  18778 MW;  7291AEF23DCA0345 CRC64;
     MAKIGLFYGT QTGVTQTIAE SIQQEFGGES IVDLNDIANA DASDLNAYDY LIIGCPTWNV
     GELQSDWEGI YDDLDSVNFQ GKKVAYFGAG DQVGYSDNFQ DAMGILEEKI SSLGSQTVGY
     WPIEGYDFNE SKAVRNNQFV GLAIDEDNQP DLTKNRIKTW VSQLKSEFGL
//
ID   FLAV_SYNP2              Reviewed;         170 AA.
AC   P31158; B1XL33;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-MAY-2012, entry version 69.
DE   RecName: Full=Flavodoxin;
GN   Name=isiB; OrderedLocusNames=SYNPCC7002_A1291;
OS   Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS   quadruplicatum).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechococcus.
OX   NCBI_TaxID=32049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92407507; PubMed=1527503;
RA   Leonhardt K.G., Straus N.A.;
RT   "An iron stress operon involved in photosynthetic electron transport
RT   in the marine cyanobacterium Synechococcus sp. PCC 7002.";
RL   J. Gen. Microbiol. 138:1613-1621(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA   Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA   Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C.,
RA   Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT   "Complete sequence of Synechococcus sp. PCC 7002.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- INDUCTION: By iron stress.
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; M88253; AAA27318.1; -; Genomic_DNA.
DR   EMBL; CP000951; ACA99288.1; -; Genomic_DNA.
DR   RefSeq; YP_001734544.1; NC_010475.1.
DR   ProteinModelPortal; P31158; -.
DR   SMR; P31158; 2-170.
DR   STRING; P31158; -.
DR   GeneID; 6055593; -.
DR   GenomeReviews; CP000951_GR; SYNPCC7002_A1291.
DR   KEGG; syp:SYNPCC7002_A1291; -.
DR   PATRIC; 23817150; VBISynSp37135_1525.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   OMA; FTETAGY; -.
DR   ProtClustDB; PRK09267; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Electron transport; Flavoprotein; FMN;
KW   Stress response; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    170       Flavodoxin.
FT                                /FTId=PRO_0000171643.
FT   DOMAIN        4    165       Flavodoxin-like.
SQ   SEQUENCE   170 AA;  18479 MW;  FFBB605F69E701BA CRC64;
     MSKIGLFFGT QTGNTEELAQ AIQAAFGGSD IVELFDVAEV DIEALRDFDQ LIIGCPTWNV
     GELQSDWEAL YDDLDDVDFS GKTIAYFGAG DQVGYADNFQ DAMGVLEEKI TSLGGKTVGQ
     WPTAGYDHSE SKAERDGKFV GLAIDEDNQP ELTAERIQAW VAQLKPAFGL
//
ID   FLAV_SYNY3              Reviewed;         170 AA.
AC   P27319;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   13-JUN-2012, entry version 88.
DE   RecName: Full=Flavodoxin;
GN   Name=isiB; OrderedLocusNames=sll0248;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Chroococcales; Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94320780; PubMed=8045418; DOI=10.1016/0378-1119(94)90342-5;
RA   Poncelet M.G.M., Cassier-Chauvat C.J.S., Chauvat F.R.L.;
RT   "Sequence of the flavodoxin-encoding gene from the cyanobacterium
RT   Synechocystis PCC6803.";
RL   Gene 145:153-154(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA   Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA   Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA   Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT   entire genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-42.
RX   MEDLINE=92338182; PubMed=1633177; DOI=10.1016/0167-4838(92)90465-P;
RA   Bottin H., Lagoutte B.;
RT   "Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp
RT   PCC 6803.";
RL   Biochim. Biophys. Acta 1101:48-56(1992).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes.
CC   -!- COFACTOR: FMN.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) are -433 mV and -238 mV;
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
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DR   EMBL; Z27091; CAA81614.1; -; Genomic_DNA.
DR   EMBL; L25881; AAA27288.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA17947.1; -; Genomic_DNA.
DR   PIR; S38632; S38632.
DR   RefSeq; NP_441267.1; NC_000911.1.
DR   RefSeq; YP_005651324.1; NC_017277.1.
DR   ProteinModelPortal; P27319; -.
DR   SMR; P27319; 3-165.
DR   STRING; P27319; -.
DR   GeneID; 12255742; -.
DR   GeneID; 954609; -.
DR   GenomeReviews; BA000022_GR; sll0248.
DR   KEGG; syn:sll0248; -.
DR   PATRIC; 23839886; VBISynSp132158_1504.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   OMA; DDKHFVG; -.
DR   ProtClustDB; PRK09267; -.
DR   BioCyc; SSP1148:SLL0248-MONOMER; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Reference proteome; Transport.
FT   CHAIN         1    170       Flavodoxin.
FT                                /FTId=PRO_0000171645.
FT   DOMAIN        4    165       Flavodoxin-like.
FT   CONFLICT      2      2       Missing (in Ref. 3; AA sequence).
FT   CONFLICT     40     40       A -> AA (in Ref. 3; AA sequence).
SQ   SEQUENCE   170 AA;  18822 MW;  B2937F347796BBD9 CRC64;
     MTKIGLFYGT QTGNTETIAE LIQKEMGGDS VVDMMDISQA DVDDFRQYSC LIIGCPTWNV
     GELQSDWEGF YDQLDEIDFN GKKVAYFGAG DQVGYADNFQ DAMGILEEKI SGLGGKTVGF
     WPTAGYDFDE SKAVKNGKFV GLALDEDNQP ELTELRVKTW VSEIKPILQS
//
ID   FLAV_TREPA              Reviewed;         146 AA.
AC   O83895;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-MAY-2012, entry version 67.
DE   RecName: Full=Flavodoxin;
GN   Name=fldA; OrderedLocusNames=TP_0925;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AE000520; AAC65882.1; -; Genomic_DNA.
DR   PIR; F71263; F71263.
DR   RefSeq; NP_219360.1; NC_000919.1.
DR   ProteinModelPortal; O83895; -.
DR   IntAct; O83895; 2.
DR   GeneID; 2611211; -.
DR   GenomeReviews; AE000520_GR; TP_0925.
DR   KEGG; tpa:TP0925; -.
DR   PATRIC; 20531963; VBITrePal57110_0977.
DR   TIGR; TP_0925; -.
DR   eggNOG; COG0716; -.
DR   OMA; FGSYDWG; -.
DR   ProtClustDB; CLSK218926; -.
DR   BioCyc; TPAL243276:TP_0925-MONOMER; -.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010087; Flav_short.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001226; Flavodoxin_CS.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01753; Flav_short; 1.
DR   PROSITE; PS00201; FLAVODOXIN; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    146       Flavodoxin.
FT                                /FTId=PRO_0000171646.
FT   DOMAIN        4    145       Flavodoxin-like.
SQ   SEQUENCE   146 AA;  15793 MW;  398A7D7C8530F2CE CRC64;
     MAKVAVIFWS GTGHTETMAR CIVEGLNVGG AKADLFSVMD FDVGTFDSYD RFAFGCSAAG
     SEELESSEFE PFFTSIEGRL SGKKVALFGS YEWAGEGEGG EWMVNWVERC KAAGADVFEG
     KGEIAYDDPS EEAQASCKAF GERFAR
//
ID   FLAV_TRIEI              Reviewed;         171 AA.
AC   O52659; Q114Y7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   16-MAY-2012, entry version 63.
DE   RecName: Full=Flavodoxin;
GN   Name=fld; OrderedLocusNames=Tery_1666;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriales; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-146.
RA   Lin S., Carpenter E.J.;
RT   "Identification of a gene encoding flavodoxin in the marine
RT   cyanobacterium Trichodesmium.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Low-potential electron donor to a number of redox
CC       enzymes (By similarity).
CC   -!- COFACTOR: FMN (By similarity).
CC   -!- SIMILARITY: Belongs to the flavodoxin family.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; CP000393; ABG50937.1; -; Genomic_DNA.
DR   EMBL; AF044318; AAC02683.1; -; Genomic_DNA.
DR   RefSeq; YP_721410.1; NC_008312.1.
DR   ProteinModelPortal; O52659; -.
DR   SMR; O52659; 3-171.
DR   GeneID; 4245460; -.
DR   GenomeReviews; CP000393_GR; Tery_1666.
DR   KEGG; ter:Tery_1666; -.
DR   PATRIC; 23987341; VBITriEry99848_2106.
DR   eggNOG; COG0716; -.
DR   HOGENOM; HOG000030543; -.
DR   KO; K03839; -.
DR   OMA; DDKHFVG; -.
DR   ProtClustDB; PRK09267; -.
DR   BioCyc; TERY203124:TERY_1666-MONOMER; -.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR010086; Flavodoxin_lc.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   TIGRFAMs; TIGR01752; Flav_long; 1.
DR   PROSITE; PS00201; FLAVODOXIN; FALSE_NEG.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Electron transport; Flavoprotein; FMN; Transport.
FT   CHAIN         1    171       Flavodoxin.
FT                                /FTId=PRO_0000171647.
FT   DOMAIN        4    166       Flavodoxin-like.
FT   CONFLICT      4      4       I -> M (in Ref. 2; AAC02683).
FT   CONFLICT      8      8       V -> F (in Ref. 2; AAC02683).
FT   CONFLICT    130    130       E -> V (in Ref. 2; AAC02683).
SQ   SEQUENCE   171 AA;  18742 MW;  677F643438653126 CRC64;
     MSKIGLFVGT TTGKTEEAAE KIKEEFGGDD VVTIHDISEA SPEDFDGYQN VIIGCPTWDV
     GELQSDWSGF YSEELDNVKF TGKKVAYFGT GDQIGYADNF QDAMGILEEK ITGLGGTTIG
     SWSTEGYDHE DSKAVKNGKF VGLALDDDNQ ADLTDERIKE WVKQLKTEFG V
//
ID   FLS1_ARATH              Reviewed;         336 AA.
AC   Q96330; O04730; O04731; O04732; O04830; O04831; O04832;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   13-JUN-2012, entry version 91.
DE   RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE            EC=1.14.11.23;
DE            EC=1.14.11.9;
DE   AltName: Full=FLS 1;
GN   Name=FLS1; Synonyms=FLS; OrderedLocusNames=At5g08640;
GN   ORFNames=MAH20.20;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY LIGHT.
RC   STRAIN=cv. Landsberg erecta;
RX   MEDLINE=97267154; PubMed=9112784; DOI=10.1104/pp.113.4.1437;
RA   Pelletier M.K., Murrell J.R., Shirley B.W.;
RT   "Characterization of flavonol synthase and leucoanthocyanidin
RT   dioxygenase genes in Arabidopsis. Further evidence for differential
RT   regulation of 'early' and 'late' genes.";
RL   Plant Physiol. 113:1437-1445(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INDUCTION BY
RP   LIGHT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX   MEDLINE=98445388; PubMed=9770503; DOI=10.1073/pnas.95.21.12432;
RA   Wisman E., Hartmann U., Sagasser M., Baumann E., Palme K.,
RA   Hahlbrock K., Saedler H., Weisshaar B.;
RT   "Knock-out mutants from an En-1 mutagenized Arabidopsis thaliana
RT   population generate phenylpropanoid biosynthesis phenotypes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12432-12437(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=98069011; PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA   Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. II.
RT   Sequence features of the regions of 1,044,062 bp covered by thirteen
RT   physically assigned P1 clones.";
RL   DNA Res. 4:291-300(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=10394944;
RA   Pelletier M.K., Burbulis I.E., Winkel-Shirley B.;
RT   "Disruption of specific flavonoid genes enhances the accumulation of
RT   flavonoid enzymes and end-products in Arabidopsis seedlings.";
RL   Plant Mol. Biol. 40:45-54(1999).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=12126705;
RA   Prescott A.G., Stamford N.P., Wheeler G., Firmin J.L.;
RT   "In vitro properties of a recombinant flavonol synthase from
RT   Arabidopsis thaliana.";
RL   Phytochemistry 60:589-593(2002).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16153644; DOI=10.1016/j.febslet.2005.08.033;
RA   Welford R.W., Kirkpatrick J.M., McNeill L.A., Puri M., Oldham N.J.,
RA   Schofield C.J.;
RT   "Incorporation of oxygen into the succinate co-product of iron(II) and
RT   2-oxoglutarate dependent oxygenases from bacteria, plants and
RT   humans.";
RL   FEBS Lett. 579:5170-5174(2005).
RN   [10]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15821875; DOI=10.1007/s11103-004-6910-0;
RA   Hartmann U., Sagasser M., Mehrtens F., Stracke R., Weisshaar B.;
RT   "Differential combinatorial interactions of cis-acting elements
RT   recognized by R2R3-MYB, BZIP, and BHLH factors control light-
RT   responsive and tissue-specific activation of phenylpropanoid
RT   biosynthesis genes.";
RL   Plant Mol. Biol. 57:155-171(2005).
RN   [11]
RP   FUNCTION, AND MUTAGENESIS OF HIS-132 AND LYS-329.
RX   PubMed=16106293; DOI=10.1039/b507153d;
RA   Welford R.W., Clifton I.J., Turnbull J.J., Wilson S.C.,
RA   Schofield C.J.;
RT   "Structural and mechanistic studies on anthocyanidin synthase
RT   catalysed oxidation of flavanone substrates: the effect of C-2
RT   stereochemistry on product selectivity and mechanism.";
RL   Org. Biomol. Chem. 3:3117-3126(2005).
RN   [12]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-132;
RP   PHE-134; LYS-202; HIS-221; ASP-223; HIS-277; ARG-287; SER-289; PHE-293
RP   AND GLU-295.
RX   PubMed=17719613; DOI=10.1016/j.phytochem.2007.07.006;
RA   Chua C.S., Biermann D., Goo K.S., Sim T.S.;
RT   "Elucidation of active site residues of Arabidopsis thaliana flavonol
RT   synthase provides a molecular platform for engineering flavonols.";
RL   Phytochemistry 69:66-75(2008).
RN   [13]
RP   FUNCTION, TISSUE SPECIFICITY, GENE FAMILY, NOMENCLATURE, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=18467451; DOI=10.1104/pp.108.117457;
RA   Owens D.K., Alerding A.B., Crosby K.C., Bandara A.B., Westwood J.H.,
RA   Winkel B.S.;
RT   "Functional analysis of a predicted flavonol synthase gene family in
RT   Arabidopsis.";
RL   Plant Physiol. 147:1046-1061(2008).
RN   [14]
RP   FUNCTION.
RX   PubMed=19433090; DOI=10.1016/j.febslet.2009.05.006;
RA   Preuss A., Stracke R., Weisshaar B., Hillebrecht A., Matern U.,
RA   Martens S.;
RT   "Arabidopsis thaliana expresses a second functional flavonol
RT   synthase.";
RL   FEBS Lett. 583:1981-1986(2009).
RN   [15]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. No-0;
RX   PubMed=18998159; DOI=10.1007/s00425-008-0841-y;
RA   Stracke R., De Vos R.C., Bartelniewoehner L., Ishihara H.,
RA   Sagasser M., Martens S., Weisshaar B.;
RT   "Metabolomic and genetic analyses of flavonol synthesis in Arabidopsis
RT   thaliana support the in vivo involvement of leucoanthocyanidin
RT   dioxygenase.";
RL   Planta 229:427-445(2009).
RN   [16]
RP   INDUCTION.
RX   PubMed=21427279; DOI=10.1104/pp.111.172502;
RA   Lewis D.R., Ramirez M.V., Miller N.D., Vallabhaneni P., Ray W.K.,
RA   Helm R.F., Winkel B.S., Muday G.K.;
RT   "Auxin and ethylene induce flavonol accumulation through distinct
RT   transcriptional networks.";
RL   Plant Physiol. 156:144-164(2011).
RN   [17]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21502189; DOI=10.1104/pp.111.175976;
RA   Kuhn B.M., Geisler M., Bigler L., Ringli C.;
RT   "Flavonols accumulate asymmetrically and affect auxin transport in
RT   Arabidopsis.";
RL   Plant Physiol. 156:585-595(2011).
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin. In vitro catalyzes the
CC       oxidation of both enantiomers of naringenin to give both cis- and
CC       trans-dihydrokaempferol.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit.
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=59 uM for dihydroquercetin.;
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in young seedlings (at protein
CC       level). Expressed in roots, emerging leaves, shoot-root transition
CC       zone, trichomes, flowers and siliques. In cotyledons, expressed
CC       mostly on the adaxial side and only in guard cells on the abaxial
CC       side.
CC   -!- INDUCTION: By light, auxin and 1-aminocyclopropane-1-carboxylic
CC       acid (ACC).
CC   -!- DISRUPTION PHENOTYPE: Accumulation of anthocyanins and
CC       glycosylated forms of dihydroflavonols, and drastic reduction of
CC       kaempferol, quercitin and favonol glycosides.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
CC   -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain.
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DR   EMBL; U72631; AAB17393.1; -; Genomic_DNA.
DR   EMBL; U84258; AAC69362.1; -; Genomic_DNA.
DR   EMBL; U84259; AAC69363.1; -; mRNA.
DR   EMBL; U84260; AAB41504.1; -; mRNA.
DR   EMBL; AB006697; BAB10013.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91332.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED91333.1; -; Genomic_DNA.
DR   EMBL; AY058068; AAL24176.1; -; mRNA.
DR   EMBL; BT000494; AAN18063.1; -; mRNA.
DR   EMBL; AY086328; AAM64397.1; -; mRNA.
DR   IPI; IPI00532962; -.
DR   RefSeq; NP_001190266.1; NM_001203337.1.
DR   RefSeq; NP_196481.1; NM_120951.2.
DR   UniGene; At.8771; -.
DR   ProteinModelPortal; Q96330; -.
DR   SMR; Q96330; 2-334.
DR   IntAct; Q96330; 3.
DR   STRING; Q96330; -.
DR   PRIDE; Q96330; -.
DR   ProMEX; Q96330; -.
DR   EnsemblPlants; AT5G08640; AT5G08640; AT5G08640.
DR   GeneID; 830765; -.
DR   GenomeReviews; BA000015_GR; AT5G08640.
DR   KEGG; ath:AT5G08640; -.
DR   TAIR; At5g08640; -.
DR   eggNOG; COG3491; -.
DR   InParanoid; Q96330; -.
DR   KO; K05278; -.
DR   OMA; EWGLFQV; -.
DR   PhylomeDB; Q96330; -.
DR   ProtClustDB; PLN02704; -.
DR   ArrayExpress; Q96330; -.
DR   Genevestigator; Q96330; -.
DR   GermOnline; AT5G08640; Arabidopsis thaliana.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045431; F:flavonol synthase activity; IDA:TAIR.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   GO; GO:0009733; P:response to auxin stimulus; IEP:TAIR.
DR   GO; GO:0080167; P:response to karrikin; IEP:TAIR.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Dioxygenase; Flavonoid biosynthesis;
KW   Iron; Metal-binding; Nucleus; Oxidoreductase; Reference proteome;
KW   Vitamin C.
FT   CHAIN         1    336       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067291.
FT   DOMAIN      196    296       Fe2OG dioxygenase.
FT   REGION      204    206       2-oxoglutarate binding (By similarity).
FT   REGION      287    289       2-oxoglutarate binding (Probable).
FT   METAL       221    221       Iron; catalytic (Probable).
FT   METAL       223    223       Iron; catalytic (Probable).
FT   METAL       277    277       Iron; catalytic (Probable).
FT   MUTAGEN     132    132       H->F: Slightly increases activity.
FT   MUTAGEN     132    132       H->Y: Slightly decreases activity.
FT   MUTAGEN     134    134       F->A: Reduces activity 7-fold.
FT   MUTAGEN     134    134       F->L: Reduces activity 2-fold.
FT   MUTAGEN     202    202       K->M: Reduces activity 25-fold.
FT   MUTAGEN     202    202       K->R: Reduces activity 8-fold.
FT   MUTAGEN     221    221       H->W: Loss of activity.
FT   MUTAGEN     223    223       D->E: Loss of activity.
FT   MUTAGEN     277    277       H->F: Loss of activity.
FT   MUTAGEN     287    287       R->K: Loss of activity.
FT   MUTAGEN     289    289       S->T: Reduces activity 2-fold.
FT   MUTAGEN     293    293       F->A,L: Reduces activity 12-fold.
FT   MUTAGEN     295    295       E->L: Reduces activity 15-fold.
FT   MUTAGEN     295    295       E->Q: Reduces activity 2-fold.
FT   MUTAGEN     329    329       K->N: Reduces activity 4-fold.
SQ   SEQUENCE   336 AA;  38282 MW;  3283E3AFE603D2A9 CRC64;
     MEVERVQDIS SSSLLTEAIP LEFIRSEKEQ PAITTFRGPT PAIPVVDLSD PDEESVRRAV
     VKASEEWGLF QVVNHGIPTE LIRRLQDVGR KFFELPSSEK ESVAKPEDSK DIEGYGTKLQ
     KDPEGKKAWV DHLFHRIWPP SCVNYRFWPK NPPEYREVNE EYAVHVKKLS ETLLGILSDG
     LGLKRDALKE GLGGEMAEYM MKINYYPPCP RPDLALGVPA HTDLSGITLL VPNEVPGLQV
     FKDDHWFDAE YIPSAVIVHI GDQILRLSNG RYKNVLHRTT VDKEKTRMSW PVFLEPPREK
     IVGPLPELTG DDNPPKFKPF AFKDYSYRKL NKLPLD
//
ID   FLS_MATIN               Reviewed;         291 AA.
AC   O04395;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   13-JUN-2012, entry version 63.
DE   RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE            Short=FLS;
DE            EC=1.14.11.23;
DE            EC=1.14.11.9;
DE   Flags: Fragment;
OS   Matthiola incana (Common stock) (Cheiranthus incanus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; malvids; Brassicales; Brassicaceae; Anchonieae; Matthiola.
OX   NCBI_TaxID=3724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Flower bud, and Petal;
RA   Henkel J., Forkmann G.;
RT   "Cloning and expression of a flavonol synthase gene from common stock
RT   (Matthiola incana).";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit.
CC   -!- COFACTOR: Binds 1 iron ion per subunit.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
CC   -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain.
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DR   EMBL; AF001391; AAB58800.1; -; mRNA.
DR   ProteinModelPortal; O04395; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:EC.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN        <1    291       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067295.
FT   DOMAIN      151    250       Fe2OG dioxygenase.
FT   METAL       175    175       Iron (By similarity).
FT   METAL       177    177       Iron (By similarity).
FT   METAL       231    231       Iron (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   291 AA;  33430 MW;  6B8E4E3D2834720A CRC64;
     QVPVVDLSCP DEELVARTVV KASEDWGVFQ VVNHGIPTEL IQRLQKVGRE FFELPEAEKR
     SCAREAGSVE GYGRRIELDI KKRKGIVDQI YLSTWPPSSV NYRYWPKSPP DYREVNEEYA
     RHVKTLSEKI MEWLSEGLGL GREAIKEVNG CWYVMNINHY PPYPHSDSFN GLEPHTDING
     LTLIITNEIP GLQVFKDDHW IEVEYIPSAI IVNIGDQIMM LSNGKYKNVL HKTTVDKEKT
     RMSWPVLVSP TYDMVVGPLP ELTSEDDPPK FKPIAYKDYV HNKITFLKNK S
//
ID   FLS_PETHY               Reviewed;         348 AA.
AC   Q07512;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-JUN-2012, entry version 66.
DE   RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE            Short=FLS;
DE            EC=1.14.11.23;
DE            EC=1.14.11.9;
GN   Name=FL;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Old Glory Blue; TISSUE=Petal;
RX   MEDLINE=94108485; PubMed=7904213;
RX   DOI=10.1046/j.1365-313X.1993.04061003.x;
RA   Holton T.A., Brugliera F., Tanaka Y.;
RT   "Cloning and expression of flavonol synthase from Petunia hybrida.";
RL   Plant J. 4:1003-1010(1993).
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit.
CC   -!- COFACTOR: Binds 1 iron ion per subunit.
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed at highest level during the first
CC       stage of flower development.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
CC   -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; Z22543; CAA80264.1; -; mRNA.
DR   PIR; S33510; S33510.
DR   ProteinModelPortal; Q07512; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   InterPro; IPR002283; Isopenicillin-N_synthase.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   PRINTS; PR00682; IPNSYNTHASE.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN         1    348       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067296.
FT   DOMAIN      209    309       Fe2OG dioxygenase.
FT   METAL       234    234       Iron (By similarity).
FT   METAL       236    236       Iron (By similarity).
FT   METAL       290    290       Iron (By similarity).
SQ   SEQUENCE   348 AA;  39427 MW;  B39E1E4381DE6379 CRC64;
     MKTAQGVSAT LTMEVARVQA IASLSKCMDT IPSEYIRSEN EQPAATTLHG VVLQVPVIDL
     RDPDENKMVK LIADASKEWG IFQLINHGIP DEAIADLQKV GKEFFEHVPQ EEKELIAKTP
     GSNDIEGYGT SLQKEVEGKK GWVDHLFHKI WPPSAVNYRY WPKNPPSYRE ANEEYGKRMR
     EVVDRIFKSL SLGLGLEGHE MIEAAGGDEI VYLLKINYYP PCPRPDLALG VVAHTDMSYI
     TILVPNEVQG LQVFKDGHWY DVKYIPNALI VHIGDQVEIL SNGKYKSVYH RTTVNKDKTR
     MSWPVFLEPP SEHEVGPIPK LLSEANPPKF KTKKYKDYVY CKLNKLPQ
//
ID   FLS_SOLTU               Reviewed;         349 AA.
AC   Q41452;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   13-JUN-2012, entry version 66.
DE   RecName: Full=Flavonol synthase/flavanone 3-hydroxylase;
DE            Short=FLS;
DE            EC=1.14.11.23;
DE            EC=1.14.11.9;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pistil;
RX   MEDLINE=97177800; PubMed=9025306;
RX   DOI=10.1046/j.1365-313X.1997.11010105.x;
RA   van Eldik G.J., Ruiter R.K., Reijnen W.H., van Herpen M.M.A.,
RA   Schrauwen J.A.M., Wullems G.J.;
RT   "Regulation of flavonol biosynthesis during anther and pistil
RT   development, and during pollen tube growth in Solanum tuberosum.";
RL   Plant J. 11:105-113(1997).
CC   -!- FUNCTION: Catalyzes the formation of flavonols from
CC       dihydroflavonols. It can act on dihydrokaempferol to produce
CC       kaempferol, on dihydroquercetin to produce quercitin and on
CC       dihydromyricetin to produce myricetin.
CC   -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a
CC       flavonol + succinate + CO(2) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a
CC       dihydroflavonol + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity).
CC   -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Temporally expressed during flower
CC       development.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family.
CC   -!- SIMILARITY: Contains 1 Fe2OG dioxygenase domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; X92178; CAA63092.1; -; mRNA.
DR   PIR; T07373; T07373.
DR   ProteinModelPortal; Q41452; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045431; F:flavonol synthase activity; IEA:EC.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN         1    349       Flavonol synthase/flavanone 3-
FT                                hydroxylase.
FT                                /FTId=PRO_0000067297.
FT   DOMAIN      213    310       Fe2OG dioxygenase.
FT   METAL       238    238       Iron (By similarity).
FT   METAL       240    240       Iron (By similarity).
FT   METAL       291    291       Iron (By similarity).
SQ   SEQUENCE   349 AA;  39728 MW;  ADBBC3F6B10A0E05 CRC64;
     MKTIQGQSAT TALTMEVARV QAISSITKCM DTIPSEYIRS ENEQPAATTL QGVVLEVPVI
     DISNVDDDEE KLVKEIVEAS KEWGIFQVIN HGIPDEVIEN LQKVGKEFFE EVPQEEKELI
     AKKPGAQSLE GYGTSLQKEI EGKKGWVDHL FHKIWPPSAI NYRYWPKNPP SYREANEEYA
     KWLRKVADGI FRSLSLGLGL EGHEMMEAAG SEDIVYMLKI NYYPPCPRPD LALGVVAHTD
     MSYITLLVPN EVQVFKDGHW YDVNYIPNAI IVHIGDQVEI LSNGKYKSVY HRTTVNKYKT
     RMSWPVFLEP SSEHEVGPIP NLINEANPPK FKTKKYKDYV YCKLNKLPQ
//
ID   FOS_TAKRU               Reviewed;         376 AA.
AC   P53450;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 67.
DE   RecName: Full=Proto-oncogene c-Fos;
DE   AltName: Full=Cellular oncogene fos;
GN   Name=fos;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96202283; PubMed=8643637; DOI=10.1073/pnas.93.4.1366;
RA   Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J.,
RA   Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R.,
RA   Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.;
RT   "Conservation of synteny between the genome of the pufferfish (Fugu
RT   rubripes) and the region on human chromosome 14 (14q24.3) associated
RT   with familial Alzheimer disease (AD3 locus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996).
CC   -!- FUNCTION: Nuclear phosphoprotein which forms a tight but non-
CC       covalently linked complex with the JUN/AP-1 transcription factor.
CC       FOS has a critical function in regulating the development of cells
CC       destined to form and maintain the skeleton. It is thought to have
CC       an important role in signal transduction, cell proliferation and
CC       differentiation (By similarity).
CC   -!- SUBUNIT: Heterodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U40757; AAC59778.1; -; Genomic_DNA.
DR   ProteinModelPortal; P53450; -.
DR   SMR; P53450; 123-182.
DR   STRING; P53450; -.
DR   eggNOG; NOG258795; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR011616; bZIP_1.
DR   InterPro; IPR000837; Leuzip_Fos.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PRINTS; PR00042; LEUZIPPRFOS.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
KW   Proto-oncogene; Reference proteome.
FT   CHAIN         1    376       Proto-oncogene c-Fos.
FT                                /FTId=PRO_0000076473.
FT   DOMAIN      149    177       Leucine-zipper.
FT   DNA_BIND    123    144       Basic motif.
SQ   SEQUENCE   376 AA;  40826 MW;  BFC28534431DB491 CRC64;
     MMFTSFNAEC DSSSRCSASP VGDNLYYPSP AGSYSSMGSP QSQDFTDLTA SSASFIPTVT
     AISTSPDLQW MVQPLISSVA PSHRAHPYSP SPSYKRTVMR SAASKAHGKR SRVEQTTPEE
     EEKKRIRRER NKQAAAKCRN RRRELTDTLQ AETDQLEDEK SSLQNDIANL LKEKERLEFI
     LAAHQPICKI PSQMDTDFSV VSMSPVHACL STTVSTQLQT SIPEATTVTS SHSTFTSTSN
     SIFSGSSDSL LSTATVSNSV VKMTDLDSSV LEESLDLLAK TEAETARSVP DVNLSNSLFA
     AQDWEPLHAT ISSSDFEPLC TPVVTCTPAC TTLTSSFVFT FPEAETFPTC GVAHRRRSNS
     NDQSSDSLSS PTLLAL
//
ID   G6PD_TAKRU              Reviewed;         530 AA.
AC   P54996;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 76.
DE   RecName: Full=Glucose-6-phosphate 1-dehydrogenase;
DE            Short=G6PD;
DE            EC=1.1.1.49;
GN   Name=g6pd;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95331796; PubMed=7607684; DOI=10.1016/0888-7543(95)80179-P;
RA   Mason P.J., Stevens D.J., Luzzatto L., Brenner S., Aparicio S.;
RT   "Genomic structure and sequence of the Fugu rubripes glucose-6-
RT   phosphate dehydrogenase gene (G6PD).";
RL   Genomics 26:587-591(1995).
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-
CC       glucono-1,5-lactone + NADPH.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
CC       step 1/3.
CC   -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
CC       family.
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DR   EMBL; X83611; CAA58590.2; -; Genomic_DNA.
DR   PIR; A56841; A56841.
DR   ProteinModelPortal; P54996; -.
DR   SMR; P54996; 43-530.
DR   GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   InterPro; IPR001282; G6P_DH.
DR   InterPro; IPR019796; G6P_DH_AS.
DR   InterPro; IPR022675; G6P_DH_C.
DR   InterPro; IPR022674; G6P_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   PANTHER; PTHR23429; G6PDH; 1.
DR   Pfam; PF02781; G6PD_C; 1.
DR   Pfam; PF00479; G6PD_N; 1.
DR   PIRSF; PIRSF000110; G6PD; 1.
DR   PRINTS; PR00079; G6PDHDRGNASE.
DR   TIGRFAMs; TIGR00871; Zwf; 1.
DR   PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Complete proteome; Glucose metabolism; NADP;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    530       Glucose-6-phosphate 1-dehydrogenase.
FT                                /FTId=PRO_0000068088.
FT   ACT_SITE    278    278       Proton acceptor (By similarity).
FT   BINDING      55     55       NADP (By similarity).
FT   BINDING      87     87       NADP (By similarity).
FT   BINDING     216    216       Substrate (By similarity).
FT   BINDING     220    220       Substrate (By similarity).
SQ   SEQUENCE   530 AA;  60469 MW;  FC73FB53D834EF29 CRC64;
     MMIILFNCFF CASFREDGQH PTVSLGGVWG AAKELHEDKE FHQSDVHVFI IMGASGDLAK
     KKIYPTLWWL FRDGLLPEQT YFVGFARSAL TVDAIRTSCM PYLKVTETES DRLSAFFSRN
     SYISGNYTAG GSFSELNAHI MSLPGASDAN RLFYLALPPT IYHSVTENIK HFCMSAKGWN
     RVIVEKPFGH DLQSSEELST HLSSLFTEDQ IYRIDHYLGK EMVQNLMVLR FGNRIFGPIW
     NRDNVACVVL TFKEPFGTQG RGGYFDDFGI IRDVMQNHML QMLCLVAMEK PASTNSDDVR
     DEKVKVLKCI VPASMSDVVL GQYVGDPEGE GDAKLGYLDD PTVPKGSTQA TFATVVLYVH
     NERWDGVPFI LRCGKALNER KAEVRLQFTD VPGDIFRNQC YRNELVVRVQ PNEAIYAKMM
     SKKPGVYFTP EETELDLTYK SRYKDVKLPD AYERLILDVF CGSQMHFVAS DELREAWRIF
     TPLLHQIEKE KPKPIPYKYG SRGPAEADEL EKRVGFRYEG TYKWVNPHRL
//
ID   GCN4_YEAST              Reviewed;         281 AA.
AC   P03069; D3DLN9; P03068; Q70D88; Q70D91; Q70D96; Q70D99; Q70DA0;
AC   Q96UT3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   13-JUN-2012, entry version 139.
DE   RecName: Full=General control protein GCN4;
DE   AltName: Full=Amino acid biosynthesis regulatory protein;
GN   Name=GCN4; Synonyms=AAS3, ARG9; OrderedLocusNames=YEL009C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=85038531; PubMed=6387704; DOI=10.1073/pnas.81.20.6442;
RA   Hinnebusch A.G.;
RT   "Evidence for translational regulation of the activator of general
RT   amino acid control in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84298088; PubMed=6433345; DOI=10.1073/pnas.81.16.5096;
RA   Thireos G., Penn M.D., Greer H.;
RT   "5' untranslated sequences are required for the translational control
RT   of a yeast regulatory gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-24; SER-62;
RP   ALA-82; ALA-91; ALA-125 AND GLU-196.
RC   STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556,
RC   CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17;
RX   PubMed=15087486; DOI=10.1093/nar/gkh529;
RA   Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S.,
RA   Souciet J.-L.;
RT   "Differential evolution of the Saccharomyces cerevisiae DUP240
RT   paralogs and implication of recombination in phylogeny.";
RL   Nucleic Acids Res. 32:2069-2078(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313264; PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RG   Saccharomyces Genome Database;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 249-281.
RX   PubMed=11896344; DOI=10.1046/j.1537-2995.2002.00018.x;
RA   Czerwinski M., Krop-Watorek A., Lisowska E., Spitalnik S.L.;
RT   "Construction of dimeric F(ab) useful in blood group serology.";
RL   Transfusion 42:257-264(2002).
RN   [7]
RP   DOMAINS.
RX   MEDLINE=87002456; PubMed=3530496; DOI=10.1016/0092-8674(86)90070-X;
RA   Hope I.A., Struhl K.;
RT   "Functional dissection of a eukaryotic transcriptional activator
RT   protein, GCN4 of yeast.";
RL   Cell 46:885-894(1986).
RN   [8]
RP   DOMAINS, AND MUTAGENESIS OF 97-PHE-PHE-98; MET-107; TYR-110; LEU-113
RP   AND 120-TRP--PHE-124.
RX   PubMed=7862116;
RA   Drysdale C.M., Duenas E., Jackson B.M., Reusser U., Braus G.H.,
RA   Hinnebusch A.G.;
RT   "The transcriptional activator GCN4 contains multiple activation
RT   domains that are critically dependent on hydrophobic amino acids.";
RL   Mol. Cell. Biol. 15:1220-1233(1995).
RN   [9]
RP   PHOSPHORYLATION AT THR-165.
RX   PubMed=12101234; DOI=10.1128/MCB.22.15.5395-5404.2002;
RA   Shemer R., Meimoun A., Holtzman T., Kornitzer D.;
RT   "Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5.";
RL   Mol. Cell. Biol. 22:5395-5404(2002).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-165 AND SER-218,
RP   AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281.
RX   MEDLINE=92054531; PubMed=1948029; DOI=10.1126/science.1948029;
RA   O'Shea E.K., Klemm J.D., Kim P.S., Alber T.;
RT   "X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel
RT   coiled coil.";
RL   Science 254:539-544(1991).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281.
RX   MEDLINE=93113690; PubMed=1473154; DOI=10.1016/S0092-8674(05)80070-4;
RA   Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C.;
RT   "The GCN4 basic region leucine zipper binds DNA as a dimer of
RT   uninterrupted alpha helices: crystal structure of the protein-DNA
RT   complex.";
RL   Cell 71:1223-1237(1992).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281.
RX   MEDLINE=99057965; PubMed=9837709; DOI=10.1006/jmbi.1998.2214;
RA   Eckert D.M., Malashkevich V.N., Kim P.S.;
RT   "Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried
RT   polar residues.";
RL   J. Mol. Biol. 284:859-865(1998).
RN   [14]
RP   STRUCTURE BY NMR OF 237-281.
RX   MEDLINE=91367802; PubMed=1891459; DOI=10.1093/protein/4.5.519;
RA   Saudek V., Pastore A., Morelli M.A., Frank R., Gausepohl H.,
RA   Gibson T.;
RT   "The solution structure of a leucine-zipper motif peptide.";
RL   Protein Eng. 4:519-529(1991).
CC   -!- FUNCTION: Is a transcription factor that is responsible for the
CC       activation of more than 30 genes required for amino acid or for
CC       purine biosynthesis in response to amino acid or purine
CC       starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA-
CC       3'.
CC   -!- SUBUNIT: Binds DNA as a dimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: Residues 89 to 100 and 106 to 125 define the N-terminal
CC       activation domain (NTAD) and the central acidic activation domain
CC       (CAAD) respectively, which can function independently to promote
CC       high-level transcription of the target genes.
CC   -!- PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation
CC       of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase
CC       complex SCF(Cdc4).
CC   -!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
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DR   EMBL; K02205; AAA34640.1; -; Genomic_DNA.
DR   EMBL; K02649; AAA65521.1; -; Genomic_DNA.
DR   EMBL; AJ585686; CAE52206.1; -; Genomic_DNA.
DR   EMBL; AJ585687; CAE52207.1; -; Genomic_DNA.
DR   EMBL; AJ585688; CAE52208.1; -; Genomic_DNA.
DR   EMBL; AJ585689; CAE52209.1; -; Genomic_DNA.
DR   EMBL; AJ585690; CAE52210.1; -; Genomic_DNA.
DR   EMBL; AJ585691; CAE52211.1; -; Genomic_DNA.
DR   EMBL; AJ585692; CAE52212.1; -; Genomic_DNA.
DR   EMBL; AJ585693; CAE52213.1; -; Genomic_DNA.
DR   EMBL; AJ585694; CAE52214.1; -; Genomic_DNA.
DR   EMBL; AJ585695; CAE52215.1; -; Genomic_DNA.
DR   EMBL; AJ585696; CAE52216.1; -; Genomic_DNA.
DR   EMBL; AJ585697; CAE52217.1; -; Genomic_DNA.
DR   EMBL; AJ585698; CAE52218.1; -; Genomic_DNA.
DR   EMBL; AJ585699; CAE52219.1; -; Genomic_DNA.
DR   EMBL; AJ585700; CAE52220.1; -; Genomic_DNA.
DR   EMBL; AJ585701; CAE52221.1; -; Genomic_DNA.
DR   EMBL; AJ585702; CAE52222.1; -; Genomic_DNA.
DR   EMBL; AJ585703; CAE52223.1; -; Genomic_DNA.
DR   EMBL; AJ585704; CAE52224.1; -; Genomic_DNA.
DR   EMBL; AF416613; AAL09032.1; -; mRNA.
DR   EMBL; U18530; AAB64486.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07643.1; -; Genomic_DNA.
DR   PIR; A03605; RGBYA2.
DR   RefSeq; NP_010907.1; NM_001178824.1.
DR   PDB; 1CE9; X-ray; 1.80 A; A/B/C/D=253-281.
DR   PDB; 1DGC; X-ray; 3.00 A; A=220-281.
DR   PDB; 1ENV; X-ray; 2.60 A; A=254-280.
DR   PDB; 1FAV; X-ray; 3.00 A; A=254-280.
DR   PDB; 1FMH; NMR; -; A/B=249-279.
DR   PDB; 1GCL; X-ray; 2.10 A; A/B/C/D=249-281.
DR   PDB; 1GCM; X-ray; 1.80 A; A/B/C=249-281.
DR   PDB; 1GK6; X-ray; 1.90 A; A/B=249-279.
DR   PDB; 1GZL; X-ray; 1.80 A; A/B=249-276.
DR   PDB; 1IHQ; NMR; -; A/B=264-281.
DR   PDB; 1IJ0; X-ray; 1.86 A; A/B/C=249-281.
DR   PDB; 1IJ1; X-ray; 1.86 A; A/B/C=249-281.
DR   PDB; 1IJ2; X-ray; 1.70 A; A/B/C=249-281.
DR   PDB; 1IJ3; X-ray; 1.80 A; A/B/C=249-281.
DR   PDB; 1KQL; X-ray; 2.70 A; A/B=255-278.
DR   PDB; 1LD4; EM; 11.40 A; E/F/G/H/I/J/K/L=225-281.
DR   PDB; 1LLM; X-ray; 1.50 A; C/D=253-281.
DR   PDB; 1NKN; X-ray; 2.50 A; A/B/C/D=250-281.
DR   PDB; 1PIQ; X-ray; 1.80 A; A=249-277.
DR   PDB; 1RB4; X-ray; 1.90 A; A/B/C=249-281.
DR   PDB; 1RB5; X-ray; 1.90 A; A/B/C=249-281.
DR   PDB; 1RB6; X-ray; 1.90 A; A/B/C=249-281.
DR   PDB; 1SWI; X-ray; 2.60 A; A/B/C=249-281.
DR   PDB; 1TMZ; NMR; -; A/B=264-281.
DR   PDB; 1UNT; X-ray; 2.07 A; A/B=249-281.
DR   PDB; 1UNU; X-ray; 2.07 A; A/B=249-281.
DR   PDB; 1UNV; X-ray; 2.14 A; A/B=249-281.
DR   PDB; 1UNW; X-ray; 2.20 A; A/B=249-281.
DR   PDB; 1UNX; X-ray; 2.40 A; A/B=249-281.
DR   PDB; 1UNY; X-ray; 2.30 A; A/B=249-281.
DR   PDB; 1UNZ; X-ray; 2.30 A; A/B=249-281.
DR   PDB; 1UO0; X-ray; 2.40 A; A/B=249-281.
DR   PDB; 1UO1; X-ray; 2.50 A; A/B=249-281.
DR   PDB; 1UO2; X-ray; 1.99 A; A/B=249-281.
DR   PDB; 1UO3; X-ray; 1.92 A; A/B=249-281.
DR   PDB; 1UO4; X-ray; 1.70 A; A/B=249-281.
DR   PDB; 1UO5; X-ray; 2.07 A; A/B=249-281.
DR   PDB; 1W5G; X-ray; 2.16 A; A/B=249-281.
DR   PDB; 1W5H; X-ray; 2.50 A; A/B=249-281.
DR   PDB; 1W5I; X-ray; 2.30 A; A/B=249-281.
DR   PDB; 1W5J; X-ray; 2.20 A; A/B/C/D=249-273.
DR   PDB; 1W5K; X-ray; 1.92 A; A/B/C/D=249-263.
DR   PDB; 1W5L; X-ray; 2.17 A; A/B=249-281.
DR   PDB; 1YSA; X-ray; 2.90 A; C/D=226-281.
DR   PDB; 1ZII; X-ray; 1.80 A; A/B=249-281.
DR   PDB; 1ZIJ; X-ray; 2.00 A; A/B/C=249-281.
DR   PDB; 1ZIK; X-ray; 1.80 A; A/B=249-281.
DR   PDB; 1ZIL; X-ray; 2.25 A; A/B=249-281.
DR   PDB; 1ZIM; X-ray; 2.00 A; A/B/C=249-281.
DR   PDB; 1ZTA; NMR; -; A=247-281.
DR   PDB; 2AHP; X-ray; 2.00 A; A/B=249-281.
DR   PDB; 2B1F; X-ray; 1.50 A; A/B/C/D=251-281.
DR   PDB; 2B22; X-ray; 2.00 A; A=251-281.
DR   PDB; 2BNI; X-ray; 1.50 A; A/B/C/D=249-281.
DR   PDB; 2CCE; X-ray; 1.90 A; A/B=249-281.
DR   PDB; 2CCF; X-ray; 1.70 A; A/B=249-281.
DR   PDB; 2CCN; X-ray; 1.60 A; A/B=249-281.
DR   PDB; 2D3E; X-ray; 2.60 A; A/B/C/D=254-277.
DR   PDB; 2DGC; X-ray; 2.20 A; A=220-281.
DR   PDB; 2EFR; X-ray; 1.80 A; A/B/C/D=249-277.
DR   PDB; 2EFS; X-ray; 2.00 A; A/B/C/D=249-277.
DR   PDB; 2G9J; NMR; -; A/B=264-281.
DR   PDB; 2HY6; X-ray; 1.25 A; A/B/C/D/E/F/G=251-281.
DR   PDB; 2IPZ; X-ray; 1.35 A; A/B/C/D=251-281.
DR   PDB; 2LPB; NMR; -; B=101-134.
DR   PDB; 2NRN; X-ray; 1.40 A; A/B/C/D=251-281.
DR   PDB; 2O7H; X-ray; 1.86 A; A/B/C/D/E/F=249-281.
DR   PDB; 2OVN; NMR; -; A=264-280.
DR   PDB; 2WG5; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272.
DR   PDB; 2WG6; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=249-272.
DR   PDB; 2WPY; X-ray; 1.75 A; A=249-281.
DR   PDB; 2WPZ; X-ray; 1.25 A; A/B/C=249-281.
DR   PDB; 2WQ0; X-ray; 1.12 A; A=249-281.
DR   PDB; 2WQ1; X-ray; 1.08 A; A=249-281.
DR   PDB; 2WQ2; X-ray; 1.36 A; A=249-281.
DR   PDB; 2WQ3; X-ray; 1.22 A; A=249-281.
DR   PDB; 2Z5H; X-ray; 2.89 A; A/B/C/D/E/F/G/H=259-278, I=267-278.
DR   PDB; 2Z5I; X-ray; 2.10 A; A/B/C/D/E/F/G/H=259-278, I/J=267-278.
DR   PDB; 2ZTA; X-ray; 1.80 A; A/B=249-281.
DR   PDB; 3AZD; X-ray; 0.98 A; A/B=264-281.
DR   PDB; 3BAS; X-ray; 2.30 A; A/B=250-281.
DR   PDB; 3BAT; X-ray; 2.30 A; A/B/C/D=250-281.
DR   PDB; 3CK4; X-ray; 1.70 A; A/B/C/D/E/F/G/H/I/J/K/L=251-281.
DR   PDB; 3CRP; X-ray; 1.70 A; A/B/C/D/E=251-281.
DR   PDB; 3G9R; X-ray; 2.00 A; A/B/C/D/E/F=258-263.
DR   PDB; 3GJP; X-ray; 2.00 A; A/B/C=249-281.
DR   PDB; 3I1G; X-ray; 1.60 A; A=249-281.
DR   PDB; 3I5C; X-ray; 1.94 A; A/B=249-278.
DR   PDB; 3K7Z; X-ray; 1.90 A; A/B/C=249-281.
DR   PDB; 3M48; X-ray; 1.45 A; A=249-281.
DR   PDB; 3P8M; X-ray; 2.90 A; C/D=250-281.
DR   PDBsum; 1CE9; -.
DR   PDBsum; 1DGC; -.
DR   PDBsum; 1ENV; -.
DR   PDBsum; 1FAV; -.
DR   PDBsum; 1FMH; -.
DR   PDBsum; 1GCL; -.
DR   PDBsum; 1GCM; -.
DR   PDBsum; 1GK6; -.
DR   PDBsum; 1GZL; -.
DR   PDBsum; 1IHQ; -.
DR   PDBsum; 1IJ0; -.
DR   PDBsum; 1IJ1; -.
DR   PDBsum; 1IJ2; -.
DR   PDBsum; 1IJ3; -.
DR   PDBsum; 1KQL; -.
DR   PDBsum; 1LD4; -.
DR   PDBsum; 1LLM; -.
DR   PDBsum; 1NKN; -.
DR   PDBsum; 1PIQ; -.
DR   PDBsum; 1RB4; -.
DR   PDBsum; 1RB5; -.
DR   PDBsum; 1RB6; -.
DR   PDBsum; 1SWI; -.
DR   PDBsum; 1TMZ; -.
DR   PDBsum; 1UNT; -.
DR   PDBsum; 1UNU; -.
DR   PDBsum; 1UNV; -.
DR   PDBsum; 1UNW; -.
DR   PDBsum; 1UNX; -.
DR   PDBsum; 1UNY; -.
DR   PDBsum; 1UNZ; -.
DR   PDBsum; 1UO0; -.
DR   PDBsum; 1UO1; -.
DR   PDBsum; 1UO2; -.
DR   PDBsum; 1UO3; -.
DR   PDBsum; 1UO4; -.
DR   PDBsum; 1UO5; -.
DR   PDBsum; 1W5G; -.
DR   PDBsum; 1W5H; -.
DR   PDBsum; 1W5I; -.
DR   PDBsum; 1W5J; -.
DR   PDBsum; 1W5K; -.
DR   PDBsum; 1W5L; -.
DR   PDBsum; 1YSA; -.
DR   PDBsum; 1ZII; -.
DR   PDBsum; 1ZIJ; -.
DR   PDBsum; 1ZIK; -.
DR   PDBsum; 1ZIL; -.
DR   PDBsum; 1ZIM; -.
DR   PDBsum; 1ZTA; -.
DR   PDBsum; 2AHP; -.
DR   PDBsum; 2B1F; -.
DR   PDBsum; 2B22; -.
DR   PDBsum; 2BNI; -.
DR   PDBsum; 2CCE; -.
DR   PDBsum; 2CCF; -.
DR   PDBsum; 2CCN; -.
DR   PDBsum; 2D3E; -.
DR   PDBsum; 2DGC; -.
DR   PDBsum; 2EFR; -.
DR   PDBsum; 2EFS; -.
DR   PDBsum; 2G9J; -.
DR   PDBsum; 2HY6; -.
DR   PDBsum; 2IPZ; -.
DR   PDBsum; 2LPB; -.
DR   PDBsum; 2NRN; -.
DR   PDBsum; 2O7H; -.
DR   PDBsum; 2OVN; -.
DR   PDBsum; 2WG5; -.
DR   PDBsum; 2WG6; -.
DR   PDBsum; 2WPY; -.
DR   PDBsum; 2WPZ; -.
DR   PDBsum; 2WQ0; -.
DR   PDBsum; 2WQ1; -.
DR   PDBsum; 2WQ2; -.
DR   PDBsum; 2WQ3; -.
DR   PDBsum; 2Z5H; -.
DR   PDBsum; 2Z5I; -.
DR   PDBsum; 2ZTA; -.
DR   PDBsum; 3AZD; -.
DR   PDBsum; 3BAS; -.
DR   PDBsum; 3BAT; -.
DR   PDBsum; 3CK4; -.
DR   PDBsum; 3CRP; -.
DR   PDBsum; 3G9R; -.
DR   PDBsum; 3GJP; -.
DR   PDBsum; 3I1G; -.
DR   PDBsum; 3I5C; -.
DR   PDBsum; 3K7Z; -.
DR   PDBsum; 3M48; -.
DR   PDBsum; 3P8M; -.
DR   DisProt; DP00083; -.
DR   ProteinModelPortal; P03069; -.
DR   SMR; P03069; 101-134, 229-277.
DR   DIP; DIP-591N; -.
DR   IntAct; P03069; 5.
DR   MINT; MINT-395967; -.
DR   STRING; P03069; -.
DR   EnsemblFungi; YEL009C; YEL009C; YEL009C.
DR   GeneID; 856709; -.
DR   KEGG; sce:YEL009C; -.
DR   CYGD; YEL009c; -.
DR   SGD; S000000735; GCN4.
DR   eggNOG; NOG329891; -.
DR   KO; K09464; -.
DR   OMA; ARKLQRM; -.
DR   OrthoDB; EOG46QB3F; -.
DR   EvolutionaryTrace; P03069; -.
DR   NextBio; 982781; -.
DR   ArrayExpress; P03069; -.
DR   Genevestigator; P03069; -.
DR   GermOnline; YEL009C; Saccharomyces cerevisiae.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0001191; F:RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription; IPI:SGD.
DR   GO; GO:0001190; F:RNA polymerase II transcription factor binding transcription factor activity involved in positive regulation of transcription; IMP:SGD.
DR   GO; GO:0001135; F:RNA polymerase II transcription factor recruiting transcription factor activity; IMP:SGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IMP:SGD.
DR   GO; GO:0001084; F:TFIID-class binding transcription factor activity; IPI:SGD.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0010691; P:negative regulation of ribosomal protein gene transcription from RNA polymerase II promoter in response to nutrient levels; IMP:SGD.
DR   GO; GO:0001080; P:nitrogen catabolite activation of transcription from RNA polymerase II promoter; IMP:SGD.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:SGD.
DR   GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IMP:SGD.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR011616; bZIP_1.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF00170; bZIP_1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Amino-acid biosynthesis; Complete proteome;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    281       General control protein GCN4.
FT                                /FTId=PRO_0000076490.
FT   DOMAIN      253    274       Leucine-zipper.
FT   DNA_BIND    231    249       Basic motif.
FT   REGION       89    100       Required for transcriptional activation.
FT   REGION      106    125       Required for transcriptional activation.
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES     165    165       Phosphothreonine; by PHO85.
FT   MOD_RES     218    218       Phosphoserine.
FT   VARIANT      24     24       S -> P (in strain: CLIB 219).
FT   VARIANT      62     62       P -> S (in strain: CLIB 630 haplotype
FT                                Ha2).
FT   VARIANT      82     82       T -> A (in strain: CLIB 556 haplotype
FT                                Ha1).
FT   VARIANT      91     91       D -> A (in strain: CLIB 95, CLIB 219,
FT                                CLIB 382, CLIB 388, CLIB 410, CLIB 413,
FT                                CLIB 556, CLIB 630, K1, R12, R13
FT                                haplotype Ha2, Sigma 1278B haplotype Ha1,
FT                                YIIc12 and YIIc17).
FT   VARIANT     125    125       D -> A (in strain: CLIB 556 haplotype
FT                                Ha1).
FT   VARIANT     196    196       D -> E (in strain: CLIB 388, CLIB 410,
FT                                CLIB 413, CLIB 630 haplotype Ha1, K1,
FT                                YIIc12 haplotype Ha2 and YIIc17 haplotype
FT                                Ha1).
FT   MUTAGEN      97     98       FF->AA: Reduces transcriptional
FT                                activation activity; when associated with
FT                                A-107; A-110; A-113; A-120; A-123 and A-
FT                                124.
FT   MUTAGEN     107    107       M->A: Reduces transcriptional activation
FT                                activity; when associated with A-97; A-
FT                                98; A-110; A-113; A-120; A-123 and A-124.
FT   MUTAGEN     110    110       Y->A: Reduces transcriptional activation
FT                                activity; when associated with A-97; A-
FT                                98; A-107; A-113; A-120; A-123 and A-124.
FT   MUTAGEN     113    113       L->A: Reduces transcriptional activation
FT                                activity; when associated with A-97; A-
FT                                98; A-107; A-110; A-120; A-123 and A-124.
FT   MUTAGEN     120    124       WTSLF->ATSAA: Reduces transcriptional
FT                                activation activity; when associated with
FT                                A-97; A-98; A-107; A-110 and A-113.
FT   CONFLICT    239    281       ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVG
FT                                ER -> PGVLVRESCKE (in Ref. 2; AAA65521).
FT   HELIX       230    248
FT   HELIX       251    280
SQ   SEQUENCE   281 AA;  31310 MW;  2ED1B8E35D509578 CRC64;
     MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK TEEDPIIKQD
     TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS STDSTPMFEY ENLEDNSKEW
     TSLFDNDIPV TTDDVSLADK AIESTEEVSL VPSNLEVSTT SFLPTPVLED AKLTQTRKVK
     KPNSVVKKSH HVGKDDESRL DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR
     RSRARKLQRM KQLEDKVEEL LSKNYHLENE VARLKKLVGE R
//
ID   HBA_HUMAN               Reviewed;         142 AA.
AC   P69905; P01922; Q1HDT5; Q3MIF5; Q53F97; Q96KF1; Q9NYR7; Q9UCM0;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 108.
DE   RecName: Full=Hemoglobin subunit alpha;
DE   AltName: Full=Alpha-globin;
DE   AltName: Full=Hemoglobin alpha chain;
GN   Name=HBA1;
GN   and
GN   Name=HBA2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
RX   MEDLINE=81088339; PubMed=7448866; DOI=10.1016/0092-8674(80)90347-5;
RA   Michelson A.M., Orkin S.H.;
RT   "The 3' untranslated regions of the duplicated human alpha-globin
RT   genes are unexpectedly divergent.";
RL   Cell 22:371-377(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
RX   MEDLINE=80137531; PubMed=6244294;
RA   Wilson J.T., Wilson L.B., Reddy V.B., Cavallesco C., Ghosh P.K.,
RA   Deriel J.K., Forget B.G., Weissman S.M.;
RT   "Nucleotide sequence of the coding portion of human alpha globin
RT   messenger RNA.";
RL   J. Biol. Chem. 255:2807-2815(1980).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2).
RX   MEDLINE=81175088; PubMed=6452630; DOI=10.1073/pnas.77.12.7054;
RA   Liebhaber S.A., Goossens M.J., Kan Y.W.;
RT   "Cloning and complete nucleotide sequence of human 5'-alpha-globin
RT   gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6946451; DOI=10.1073/pnas.78.8.5041;
RA   Orkin S.H., Goff S.C., Hechtman R.L.;
RT   "Mutation in an intervening sequence splice junction in man.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:5041-5045(1981).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-32.
RX   MEDLINE=21303311; PubMed=11410421;
RA   Zhao Y., Xu X.;
RT   "Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha-
RT   thalassemia in a Chinese family with HbH disease.";
RL   Haematologica 86:541-542(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1).
RX   MEDLINE=21295668; PubMed=11402454;
RA   Zhao Y., Zhong M., Liu Z., Xu X.;
RT   "Rapid detection of the common alpha-thalassemia-2 determinants by PCR
RT   assay.";
RL   Zhonghua Yi Xue Yi Chuan Xue Za Zhi 18:216-218(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-1 AND ALPHA-2).
RX   PubMed=16728641; DOI=10.1126/science.1126431;
RA   De Gobbi M., Viprakasit V., Hughes J.R., Fisher C., Buckle V.J.,
RA   Ayyub H., Gibbons R.J., Vernimmen D., Yoshinaga Y., de Jong P.,
RA   Cheng J.-F., Rubin E.M., Wood W.G., Bowden D., Higgs D.R.;
RT   "A regulatory SNP causes a human genetic disease by creating a new
RT   transcriptional promoter.";
RL   Science 312:1215-1217(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (HBA2).
RC   TISSUE=Blood;
RA   Kutlar F., Leithner C., Kutlar A.;
RT   "Rapid sequencing of mRNA of the human alpha two globin, directly
RT   isolated from reticulocytes in whole blood.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] (HBA1).
RC   TISSUE=Blood;
RA   Kutlar F., Leithner C., Kutlar A.;
RT   "cDNA sequencing of human alpha one globin mRNA, the 3'untranslated
RT   region is different than alpha two globin.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RA   Kutlar F., Holley L., Leithner C., Kutlar A.;
RT   "An alpha chain variant 'Hemoglobin J-Toronto (Cd.5 /Ala to Asp)'
RT   mutation was detected on the alpha-1 globin mRNA by sequencing of
RT   cDNA.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT EVANS MET-63.
RC   TISSUE=Blood;
RA   Kutlar F., Elam D., Hoff J.V., Holley L., Kutlar A.;
RT   "Unstable Hb 'Evans' (GTG->ATG/Val 62 Met) was detected on the alpha-2
RT   globin gene of an Hispanic girl.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT G-PHILADELPHIA
RP   LYS-69.
RA   Kutlar F., Davis D.H., Nechtman J., Elam D.;
RT   "Hb G-Philadelphia (Alpha,Codon 68;AAC>AAG/Asn>Lys)in black is
RT   detected on a chromosome that carries alpha 3.7 kb deletion showed
RT   completely normal alpha-2 globin gene sequence.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
RX   MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA   Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K.,
RA   Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA   Higgs D.R.;
RT   "Sequence, structure and pathology of the fully annotated terminal 2
RT   Mb of the short arm of human chromosome 16.";
RL   Hum. Mol. Genet. 10:339-352(2001).
RN   [15]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2).
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA   Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA   Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA   Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA   Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA   Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA   Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA   Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA   Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA   Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA   Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA   Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA   Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA   Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA   Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA   Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA   Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA   Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA   Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA   Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA   Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HBA1 AND HBA2).
RC   TISSUE=Bone marrow, Brain, Lung, and Spleen;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [17]
RP   PROTEIN SEQUENCE OF 2-142.
RX   PubMed=13872627;
RA   Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G.,
RA   Rudloff V., Wittmann-Liebold B.;
RT   "The constitution of normal adult human haemoglobin.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
RN   [18]
RP   PROTEIN SEQUENCE OF 2-142.
RX   PubMed=13954546;
RA   Hill R.J., Konigsberg W.;
RT   "The structure of human hemoglobin: IV. The chymotryptic digestion of
RT   the alpha chain of human hemoglobin.";
RL   J. Biol. Chem. 237:3151-3156(1962).
RN   [19]
RP   PROTEIN SEQUENCE OF 2-142.
RX   PubMed=14093912; DOI=10.1021/bi00906a030;
RA   Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J.;
RT   "The amino acid sequence of the alpha chain of human fetal
RT   hemoglobin.";
RL   Biochemistry 2:1353-1357(1963).
RN   [20]
RP   PROTEIN SEQUENCE OF 2-32.
RC   TISSUE=Platelet;
RX   MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA   Thomas G.R., Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass
RT   spectrometric identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [21]
RP   PROTEIN SEQUENCE OF 128-142, AND VARIANT ETHIOPIA HIS-141.
RC   TISSUE=Umbilical cord blood;
RX   MEDLINE=93053735; PubMed=1428951;
RA   Webber B.B., Wilson J.B., Gu L.-H., Huisman T.H.J.;
RT   "Hb Ethiopia or alpha 2(140)(HC2)Tyr----His beta 2.";
RL   Hemoglobin 16:441-443(1992).
RN   [22]
RP   GLYCATION AT LYS-8; LYS-17; LYS-41 AND LYS-62, AND LACK OF GLYCATION
RP   AT LYS-12; LYS-57; LYS-61; LYS-91 AND LYS-100.
RX   PubMed=7358733;
RA   Shapiro R., McManus M.J., Zalut C., Bunn H.F.;
RT   "Sites of nonenzymatic glycosylation of human hemoglobin A.";
RL   J. Biol. Chem. 255:3120-3127(1980).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Lung carcinoma;
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RX   MEDLINE=76027820; PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4;
RA   Fermi G.;
RT   "Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2.5-
RT   A resolution: refinement of the atomic model.";
RL   J. Mol. Biol. 97:237-256(1975).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3;
RA   Baldwin J.M.;
RT   "The structure of human carbonmonoxy haemoglobin at 2.7-A
RT   resolution.";
RL   J. Mol. Biol. 136:103-128(1980).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE.
RX   MEDLINE=92381041; PubMed=1512262;
RA   Silva M.M., Rogers P.H., Arnone A.;
RT   "A third quaternary structure of human hemoglobin A at 1.7-A
RT   resolution.";
RL   J. Biol. Chem. 267:17248-17256(1992).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2.
RX   MEDLINE=98332748; PubMed=9665850; DOI=10.1006/jmbi.1998.1868;
RA   Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T.,
RA   Baker E.N.;
RT   "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy
RT   form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution.";
RL   J. Mol. Biol. 280:475-484(1998).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38
RP   INS.
RX   MEDLINE=93192190; PubMed=8448109; DOI=10.1021/bi00061a007;
RA   Kavanaugh J.S., Moo-Penn W.F., Arnone A.;
RT   "Accommodation of insertions in helices: the mutation in hemoglobin
RT   Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha
RT   bulge.";
RL   Biochemistry 32:2509-2513(1993).
RN   [30]
RP   VARIANT AL-AIN ABU DHABI ASP-19.
RX   MEDLINE=93053723; PubMed=1428941;
RA   Abbes S., M'Rad A., Fitzgerald P.A., Dormer P., Blouquit Y.,
RA   Kister J., Galacteros F., Wajcman H.;
RT   "HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin
RT   variant discovered in an Emiratee family.";
RL   Hemoglobin 16:355-362(1992).
RN   [31]
RP   VARIANT ATAGO TYR-86.
RX   MEDLINE=72030550; PubMed=5115619;
RA   Fujiwara N., Maekawa T., Matsuda G.;
RT   "Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human
RT   hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and
RT   myoglobins. VI.";
RL   Int. J. Protein Res. 3:35-39(1971).
RN   [32]
RP   VARIANT AUCKLAND ASN-88.
RX   MEDLINE=97463291; PubMed=9322075;
RA   Brennan S.O., Matthews J.R.;
RT   "Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal
RT   histidine identified by electrospray mass spectrometry.";
RL   Hemoglobin 21:393-403(1997).
RN   [33]
RP   VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75.
RA   Brimhall B.J., Duerst M., Hollan S.R., Stenzel P., Szelenyi J.,
RA   Jones R.T.;
RT   "Structural characterizations of hemoglobins J-Buda (alpha 61 (E10)
RT   Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn).";
RL   Biochim. Biophys. Acta 336:344-360(1974).
RN   [34]
RP   VARIANT CEMENELUM TRP-93.
RX   PubMed=8148419; DOI=10.1007/BF01715134;
RA   Wajcman H., Kister J., M'Rad A., Soummer A.M., Galacteros F.;
RT   "Hb Cemenelum [alpha 92 (FG4) Arg-->Trp]: a hemoglobin variant of the
RT   alpha 1/beta 2 interface that displays a moderate increase in oxygen
RT   affinity.";
RL   Ann. Hematol. 68:73-76(1994).
RN   [35]
RP   VARIANTS CHONGQING ARG-3 AND HARBIN MET-17.
RX   MEDLINE=85130255; PubMed=6526652;
RA   Zeng Y.-T., Huang S.-Z., Qiu X.-K., Cheng G.-C., Ren Z.-R., Jin Q.-C.,
RA   Chen C.-Y., Jiao C.-T., Tang Z.-G., Liu R.-H., Bao X.-H., Zeng L.-Z.,
RA   Duan Y.-Q., Zhang G.-Y.;
RT   "Hemoglobin Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin
RT   [alpha 16(A14)Lys-->Met] found in China.";
RL   Hemoglobin 8:569-581(1984).
RN   [36]
RP   VARIANT CLINIC LYS-61 DEL.
RX   PubMed=10206681;
RX   DOI=10.1002/(SICI)1098-1004(1998)11:5<412::AID-HUMU14>3.3.CO;2-I;
RA   Ayala S., Colomer D., Gelpi J.L., Corron J.L.V.;
RT   "Alpha-thalassaemia due to a single codon deletion in the alpha 1-
RT   globin gene. Computational structural analysis of the new alpha-chain
RT   variant.";
RL   Hum. Mutat. 11:412-412(1998).
RN   [37]
RP   VARIANT DAVENPORT HIS-79.
RX   MEDLINE=91331854; PubMed=2101836;
RA   Wilson J.B., Webber B.B., Plaseska D., de Alarcon P.A., McMillan S.K.,
RA   Huisman T.H.J.;
RT   "Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2.";
RL   Hemoglobin 14:599-605(1990).
RN   [38]
RP   VARIANT EVANS MET-63.
RX   MEDLINE=90109650; PubMed=2606724;
RA   Wilson J.B., Webber B.B., Kutlar A., Reese A.L., McKie V.C.,
RA   Lutcher C.L., Felice A.E., Huisman T.H.J.;
RT   "Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin
RT   causing a mild hemolytic anemia.";
RL   Hemoglobin 13:557-566(1989).
RN   [39]
RP   VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46.
RX   MEDLINE=89323437; PubMed=2752146;
RA   Cash F.E., Monplaisir N., Goossens M., Liebhaber S.A.;
RT   "Locus assignment of two alpha-globin structural mutants from the
RT   Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish
RT   Town (alpha 27 Val).";
RL   Blood 74:833-835(1989).
RN   [40]
RP   VARIANT GODAVARI THR-96.
RX   MEDLINE=98153063; PubMed=9494044;
RA   Wajcman H., Kister J., Riou J., Galacteros F., Girot R.,
RA   Maier-Redelsperger M., Nayudu N.V.S., Giordano P.C.;
RT   "Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid
RT   substitution in the alpha 1 beta 2 interface that modifies the
RT   electrophoretic mobility of hemoglobin.";
RL   Hemoglobin 22:11-22(1998).
RN   [41]
RP   VARIANT GRADY GLU-PHE-THR-119 INS.
RX   MEDLINE=75010592; PubMed=4528583; DOI=10.1073/pnas.71.8.3270;
RA   Huisman T.H.J., Wilson J.B., Gravely M., Hubbard M.;
RT   "Hemoglobin Grady: the first example of a variant with elongated
RT   chains due to an insertion of residues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974).
RN   [42]
RP   VARIANT HANAMAKI GLU-140.
RX   MEDLINE=92340291; PubMed=1634363;
RA   Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K.;
RT   "A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys-->Glu
RT   beta 2, found in a Japanese family.";
RL   Hemoglobin 16:67-71(1992).
RN   [43]
RP   VARIANT HANDA MET-91.
RX   MEDLINE=83056269; PubMed=6815131;
RA   Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.;
RT   "HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and
RT   biosynthesis of a new slightly higher oxygen affinity variant.";
RL   Hemoglobin 6:379-389(1982).
RN   [44]
RP   VARIANT HASHARON HIS-48.
RX   MEDLINE=69165810; PubMed=5780195; DOI=10.1172/JCI106041;
RA   Charache S., Mondzac A.M., Gessner U.;
RT   "Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found
RT   in low concentration.";
RL   J. Clin. Invest. 48:834-847(1969).
RN   [45]
RP   VARIANT HOBART ARG-21.
RX   MEDLINE=88006902; PubMed=3654264;
RA   Fleming P.J., Sumner D.R., Wyatt K., Hughes W.G., Melrose W.D.,
RA   Jupe D.M.D., Baikie M.J.;
RT   "Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain
RT   hemoglobin variant.";
RL   Hemoglobin 11:211-220(1987).
RN   [46]
RP   VARIANT INKSTER VAL-86.
RX   MEDLINE=74302151; PubMed=4212045;
RX   DOI=10.1111/j.1365-2141.1974.tb00489.x;
RA   Reed R.E., Winter W.P., Rucknagel D.L.;
RT   "Haemoglobin inkster (alpha2 85aspartic acid leads to valine beta2)
RT   coexisting with beta-thalassaemia in a Caucasian family.";
RL   Br. J. Haematol. 26:475-484(1974).
RN   [47]
RP   VARIANT KANAGAWA MET-41.
RX   MEDLINE=92340282; PubMed=1634355;
RA   Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T.,
RA   Harano K., Imai K.;
RT   "Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with
RT   an increased oxygen affinity.";
RL   Hemoglobin 16:1-10(1992).
RN   [48]
RP   VARIANT KURDISTAN TYR-48.
RX   MEDLINE=94252883; PubMed=8195005;
RA   Giordano P.C., Harteveld C.L., Streng H., Oosterwijk J.C.,
RA   Heister J.G.A.M., Amons R., Bernini L.F.;
RT   "Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in
RT   combination with beta (0)-thalassemia.";
RL   Hemoglobin 18:11-18(1994).
RN   [49]
RP   VARIANT KUROSAKI GLU-8.
RX   MEDLINE=96031515; PubMed=7558876;
RA   Harano T., Harano K., Imai K., Murakami T., Matsubara H.;
RT   "Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found
RT   in a Japanese woman.";
RL   Hemoglobin 19:197-201(1995).
RN   [50]
RP   VARIANT J-MEERUT/J-BIRMINGHAM GLU-121.
RX   MEDLINE=95229430; PubMed=7713747;
RA   Yalcin A., Avcu F., Beyan C., Guergey A., Ural A.U.;
RT   "A case of HB J-Meerut (or Hb J-Birmingham) [alpha
RT   120(H3)Ala-->Glu].";
RL   Hemoglobin 18:433-435(1994).
RN   [51]
RP   VARIANT MELUSINE SER-115.
RX   MEDLINE=94124250; PubMed=8294199;
RA   Wacjman H., Klames G., Groff P., Prome D., Riou J., Galacteros F.;
RT   "Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin
RT   variant.";
RL   Hemoglobin 17:397-405(1993).
RN   [52]
RP   VARIANT MONTGOMERY ARG-49.
RX   MEDLINE=75109326; PubMed=1115799;
RA   Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G.,
RA   Atkins R.;
RT   "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys)
RT   and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
RL   Biochim. Biophys. Acta 379:28-32(1975).
RN   [53]
RP   VARIANT PETAH TIKVA ASP-111.
RX   MEDLINE=81134478; PubMed=7470621;
RA   Honig G.R., Shamsuddin M., Zaizov R., Steinherz M., Solar I.,
RA   Kirschman C.;
RT   "Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new
RT   unstable variant with alpha-thalassemia-like expression.";
RL   Blood 57:705-711(1981).
RN   [54]
RP   VARIANT PHNOM PENH ILE-118 INS.
RX   MEDLINE=98112407; PubMed=9452028;
RA   Wajcman H., Prehu M.O., Prehu C., Blouquit Y., Prome D.,
RA   Galacteros F.;
RT   "Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence
RT   for a hotspot for insertion of residues in the third exon of the
RT   alpha1-globin gene.";
RL   Hum. Mutat. Suppl. 1:S20-S22(1998).
RN   [55]
RP   VARIANT PORT HURON ARG-57.
RX   MEDLINE=92202056; PubMed=1802882;
RA   Zwerdling T., Williams S., Nasr S.A., Rucknagel D.L.;
RT   "Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant.";
RL   Hemoglobin 15:381-391(1991).
RN   [56]
RP   VARIANT SAWARA ALA-7.
RX   MEDLINE=74008827; PubMed=4744335;
RA   Sumida I., Ohta Y., Imamura T., Yanase T.;
RT   "Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine.";
RL   Biochim. Biophys. Acta 322:23-26(1973).
RN   [57]
RP   VARIANT SHENYANG GLU-27.
RX   MEDLINE=83135048; PubMed=7161109;
RA   Zeng Y.-T., Huang S.-Z., Zhou X., Qiu X.-K., Dong Q., Li M., Bai J.;
RT   "Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable
RT   variant found in China.";
RL   Hemoglobin 6:625-628(1982).
RN   [58]
RP   VARIANT SUAN-DOK ARG-110.
RX   MEDLINE=80006169; PubMed=478977;
RA   Sanguansermsri T., Matragoon S., Changloah L., Flatz G.;
RT   "Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2):
RT   an unstable variant associated with alpha-thalassemia.";
RL   Hemoglobin 3:161-174(1979).
RN   [59]
RP   INVOLVEMENT IN HEIBAN, AND VARIANT TOYAMA ARG-137.
RX   PubMed=2833478;
RA   Ohba Y., Yamamoto K., Hattori Y., Kawata R., Miyaji T.;
RT   "Hyperunstable hemoglobin Toyama [alpha 2 136(H19)Leu----Arg beta 2]:
RT   detection and identification by in vitro biosynthesis with radioactive
RT   amino acids.";
RL   Hemoglobin 11:539-556(1987).
RN   [60]
RP   VARIANT SUN PRAIRIE PRO-131.
RX   MEDLINE=91177710; PubMed=2079430;
RA   Harkness M., Harkness D.R., Kutlar F., Kutlar A., Wilson J.B.,
RA   Webber B.B., Codrington J.F., Huisman T.H.J.;
RT   "Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable
RT   variant occurring in low quantities.";
RL   Hemoglobin 14:479-489(1990).
RN   [61]
RP   VARIANT SWAN RIVER GLY-7.
RX   MEDLINE=96351655; PubMed=8745434;
RA   Harano T., Harano K., Imai K., Terunuma S.;
RT   "HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man.";
RL   Hemoglobin 20:75-78(1996).
RN   [62]
RP   VARIANT THIONVILLE GLU-2.
RX   MEDLINE=92316953; PubMed=1618774;
RA   Vasseur C., Blouquit Y., Kister J., Prome D., Kavanaugh J.S.,
RA   Rogers P.H., Guillemin C., Arnone A., Galacteros F., Poyart C.,
RA   Rosa J., Wajcman H.;
RT   "Hemoglobin Thionville. An alpha-chain variant with a substitution of
RT   a glutamate for valine at NA-1 and having an acetylated methionine NH2
RT   terminus.";
RL   J. Biol. Chem. 267:12682-12691(1992).
RN   [63]
RP   VARIANT TUNIS-BIZERTE PRO-130.
RX   MEDLINE=95306384; PubMed=7786798;
RX   DOI=10.1111/j.1365-2141.1995.tb03382.x;
RA   Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris P.;
RT   "Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro
RT   unstable variant with thalassaemic phenotype.";
RL   Br. J. Haematol. 90:71-76(1995).
RN   [64]
RP   VARIANT TURRIFF GLU-100.
RX   MEDLINE=92340284; PubMed=1634357;
RA   Langdown J.V., Davidson R.J., Williamson D.;
RT   "A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the
RT   interference of abnormal hemoglobins in Hb A1c determination.";
RL   Hemoglobin 16:11-17(1992).
RN   [65]
RP   VARIANT VAL DE MARNE ARG-134.
RX   MEDLINE=94124251; PubMed=8294200;
RA   Wacjman H., Kister J., M'Rad A., Marden M.C., Riou J., Galacteros F.;
RT   "Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant
RT   with moderate increase in oxygen affinity.";
RL   Hemoglobin 17:407-417(1993).
RN   [66]
RP   VARIANT WESTMEAD GLN-123.
RX   MEDLINE=92155975; PubMed=1686260;
RA   Jiang N.H., Liang S., Wen X.J., Liang R., Su C., Tang Z.;
RT   "Hb Westmead: an alpha 2-globin gene mutation detected by polymerase
RT   chain reaction and Stu I cleavage.";
RL   Hemoglobin 15:291-295(1991).
RN   [67]
RP   VARIANT WOODVILLE TYR-7.
RX   MEDLINE=86167529; PubMed=3754246;
RA   Como P.F., Barber S., Sage R.E., Kronenberg H.;
RT   "Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine.";
RL   Hemoglobin 10:135-141(1986).
RN   [68]
RP   VARIANT YUDA ASP-131.
RX   MEDLINE=93053734; PubMed=1428950;
RA   Fujisawa K., Hattori Y., Ohba Y., Ando S.;
RT   "Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with
RT   low oxygen affinity.";
RL   Hemoglobin 16:435-439(1992).
RN   [69]
RP   VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS.
RX   MEDLINE=92380658; PubMed=1511986; DOI=10.1007/BF00221961;
RA   Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M.,
RA   Melevendi C., Rasore A., Galacteros F.;
RT   "Two new human hemoglobin variants caused by unusual mutational
RT   events: Hb Zaire contains a five residue repetition within the alpha-
RT   chain and Hb Duino has two residues substituted in the beta-chain.";
RL   Hum. Genet. 89:676-680(1992).
RN   [70]
RP   VARIANT HBH VAL-63 DEL.
RX   PubMed=10569720;
RA   Traeger-Synodinos J., Harteveld C.L., Kanavakis E., Giordano P.C.,
RA   Kattamis C., Bernini L.F.;
RT   "Hb Aghia Sophia [alpha62(E11)Val-->0 (alpha1)], an 'in-frame'
RT   deletion causing alpha-thalassemia.";
RL   Hemoglobin 23:317-324(1999).
RN   [71]
RP   VARIANT BOGHE GLN-59, AND VARIANT CHAROLLES TYR-104.
RX   PubMed=10569723;
RA   Lacan P., Francina A., Souillet G., Aubry M., Couprie N.,
RA   Dementhon L., Becchi M.;
RT   "Two new alpha chain variants: Hb Boghe [alpha58(E7)His-->Gln,
RT   alpha2], a variant on the distal histidine, and Hb CHarolles
RT   [alpha103(G10)His-Tyr, alpha1].";
RL   Hemoglobin 23:345-352(1999).
RN   [72]
RP   VARIANT CAMPINAS VAL-27, AND VARIANT WEST ONE GLY-127.
RX   PubMed=14576901; DOI=10.1590/S0100-879X2003001100004;
RA   Jorge S.B., Melo M.B., Costa F.F., Sonati M.F.;
RT   "Screening for mutations in human alpha-globin genes by nonradioactive
RT   single-strand conformation polymorphism.";
RL   Braz. J. Med. Biol. Res. 36:1471-1474(2003).
RN   [73]
RP   VARIANT BASSETT ALA-95, AND CHARACTERIZATION OF VARIANT BASSETT
RP   ALA-95.
RX   PubMed=15495251; DOI=10.1002/ajh.20184;
RA   Abdulmalik O., Safo M.K., Lerner N.B., Ochotorena J., Daikhin E.,
RA   Lakka V., Santacroce R., Abraham D.J., Asakura T.;
RT   "Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant
RT   with very low oxygen affinity.";
RL   Am. J. Hematol. 77:268-276(2004).
RN   [74]
RP   VARIANT PLASENCIA ARG-126.
RX   PubMed=15921163; DOI=10.1081/HEM-200058578;
RA   Martin G., Villegas A., Gonzalez F.A., Ropero P., Hojas R., Polo M.,
RA   Mateo M., Salvador M., Benavente C.;
RT   "A novel mutation of the alpha2-globin causing alpha(+)-thalassemia:
RT   Hb Plasencia [alpha125(H8)Leu-->Arg (alpha2).";
RL   Hemoglobin 29:113-117(2005).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA); two alpha chains and two delta chains in
CC       adult hemoglobin A2 (HbA2); two alpha chains and two epsilon
CC       chains in early embryonic hemoglobin Gower-2; two alpha chains and
CC       two gamma chains in fetal hemoglobin F (HbF).
CC   -!- INTERACTION:
CC       P68871:HBB; NbExp=19; IntAct=EBI-714680, EBI-715554;
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- PTM: The initiator Met is not cleaved in variant Thionville and is
CC       acetylated.
CC   -!- DISEASE: Defects in HBA1 may be a cause of Heinz body anemias
CC       (HEIBAN) [MIM:140700]. This is a form of non-spherocytic hemolytic
CC       anemia of Dacie type 1. After splenectomy, which has little
CC       benefit, basophilic inclusions called Heinz bodies are
CC       demonstrable in the erythrocytes. Before splenectomy, diffuse or
CC       punctate basophilia may be evident. Most of these cases are
CC       probably instances of hemoglobinopathy. The hemoglobin
CC       demonstrates heat lability. Heinz bodies are observed also with
CC       the Ivemark syndrome (asplenia with cardiovascular anomalies) and
CC       with glutathione peroxidase deficiency.
CC   -!- DISEASE: Defects in HBA1 are the cause of alpha-thalassemia (A-
CC       THAL) [MIM:604131]. The thalassemias are the most common monogenic
CC       diseases and occur mostly in Mediterranean and Southeast Asian
CC       populations. The hallmark of alpha-thalassemia is an imbalance in
CC       globin-chain production in the adult HbA molecule. The level of
CC       alpha chain production can range from none to very nearly normal
CC       levels. Deletion of both copies of each of the two alpha-globin
CC       genes causes alpha(0)-thalassemia, also known as homozygous alpha
CC       thalassemia. Due to the complete absence of alpha chains, the
CC       predominant fetal hemoglobin is a tetramer of gamma-chains (Bart
CC       hemoglobin) that has essentially no oxygen carrying capacity. This
CC       causes oxygen starvation in the fetal tissues leading to prenatal
CC       lethality or early neonatal death. The loss of three alpha genes
CC       results in high levels of a tetramer of four beta chains
CC       (hemoglobin H), causing a severe and life-threatening anemia known
CC       as hemoglobin H disease. Untreated, most patients die in childhood
CC       or early adolescence. The loss of two alpha genes results in mild
CC       alpha-thalassemia, also known as heterozygous alpha-thalassemia.
CC       Affected individuals have small red cells and a mild anemia
CC       (microcytosis). If three of the four alpha-globin genes are
CC       functional, individuals are completely asymptomatic. Some rare
CC       forms of alpha-thalassemia are due to point mutations (non-
CC       deletional alpha-thalassemia). The thalassemic phenotype is due to
CC       unstable globin alpha chains that are rapidly catabolized prior to
CC       formation of the alpha-beta heterotetramers.
CC   -!- DISEASE: Note=Alpha(0)-thalassemia is associated with non-immune
CC       hydrops fetalis, a generalized edema of the fetus with fluid
CC       accumulation in the body cavities due to non-immune causes. Non-
CC       immune hydrops fetalis is not a diagnosis in itself but a symptom,
CC       a feature of many genetic disorders, and the end-stage of a wide
CC       variety of disorders.
CC   -!- DISEASE: Defects in HBA1 are the cause of hemoglobin H disease
CC       (HBH) [MIM:613978]. HBH is a form of alpha-thalassemia due to the
CC       loss of three alpha genes. This results in high levels of a
CC       tetramer of four beta chains (hemoglobin H), causing a severe and
CC       life-threatening anemia. Untreated, most patients die in childhood
CC       or early adolescence.
CC   -!- MISCELLANEOUS: Gives blood its red color.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD97112.1; Type=Erroneous initiation;
CC   -!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
CC       thalassemias;
CC       URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA1";
CC   -!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
CC       thalassemias;
CC       URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA2";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/HBA1";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/HBA2";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBA1";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry;
CC       URL="http://en.wikipedia.org/wiki/Hemoglobin";
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DR   EMBL; J00153; AAB59407.1; -; Genomic_DNA.
DR   EMBL; J00153; AAB59408.1; -; Genomic_DNA.
DR   EMBL; V00491; CAA23750.1; -; Genomic_DNA.
DR   EMBL; V00493; CAA23752.1; -; mRNA.
DR   EMBL; V00488; CAA23748.1; -; Genomic_DNA.
DR   EMBL; V00516; CAA23774.1; -; Genomic_DNA.
DR   EMBL; AF230076; AAF72612.1; -; Genomic_DNA.
DR   EMBL; AF525460; AAM83102.1; -; Genomic_DNA.
DR   EMBL; DQ431198; ABD95910.1; -; Genomic_DNA.
DR   EMBL; DQ431198; ABD95911.1; -; Genomic_DNA.
DR   EMBL; AF097635; AAC72839.1; -; mRNA.
DR   EMBL; AF105974; AAC97373.1; -; mRNA.
DR   EMBL; AF349571; AAK37554.1; -; mRNA.
DR   EMBL; AF536204; AAN04486.1; -; Genomic_DNA.
DR   EMBL; DQ499017; ABF56144.1; -; Genomic_DNA.
DR   EMBL; DQ499018; ABF56145.1; -; Genomic_DNA.
DR   EMBL; AK223392; BAD97112.1; ALT_INIT; mRNA.
DR   EMBL; AE006462; AAK61215.1; -; Genomic_DNA.
DR   EMBL; AE006462; AAK61216.1; -; Genomic_DNA.
DR   EMBL; Z84721; CAB06554.1; -; Genomic_DNA.
DR   EMBL; Z84721; CAB06555.1; -; Genomic_DNA.
DR   EMBL; BC005931; AAH05931.1; -; mRNA.
DR   EMBL; BC008572; AAH08572.1; -; mRNA.
DR   EMBL; BC032122; AAH32122.1; -; mRNA.
DR   EMBL; BC050661; AAH50661.1; -; mRNA.
DR   EMBL; BC101846; AAI01847.1; -; mRNA.
DR   EMBL; BC101848; AAI01849.1; -; mRNA.
DR   IPI; IPI00410714; -.
DR   PIR; A90807; HAHU.
DR   PIR; C93303; HACZP.
DR   PIR; I58217; HACZ.
DR   RefSeq; NP_000508.1; NM_000517.4.
DR   RefSeq; NP_000549.1; NM_000558.3.
DR   UniGene; Hs.449630; -.
DR   UniGene; Hs.654744; -.
DR   PDB; 1A00; X-ray; 2.00 A; A/C=2-142.
DR   PDB; 1A01; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1A0U; X-ray; 2.14 A; A/C=2-142.
DR   PDB; 1A0Z; X-ray; 2.00 A; A/C=2-142.
DR   PDB; 1A3N; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1A3O; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1A9W; X-ray; 2.90 A; A/C=2-142.
DR   PDB; 1ABW; X-ray; 2.00 A; A=2-142.
DR   PDB; 1ABY; X-ray; 2.60 A; A=2-142.
DR   PDB; 1AJ9; X-ray; 2.20 A; A=2-142.
DR   PDB; 1B86; X-ray; 2.50 A; A/C=2-142.
DR   PDB; 1BAB; X-ray; 1.50 A; A/C=3-142.
DR   PDB; 1BBB; X-ray; 1.70 A; A/C=2-142.
DR   PDB; 1BIJ; X-ray; 2.30 A; A/C=2-142.
DR   PDB; 1BUW; X-ray; 1.90 A; A/C=2-142.
DR   PDB; 1BZ0; X-ray; 1.50 A; A/C=2-142.
DR   PDB; 1BZ1; X-ray; 1.59 A; A/C=2-142.
DR   PDB; 1BZZ; X-ray; 1.59 A; A/C=3-142.
DR   PDB; 1C7B; X-ray; 1.80 A; A/C=3-142.
DR   PDB; 1C7C; X-ray; 1.80 A; A=2-142.
DR   PDB; 1C7D; X-ray; 1.80 A; A=2-142.
DR   PDB; 1CLS; X-ray; 1.90 A; A/C=2-142.
DR   PDB; 1CMY; X-ray; 3.00 A; A/C=2-142.
DR   PDB; 1COH; X-ray; 2.90 A; A/C=2-142.
DR   PDB; 1DKE; X-ray; 2.10 A; A/C=2-142.
DR   PDB; 1DXT; X-ray; 1.70 A; A/C=2-142.
DR   PDB; 1DXU; X-ray; 1.70 A; A/C=2-142.
DR   PDB; 1DXV; X-ray; 1.70 A; A/C=2-142.
DR   PDB; 1FDH; X-ray; 2.50 A; A/B=2-142.
DR   PDB; 1FN3; X-ray; 2.48 A; A/C=2-142.
DR   PDB; 1G9V; X-ray; 1.85 A; A/C=2-142.
DR   PDB; 1GBU; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1GBV; X-ray; 2.00 A; A/C=2-142.
DR   PDB; 1GLI; X-ray; 2.50 A; A/C=3-142.
DR   PDB; 1GZX; X-ray; 2.10 A; A/C=2-142.
DR   PDB; 1HAB; X-ray; 2.30 A; A/C=2-142.
DR   PDB; 1HAC; X-ray; 2.60 A; A/C=2-142.
DR   PDB; 1HBA; X-ray; 2.10 A; A/C=2-142.
DR   PDB; 1HBB; X-ray; 1.90 A; A/C=2-142.
DR   PDB; 1HBS; X-ray; 3.00 A; A/C/E/G=2-141.
DR   PDB; 1HCO; X-ray; 2.70 A; A=2-142.
DR   PDB; 1HDB; X-ray; 2.20 A; A/C=2-142.
DR   PDB; 1HGA; X-ray; 2.10 A; A/C=2-142.
DR   PDB; 1HGB; X-ray; 2.10 A; A/C=2-142.
DR   PDB; 1HGC; X-ray; 2.10 A; A/C=2-142.
DR   PDB; 1HHO; X-ray; 2.10 A; A=2-141.
DR   PDB; 1IRD; X-ray; 1.25 A; A=2-142.
DR   PDB; 1J3Y; X-ray; 1.55 A; A/C/E/G=2-142.
DR   PDB; 1J3Z; X-ray; 1.60 A; A/C/E/G=2-142.
DR   PDB; 1J40; X-ray; 1.45 A; A/C/E/G=2-142.
DR   PDB; 1J41; X-ray; 1.45 A; A/C/E/G=2-142.
DR   PDB; 1J7S; X-ray; 2.20 A; A/C=3-142.
DR   PDB; 1J7W; X-ray; 2.00 A; A/C=3-142.
DR   PDB; 1J7Y; X-ray; 1.70 A; A/C=3-142.
DR   PDB; 1JY7; X-ray; 3.20 A; A/C/P/R/U/W=2-142.
DR   PDB; 1K0Y; X-ray; 1.87 A; A/C=2-142.
DR   PDB; 1K1K; X-ray; 2.00 A; A=2-142.
DR   PDB; 1KD2; X-ray; 1.87 A; A/C=2-142.
DR   PDB; 1LFL; X-ray; 2.70 A; A/C/P/R=2-142.
DR   PDB; 1LFQ; X-ray; 2.60 A; A=2-142.
DR   PDB; 1LFT; X-ray; 2.60 A; A=2-142.
DR   PDB; 1LFV; X-ray; 2.80 A; A=2-142.
DR   PDB; 1LFY; X-ray; 3.30 A; A=2-142.
DR   PDB; 1LFZ; X-ray; 3.10 A; A=2-142.
DR   PDB; 1LJW; X-ray; 2.16 A; A=2-142.
DR   PDB; 1M9P; X-ray; 2.10 A; A/C=2-142.
DR   PDB; 1MKO; X-ray; 2.18 A; A/C=2-142.
DR   PDB; 1NEJ; X-ray; 2.10 A; A/C=2-142.
DR   PDB; 1NIH; X-ray; 2.60 A; A/C=2-142.
DR   PDB; 1NQP; X-ray; 1.73 A; A/C=2-142.
DR   PDB; 1O1I; X-ray; 2.30 A; A=2-142.
DR   PDB; 1O1J; X-ray; 1.90 A; A=2-142.
DR   PDB; 1O1K; X-ray; 2.00 A; A/C=3-142.
DR   PDB; 1O1L; X-ray; 1.80 A; A=2-142.
DR   PDB; 1O1M; X-ray; 1.85 A; A=2-142.
DR   PDB; 1O1N; X-ray; 1.80 A; A=2-142.
DR   PDB; 1O1O; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1O1P; X-ray; 1.80 A; A=2-142.
DR   PDB; 1QI8; X-ray; 1.80 A; A/C=3-142.
DR   PDB; 1QSH; X-ray; 1.70 A; A/C=2-142.
DR   PDB; 1QSI; X-ray; 1.70 A; A/C=2-142.
DR   PDB; 1QXD; X-ray; 2.25 A; A/C=2-142.
DR   PDB; 1QXE; X-ray; 1.85 A; A/C=2-142.
DR   PDB; 1R1X; X-ray; 2.15 A; A=2-142.
DR   PDB; 1R1Y; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1RPS; X-ray; 2.11 A; A/C=2-142.
DR   PDB; 1RQ3; X-ray; 1.91 A; A/C=2-142.
DR   PDB; 1RQ4; X-ray; 2.11 A; A/C=2-142.
DR   PDB; 1RQA; X-ray; 2.11 A; A/C=2-141.
DR   PDB; 1RVW; X-ray; 2.50 A; A=2-142.
DR   PDB; 1SDK; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1SDL; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1SHR; X-ray; 1.88 A; A/C=2-142.
DR   PDB; 1SI4; X-ray; 2.20 A; A/C=2-142.
DR   PDB; 1THB; X-ray; 1.50 A; A/C=2-142.
DR   PDB; 1UIW; X-ray; 1.50 A; A/C/E/G=2-142.
DR   PDB; 1VWT; X-ray; 1.90 A; A/C=2-141.
DR   PDB; 1XXT; X-ray; 1.91 A; A/C=2-142.
DR   PDB; 1XY0; X-ray; 1.99 A; A/C=3-142.
DR   PDB; 1XYE; X-ray; 2.13 A; A/C=3-142.
DR   PDB; 1XZ2; X-ray; 1.90 A; A/C=1-142.
DR   PDB; 1XZ4; X-ray; 2.00 A; A/C=3-142.
DR   PDB; 1XZ5; X-ray; 2.11 A; A/C=3-142.
DR   PDB; 1XZ7; X-ray; 1.90 A; A/C=3-142.
DR   PDB; 1XZU; X-ray; 2.16 A; A/C=3-142.
DR   PDB; 1XZV; X-ray; 2.11 A; A/C=3-142.
DR   PDB; 1Y01; X-ray; 2.80 A; B=2-141.
DR   PDB; 1Y09; X-ray; 2.25 A; A/C=3-142.
DR   PDB; 1Y0A; X-ray; 2.22 A; A/C=3-142.
DR   PDB; 1Y0C; X-ray; 2.30 A; A/C=3-142.
DR   PDB; 1Y0D; X-ray; 2.10 A; A/C=2-140.
DR   PDB; 1Y0T; X-ray; 2.14 A; A/C=1-142.
DR   PDB; 1Y0W; X-ray; 2.14 A; A/C=1-142.
DR   PDB; 1Y22; X-ray; 2.16 A; A/C=1-142.
DR   PDB; 1Y2Z; X-ray; 2.07 A; A/C=1-142.
DR   PDB; 1Y31; X-ray; 2.13 A; A/C=2-141.
DR   PDB; 1Y35; X-ray; 2.12 A; A/C=1-142.
DR   PDB; 1Y45; X-ray; 2.00 A; A/C=1-142.
DR   PDB; 1Y46; X-ray; 2.22 A; A/C=2-141.
DR   PDB; 1Y4B; X-ray; 2.10 A; A/C=1-142.
DR   PDB; 1Y4F; X-ray; 2.00 A; A/C=2-141.
DR   PDB; 1Y4G; X-ray; 1.91 A; A/C=2-141.
DR   PDB; 1Y4P; X-ray; 1.98 A; A/C=2-141.
DR   PDB; 1Y4Q; X-ray; 2.11 A; A/C=1-142.
DR   PDB; 1Y4R; X-ray; 2.22 A; A/C=1-142.
DR   PDB; 1Y4V; X-ray; 1.84 A; A/C=1-142.
DR   PDB; 1Y5F; X-ray; 2.14 A; A/C=1-142.
DR   PDB; 1Y5J; X-ray; 2.03 A; A/C=1-142.
DR   PDB; 1Y5K; X-ray; 2.20 A; A/C=1-142.
DR   PDB; 1Y7C; X-ray; 2.10 A; A/C=1-142.
DR   PDB; 1Y7D; X-ray; 1.90 A; A/C=1-142.
DR   PDB; 1Y7G; X-ray; 2.10 A; A/C=1-142.
DR   PDB; 1Y7Z; X-ray; 1.98 A; A/C=1-142.
DR   PDB; 1Y83; X-ray; 1.90 A; A/C=1-142.
DR   PDB; 1Y85; X-ray; 2.13 A; A/C=2-141.
DR   PDB; 1Y8W; X-ray; 2.90 A; A/C=3-142.
DR   PDB; 1YDZ; X-ray; 3.30 A; A/C=3-142.
DR   PDB; 1YE0; X-ray; 2.50 A; A/C=1-142.
DR   PDB; 1YE1; X-ray; 4.50 A; A/C=1-142.
DR   PDB; 1YE2; X-ray; 1.80 A; A/C=1-142.
DR   PDB; 1YEN; X-ray; 2.80 A; A/C=1-142.
DR   PDB; 1YEO; X-ray; 2.22 A; A/C=1-142.
DR   PDB; 1YEQ; X-ray; 2.75 A; A/C=1-142.
DR   PDB; 1YEU; X-ray; 2.12 A; A/C=1-142.
DR   PDB; 1YEV; X-ray; 2.11 A; A/C=1-142.
DR   PDB; 1YFF; X-ray; 2.40 A; A/C/E/G=2-142.
DR   PDB; 1YG5; X-ray; 2.70 A; A/C=1-142.
DR   PDB; 1YGD; X-ray; 2.73 A; A/C=1-142.
DR   PDB; 1YGF; X-ray; 2.70 A; A/C=1-142.
DR   PDB; 1YH9; X-ray; 2.20 A; A/C=1-142.
DR   PDB; 1YHE; X-ray; 2.10 A; A/C=1-142.
DR   PDB; 1YHR; X-ray; 2.60 A; A/C=1-142.
DR   PDB; 1YIE; X-ray; 2.40 A; A/C=1-142.
DR   PDB; 1YIH; X-ray; 2.00 A; A/C=1-142.
DR   PDB; 1YVQ; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 1YVT; X-ray; 1.80 A; A=1-142.
DR   PDB; 1YZI; X-ray; 2.07 A; A=1-142.
DR   PDB; 1Z8U; X-ray; 2.40 A; B/D=1-142.
DR   PDB; 2D5Z; X-ray; 1.45 A; A/C=1-142.
DR   PDB; 2D60; X-ray; 1.70 A; A/C=1-142.
DR   PDB; 2DN1; X-ray; 1.25 A; A=2-141.
DR   PDB; 2DN2; X-ray; 1.25 A; A/C=2-141.
DR   PDB; 2DN3; X-ray; 1.25 A; A=1-142.
DR   PDB; 2DXM; Neutron; 2.10 A; A/C=2-142.
DR   PDB; 2H35; NMR; -; A=1-142, C=2-142.
DR   PDB; 2HBC; X-ray; 2.10 A; A=1-142.
DR   PDB; 2HBD; X-ray; 2.20 A; A=2-142.
DR   PDB; 2HBE; X-ray; 2.00 A; A=1-142.
DR   PDB; 2HBF; X-ray; 2.20 A; A=1-142.
DR   PDB; 2HBS; X-ray; 2.05 A; A/C/E/G=1-142.
DR   PDB; 2HCO; X-ray; 2.70 A; A=2-142.
DR   PDB; 2HHB; X-ray; 1.74 A; A/C=2-142.
DR   PDB; 2HHD; X-ray; 2.20 A; A/C=2-142.
DR   PDB; 2HHE; X-ray; 2.20 A; A/C=1-142.
DR   PDB; 2W6V; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 2W72; X-ray; 1.07 A; A=2-142, C=3-142.
DR   PDB; 2YRS; X-ray; 2.30 A; A/C/I/M=2-142.
DR   PDB; 3B75; X-ray; 2.30 A; A/C/E/G/S=2-142.
DR   PDB; 3D17; X-ray; 2.80 A; A/C=2-142.
DR   PDB; 3D7O; X-ray; 1.80 A; A=2-142.
DR   PDB; 3DUT; X-ray; 1.55 A; A/C=2-142.
DR   PDB; 3HHB; X-ray; 1.74 A; A/C=2-142.
DR   PDB; 3HXN; X-ray; 2.00 A; A/C=2-142.
DR   PDB; 3IA3; X-ray; 3.20 A; B/D=2-142.
DR   PDB; 3IC0; X-ray; 1.80 A; A/C=2-141.
DR   PDB; 3IC2; X-ray; 2.40 A; A/C=2-142.
DR   PDB; 3KMF; Neutron; 2.00 A; A/E=2-142.
DR   PDB; 3NL7; X-ray; 1.80 A; A=2-142.
DR   PDB; 3NMM; X-ray; 1.60 A; A/C=2-142.
DR   PDB; 3ODQ; X-ray; 3.10 A; A/C=2-142.
DR   PDB; 3ONZ; X-ray; 2.09 A; A=2-142.
DR   PDB; 3OO4; X-ray; 1.90 A; A=2-142.
DR   PDB; 3OO5; X-ray; 2.10 A; A=2-142.
DR   PDB; 3OVU; X-ray; 2.83 A; C=2-142.
DR   PDB; 3P5Q; X-ray; 2.00 A; A=2-142.
DR   PDB; 3QJB; X-ray; 1.80 A; A=2-142.
DR   PDB; 3QJC; X-ray; 2.00 A; A=2-142.
DR   PDB; 3QJD; X-ray; 1.56 A; A/C=2-142.
DR   PDB; 3QJE; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 3R5I; X-ray; 2.20 A; A/C=2-142.
DR   PDB; 3S65; X-ray; 1.80 A; A/C=2-142.
DR   PDB; 3S66; X-ray; 1.40 A; A=2-142.
DR   PDB; 3SZK; X-ray; 3.01 A; A/D=2-142.
DR   PDB; 4HHB; X-ray; 1.74 A; A/C=1-142.
DR   PDB; 6HBW; X-ray; 2.00 A; A/C=1-142.
DR   PDBsum; 1A00; -.
DR   PDBsum; 1A01; -.
DR   PDBsum; 1A0U; -.
DR   PDBsum; 1A0Z; -.
DR   PDBsum; 1A3N; -.
DR   PDBsum; 1A3O; -.
DR   PDBsum; 1A9W; -.
DR   PDBsum; 1ABW; -.
DR   PDBsum; 1ABY; -.
DR   PDBsum; 1AJ9; -.
DR   PDBsum; 1B86; -.
DR   PDBsum; 1BAB; -.
DR   PDBsum; 1BBB; -.
DR   PDBsum; 1BIJ; -.
DR   PDBsum; 1BUW; -.
DR   PDBsum; 1BZ0; -.
DR   PDBsum; 1BZ1; -.
DR   PDBsum; 1BZZ; -.
DR   PDBsum; 1C7B; -.
DR   PDBsum; 1C7C; -.
DR   PDBsum; 1C7D; -.
DR   PDBsum; 1CLS; -.
DR   PDBsum; 1CMY; -.
DR   PDBsum; 1COH; -.
DR   PDBsum; 1DKE; -.
DR   PDBsum; 1DXT; -.
DR   PDBsum; 1DXU; -.
DR   PDBsum; 1DXV; -.
DR   PDBsum; 1FDH; -.
DR   PDBsum; 1FN3; -.
DR   PDBsum; 1G9V; -.
DR   PDBsum; 1GBU; -.
DR   PDBsum; 1GBV; -.
DR   PDBsum; 1GLI; -.
DR   PDBsum; 1GZX; -.
DR   PDBsum; 1HAB; -.
DR   PDBsum; 1HAC; -.
DR   PDBsum; 1HBA; -.
DR   PDBsum; 1HBB; -.
DR   PDBsum; 1HBS; -.
DR   PDBsum; 1HCO; -.
DR   PDBsum; 1HDB; -.
DR   PDBsum; 1HGA; -.
DR   PDBsum; 1HGB; -.
DR   PDBsum; 1HGC; -.
DR   PDBsum; 1HHO; -.
DR   PDBsum; 1IRD; -.
DR   PDBsum; 1J3Y; -.
DR   PDBsum; 1J3Z; -.
DR   PDBsum; 1J40; -.
DR   PDBsum; 1J41; -.
DR   PDBsum; 1J7S; -.
DR   PDBsum; 1J7W; -.
DR   PDBsum; 1J7Y; -.
DR   PDBsum; 1JY7; -.
DR   PDBsum; 1K0Y; -.
DR   PDBsum; 1K1K; -.
DR   PDBsum; 1KD2; -.
DR   PDBsum; 1LFL; -.
DR   PDBsum; 1LFQ; -.
DR   PDBsum; 1LFT; -.
DR   PDBsum; 1LFV; -.
DR   PDBsum; 1LFY; -.
DR   PDBsum; 1LFZ; -.
DR   PDBsum; 1LJW; -.
DR   PDBsum; 1M9P; -.
DR   PDBsum; 1MKO; -.
DR   PDBsum; 1NEJ; -.
DR   PDBsum; 1NIH; -.
DR   PDBsum; 1NQP; -.
DR   PDBsum; 1O1I; -.
DR   PDBsum; 1O1J; -.
DR   PDBsum; 1O1K; -.
DR   PDBsum; 1O1L; -.
DR   PDBsum; 1O1M; -.
DR   PDBsum; 1O1N; -.
DR   PDBsum; 1O1O; -.
DR   PDBsum; 1O1P; -.
DR   PDBsum; 1QI8; -.
DR   PDBsum; 1QSH; -.
DR   PDBsum; 1QSI; -.
DR   PDBsum; 1QXD; -.
DR   PDBsum; 1QXE; -.
DR   PDBsum; 1R1X; -.
DR   PDBsum; 1R1Y; -.
DR   PDBsum; 1RPS; -.
DR   PDBsum; 1RQ3; -.
DR   PDBsum; 1RQ4; -.
DR   PDBsum; 1RQA; -.
DR   PDBsum; 1RVW; -.
DR   PDBsum; 1SDK; -.
DR   PDBsum; 1SDL; -.
DR   PDBsum; 1SHR; -.
DR   PDBsum; 1SI4; -.
DR   PDBsum; 1THB; -.
DR   PDBsum; 1UIW; -.
DR   PDBsum; 1VWT; -.
DR   PDBsum; 1XXT; -.
DR   PDBsum; 1XY0; -.
DR   PDBsum; 1XYE; -.
DR   PDBsum; 1XZ2; -.
DR   PDBsum; 1XZ4; -.
DR   PDBsum; 1XZ5; -.
DR   PDBsum; 1XZ7; -.
DR   PDBsum; 1XZU; -.
DR   PDBsum; 1XZV; -.
DR   PDBsum; 1Y01; -.
DR   PDBsum; 1Y09; -.
DR   PDBsum; 1Y0A; -.
DR   PDBsum; 1Y0C; -.
DR   PDBsum; 1Y0D; -.
DR   PDBsum; 1Y0T; -.
DR   PDBsum; 1Y0W; -.
DR   PDBsum; 1Y22; -.
DR   PDBsum; 1Y2Z; -.
DR   PDBsum; 1Y31; -.
DR   PDBsum; 1Y35; -.
DR   PDBsum; 1Y45; -.
DR   PDBsum; 1Y46; -.
DR   PDBsum; 1Y4B; -.
DR   PDBsum; 1Y4F; -.
DR   PDBsum; 1Y4G; -.
DR   PDBsum; 1Y4P; -.
DR   PDBsum; 1Y4Q; -.
DR   PDBsum; 1Y4R; -.
DR   PDBsum; 1Y4V; -.
DR   PDBsum; 1Y5F; -.
DR   PDBsum; 1Y5J; -.
DR   PDBsum; 1Y5K; -.
DR   PDBsum; 1Y7C; -.
DR   PDBsum; 1Y7D; -.
DR   PDBsum; 1Y7G; -.
DR   PDBsum; 1Y7Z; -.
DR   PDBsum; 1Y83; -.
DR   PDBsum; 1Y85; -.
DR   PDBsum; 1Y8W; -.
DR   PDBsum; 1YDZ; -.
DR   PDBsum; 1YE0; -.
DR   PDBsum; 1YE1; -.
DR   PDBsum; 1YE2; -.
DR   PDBsum; 1YEN; -.
DR   PDBsum; 1YEO; -.
DR   PDBsum; 1YEQ; -.
DR   PDBsum; 1YEU; -.
DR   PDBsum; 1YEV; -.
DR   PDBsum; 1YFF; -.
DR   PDBsum; 1YG5; -.
DR   PDBsum; 1YGD; -.
DR   PDBsum; 1YGF; -.
DR   PDBsum; 1YH9; -.
DR   PDBsum; 1YHE; -.
DR   PDBsum; 1YHR; -.
DR   PDBsum; 1YIE; -.
DR   PDBsum; 1YIH; -.
DR   PDBsum; 1YVQ; -.
DR   PDBsum; 1YVT; -.
DR   PDBsum; 1YZI; -.
DR   PDBsum; 1Z8U; -.
DR   PDBsum; 2D5Z; -.
DR   PDBsum; 2D60; -.
DR   PDBsum; 2DN1; -.
DR   PDBsum; 2DN2; -.
DR   PDBsum; 2DN3; -.
DR   PDBsum; 2DXM; -.
DR   PDBsum; 2H35; -.
DR   PDBsum; 2HBC; -.
DR   PDBsum; 2HBD; -.
DR   PDBsum; 2HBE; -.
DR   PDBsum; 2HBF; -.
DR   PDBsum; 2HBS; -.
DR   PDBsum; 2HCO; -.
DR   PDBsum; 2HHB; -.
DR   PDBsum; 2HHD; -.
DR   PDBsum; 2HHE; -.
DR   PDBsum; 2W6V; -.
DR   PDBsum; 2W72; -.
DR   PDBsum; 2YRS; -.
DR   PDBsum; 3B75; -.
DR   PDBsum; 3D17; -.
DR   PDBsum; 3D7O; -.
DR   PDBsum; 3DUT; -.
DR   PDBsum; 3HHB; -.
DR   PDBsum; 3HXN; -.
DR   PDBsum; 3IA3; -.
DR   PDBsum; 3IC0; -.
DR   PDBsum; 3IC2; -.
DR   PDBsum; 3KMF; -.
DR   PDBsum; 3NL7; -.
DR   PDBsum; 3NMM; -.
DR   PDBsum; 3ODQ; -.
DR   PDBsum; 3ONZ; -.
DR   PDBsum; 3OO4; -.
DR   PDBsum; 3OO5; -.
DR   PDBsum; 3OVU; -.
DR   PDBsum; 3P5Q; -.
DR   PDBsum; 3QJB; -.
DR   PDBsum; 3QJC; -.
DR   PDBsum; 3QJD; -.
DR   PDBsum; 3QJE; -.
DR   PDBsum; 3R5I; -.
DR   PDBsum; 3S65; -.
DR   PDBsum; 3S66; -.
DR   PDBsum; 3SZK; -.
DR   PDBsum; 4HHB; -.
DR   PDBsum; 6HBW; -.
DR   ProteinModelPortal; P69905; -.
DR   SMR; P69905; 2-142.
DR   IntAct; P69905; 15.
DR   MINT; MINT-1519936; -.
DR   STRING; P69905; -.
DR   PhosphoSite; P69905; -.
DR   DOSAC-COBS-2DPAGE; P69905; -.
DR   REPRODUCTION-2DPAGE; IPI00410714; -.
DR   Siena-2DPAGE; P69905; -.
DR   SWISS-2DPAGE; P69905; -.
DR   UCD-2DPAGE; P01922; -.
DR   UCD-2DPAGE; P69905; -.
DR   PeptideAtlas; P69905; -.
DR   PRIDE; P69905; -.
DR   DNASU; 3039; -.
DR   Ensembl; ENST00000251595; ENSP00000251595; ENSG00000188536.
DR   Ensembl; ENST00000320868; ENSP00000322421; ENSG00000206172.
DR   GeneID; 3039; -.
DR   GeneID; 3040; -.
DR   KEGG; hsa:3039; -.
DR   KEGG; hsa:3040; -.
DR   UCSC; uc002cfv.4; human.
DR   CTD; 3039; -.
DR   CTD; 3040; -.
DR   GeneCards; GC16P000257; -.
DR   GeneCards; GC16P000258; -.
DR   HGNC; HGNC:4823; HBA1.
DR   HGNC; HGNC:4824; HBA2.
DR   HPA; CAB032534; -.
DR   HPA; CAB038417; -.
DR   HPA; HPA043780; -.
DR   MIM; 140700; phenotype.
DR   MIM; 141800; gene+phenotype.
DR   MIM; 141850; gene.
DR   MIM; 141860; gene.
DR   MIM; 604131; phenotype.
DR   MIM; 613978; phenotype.
DR   neXtProt; NX_P69905; -.
DR   Orphanet; 98791; Alpha thalassemia - intellectual deficit syndrome.
DR   Orphanet; 93616; Hemoglobin H disease.
DR   Orphanet; 163596; Hydrops fetalis of Bart.
DR   PharmGKB; PA29199; -.
DR   eggNOG; NOG283543; -.
DR   GeneTree; ENSGT00650000093280; -.
DR   HOVERGEN; HBG009709; -.
DR   InParanoid; P69905; -.
DR   KO; K13822; -.
DR   OMA; TPEVHAS; -.
DR   OrthoDB; EOG47M209; -.
DR   DrugBank; DB00613; Amodiaquine.
DR   DrugBank; DB00608; Chloroquine.
DR   DrugBank; DB00893; Iron Dextran.
DR   DrugBank; DB00358; Mefloquine.
DR   DrugBank; DB01087; Primaquine.
DR   DrugBank; DB00468; Quinine.
DR   EvolutionaryTrace; P69905; -.
DR   NextBio; 12034; -.
DR   PMAP-CutDB; P69905; -.
DR   ArrayExpress; P69905; -.
DR   Bgee; P69905; -.
DR   CleanEx; HS_HBA1; -.
DR   CleanEx; HS_HBA2; -.
DR   Genevestigator; P69905; -.
DR   GermOnline; ENSG00000188536; Homo sapiens.
DR   GermOnline; ENSG00000206172; Homo sapiens.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL.
DR   GO; GO:0005833; C:hemoglobin complex; TAS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
DR   GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL.
DR   GO; GO:0051291; P:protein heterooligomerization; IDA:BHF-UCL.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR012292; Globin_dom.
DR   InterPro; IPR002338; Haemoglobin_a.
DR   InterPro; IPR018331; Haemoglobin_alpha_chain.
DR   InterPro; IPR002339; Haemoglobin_pi.
DR   PANTHER; PTHR11442:SF14; Pi_haem; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
DR   SUPFAM; SSF46458; Globin_like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   Disease mutation; Glycation; Glycoprotein; Heme;
KW   Hereditary hemolytic anemia; Iron; Metal-binding; Oxygen transport;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    142       Hemoglobin subunit alpha.
FT                                /FTId=PRO_0000052653.
FT   METAL        59     59       Iron (heme distal ligand).
FT   METAL        88     88       Iron (heme proximal ligand).
FT   SITE         12     12       Not glycated.
FT   SITE         57     57       Not glycated.
FT   SITE         61     61       Not glycated.
FT   SITE         91     91       Not glycated.
FT   SITE        100    100       Not glycated.
FT   MOD_RES      25     25       Phosphotyrosine.
FT   MOD_RES      43     43       Phosphotyrosine.
FT   CARBOHYD      8      8       N-linked (Glc) (glycation).
FT   CARBOHYD     17     17       N-linked (Glc) (glycation).
FT   CARBOHYD     41     41       N-linked (Glc) (glycation).
FT   CARBOHYD     62     62       N-linked (Glc) (glycation).
FT   VARIANT       2      2       V -> E (in Thionville; O(2) affinity
FT                                down).
FT                                /FTId=VAR_002719.
FT   VARIANT       3      3       L -> R (in ChongQing; O(2) affinity up;
FT                                dbSNP:rs36030576).
FT                                /FTId=VAR_002720.
FT   VARIANT       6      6       A -> D (in J-Toronto; dbSNP:rs34090856).
FT                                /FTId=VAR_002721.
FT   VARIANT       6      6       A -> P (in Karachi; dbSNP:rs34751764).
FT                                /FTId=VAR_002722.
FT   VARIANT       7      7       D -> A (in Sawara; O(2) affinity up;
FT                                dbSNP:rs33986902).
FT                                /FTId=VAR_002723.
FT   VARIANT       7      7       D -> G (in Swan River).
FT                                /FTId=VAR_002724.
FT   VARIANT       7      7       D -> N (in Dunn; O(2) affinity up;
FT                                dbSNP:rs33961916).
FT                                /FTId=VAR_002725.
FT   VARIANT       7      7       D -> V (in Ferndown; O(2) affinity up).
FT                                /FTId=VAR_002726.
FT   VARIANT       7      7       D -> Y (in Woodville; O(2) affinity up).
FT                                /FTId=VAR_002727.
FT   VARIANT       8      8       K -> E (in Kurosaki; dbSNP:rs34817956).
FT                                /FTId=VAR_002728.
FT   VARIANT      10     10       N -> T (in Broomfield).
FT                                /FTId=VAR_038149.
FT   VARIANT      11     11       V -> F (in dbSNP:rs1799896).
FT                                /FTId=VAR_014605.
FT   VARIANT      12     12       K -> E (in Anantharaj).
FT                                /FTId=VAR_002729.
FT   VARIANT      13     13       A -> D (in J-Paris 1/J-Aljezur;
FT                                dbSNP:rs35615982).
FT                                /FTId=VAR_002730.
FT   VARIANT      14     14       A -> P (in Ravenscourt Park; causes
FT                                alpha-thalassemia; dbSNP:rs35331909).
FT                                /FTId=VAR_038150.
FT   VARIANT      15     15       W -> R (in Evanston; O(2) affinity up;
FT                                dbSNP:rs33964317).
FT                                /FTId=VAR_002731.
FT   VARIANT      16     16       G -> R (in Ottawa/Siam;
FT                                dbSNP:rs35816645).
FT                                /FTId=VAR_002732.
FT   VARIANT      17     17       K -> M (in Harbin; slightly unstable;
FT                                dbSNP:rs35210126).
FT                                /FTId=VAR_002733.
FT   VARIANT      17     17       K -> N (in Beijing; dbSNP:rs33923844).
FT                                /FTId=VAR_002734.
FT   VARIANT      19     19       G -> D (in Al-Ain Abu Dhabi;
FT                                dbSNP:rs35993097).
FT                                /FTId=VAR_002735.
FT   VARIANT      19     19       G -> R (in Handsworth; dbSNP:rs34504387).
FT                                /FTId=VAR_002736.
FT   VARIANT      20     20       A -> D (in J-Kurosh).
FT                                /FTId=VAR_002737.
FT   VARIANT      20     20       A -> E (in J-Tashikuergan;
FT                                dbSNP:rs35628685).
FT                                /FTId=VAR_002738.
FT   VARIANT      21     21       H -> Q (in Le Lamentin;
FT                                dbSNP:rs41525149).
FT                                /FTId=VAR_002739.
FT   VARIANT      21     21       H -> R (in Hobart; dbSNP:rs33943087).
FT                                /FTId=VAR_002740.
FT   VARIANT      22     22       A -> D (in J-Nyanza; dbSNP:rs11548605).
FT                                /FTId=VAR_002741.
FT   VARIANT      22     22       A -> P (in Fontainebleau;
FT                                dbSNP:rs34324664).
FT                                /FTId=VAR_002742.
FT   VARIANT      23     23       G -> D (in J-Medellin; dbSNP:rs34608326).
FT                                /FTId=VAR_002743.
FT   VARIANT      24     24       E -> G (in Reims; slightly unstable;
FT                                dbSNP:rs33939421).
FT                                /FTId=VAR_002744.
FT   VARIANT      24     24       E -> K (in Chad).
FT                                /FTId=VAR_002745.
FT   VARIANT      25     25       Y -> H (in Luxembourg; unstable).
FT                                /FTId=VAR_002746.
FT   VARIANT      27     27       A -> E (in Shenyang; unstable).
FT                                /FTId=VAR_002747.
FT   VARIANT      27     27       A -> V (in Campinas).
FT                                /FTId=VAR_025387.
FT   VARIANT      28     28       E -> D (in Hekinan).
FT                                /FTId=VAR_002748.
FT   VARIANT      28     28       E -> G (in Fort Worth).
FT                                /FTId=VAR_002749.
FT   VARIANT      28     28       E -> V (in Spanish town).
FT                                /FTId=VAR_002750.
FT   VARIANT      31     31       E -> K (in O-Padova).
FT                                /FTId=VAR_002751.
FT   VARIANT      32     32       R -> K (causes alpha-thalassemia).
FT                                /FTId=VAR_025002.
FT   VARIANT      32     32       R -> S (in Prato; unstable).
FT                                /FTId=VAR_002752.
FT   VARIANT      35     35       L -> R (in Queens/Ogi).
FT                                /FTId=VAR_002753.
FT   VARIANT      38     38       P -> PE (in Catonsville).
FT                                /FTId=VAR_002755.
FT   VARIANT      38     38       P -> R (in Bourmedes).
FT                                /FTId=VAR_002754.
FT   VARIANT      41     41       K -> M (in Kanagawa; O(2) affinity up).
FT                                /FTId=VAR_002756.
FT   VARIANT      42     42       T -> S (in Miyano; O(2) affinity up).
FT                                /FTId=VAR_002757.
FT   VARIANT      44     44       F -> L (in Hirosaki; unstable).
FT                                /FTId=VAR_002758.
FT   VARIANT      45     45       P -> L (in Milledgeville; O(2) affinity
FT                                up; dbSNP:rs41514946).
FT                                /FTId=VAR_002759.
FT   VARIANT      45     45       P -> R (in Kawachi; O(2) affinity up).
FT                                /FTId=VAR_002760.
FT   VARIANT      46     46       H -> Q (in Bari).
FT                                /FTId=VAR_002761.
FT   VARIANT      46     46       H -> R (in Fort de France; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002762.
FT   VARIANT      48     48       D -> A (in Cordele; unstable).
FT                                /FTId=VAR_002763.
FT   VARIANT      48     48       D -> G (in Umi/Michigan; unstable).
FT                                /FTId=VAR_002764.
FT   VARIANT      48     48       D -> H (in Hasharon/Sinai; unstable).
FT                                /FTId=VAR_002765.
FT   VARIANT      48     48       D -> Y (in Kurdistan).
FT                                /FTId=VAR_002766.
FT   VARIANT      49     49       L -> R (in Montgomery).
FT                                /FTId=VAR_002767.
FT   VARIANT      50     50       S -> R (in Savaria).
FT                                /FTId=VAR_002768.
FT   VARIANT      51     51       H -> R (in Aichi; slightly unstable).
FT                                /FTId=VAR_002769.
FT   VARIANT      52     52       G -> D (in J-Abidjan).
FT                                /FTId=VAR_002770.
FT   VARIANT      52     52       G -> R (in Russ).
FT                                /FTId=VAR_002771.
FT   VARIANT      54     54       A -> D (in J-Rovigo; unstable).
FT                                /FTId=VAR_002772.
FT   VARIANT      55     55       Q -> R (in Hikoshima/Shimonoseki).
FT                                /FTId=VAR_002773.
FT   VARIANT      57     57       K -> R (in Port Huron).
FT                                /FTId=VAR_002774.
FT   VARIANT      57     57       K -> T (in Thailand).
FT                                /FTId=VAR_002775.
FT   VARIANT      58     58       G -> R (in L-Persian Gulf).
FT                                /FTId=VAR_002776.
FT   VARIANT      59     59       H -> Q (in Boghe).
FT                                /FTId=VAR_025388.
FT   VARIANT      59     59       H -> Y (in M-Boston/M-Osaka; O(2)
FT                                affinity down).
FT                                /FTId=VAR_002777.
FT   VARIANT      60     60       G -> D (in Adana; unstable; causes alpha-
FT                                thalassemia; dbSNP:rs28928878).
FT                                /FTId=VAR_002778.
FT   VARIANT      60     60       G -> V (in Tottori; unstable).
FT                                /FTId=VAR_002779.
FT   VARIANT      61     61       K -> N (in Zambia; dbSNP:rs28928887).
FT                                /FTId=VAR_002780.
FT   VARIANT      61     61       Missing (in Clinic; unstable; causes
FT                                alpha-thalassemia).
FT                                /FTId=VAR_002781.
FT   VARIANT      62     62       K -> N (in J-Buda).
FT                                /FTId=VAR_002782.
FT   VARIANT      62     62       K -> T (in J-Anatolia).
FT                                /FTId=VAR_002783.
FT   VARIANT      63     63       V -> M (in Evans; unstable).
FT                                /FTId=VAR_002784.
FT   VARIANT      63     63       Missing (in HBH; hemoglobin Aghia
FT                                Sophia).
FT                                /FTId=VAR_066401.
FT   VARIANT      64     64       A -> D (in Pontoise; unstable).
FT                                /FTId=VAR_002785.
FT   VARIANT      65     65       D -> Y (in Persepolis).
FT                                /FTId=VAR_002786.
FT   VARIANT      69     69       N -> K (in G-Philadelphia;
FT                                dbSNP:rs1060339).
FT                                /FTId=VAR_002787.
FT   VARIANT      72     72       A -> E (in J-Habana).
FT                                /FTId=VAR_002788.
FT   VARIANT      72     72       A -> V (in Ozieri).
FT                                /FTId=VAR_002789.
FT   VARIANT      73     73       H -> R (in Daneskgah-Teheran).
FT                                /FTId=VAR_002790.
FT   VARIANT      75     75       D -> A (in Lille).
FT                                /FTId=VAR_002791.
FT   VARIANT      75     75       D -> G (in Chapel Hill).
FT                                /FTId=VAR_002792.
FT   VARIANT      75     75       D -> N (in G-Pest).
FT                                /FTId=VAR_002793.
FT   VARIANT      76     76       D -> A (in Duan).
FT                                /FTId=VAR_002794.
FT   VARIANT      76     76       D -> H (in Q-Iran).
FT                                /FTId=VAR_002795.
FT   VARIANT      77     77       M -> K (in Noko).
FT                                /FTId=VAR_002796.
FT   VARIANT      77     77       M -> T (in Aztec).
FT                                /FTId=VAR_002797.
FT   VARIANT      78     78       P -> R (in Guizhou).
FT                                /FTId=VAR_002798.
FT   VARIANT      79     79       N -> H (in Davenport).
FT                                /FTId=VAR_002799.
FT   VARIANT      79     79       N -> K (in Stanleyville-2).
FT                                /FTId=VAR_002800.
FT   VARIANT      80     80       A -> G (in Singapore).
FT                                /FTId=VAR_012662.
FT   VARIANT      81     81       L -> R (in Ann Arbor; unstable).
FT                                /FTId=VAR_002801.
FT   VARIANT      82     82       S -> C (in Nigeria).
FT                                /FTId=VAR_002802.
FT   VARIANT      83     83       A -> D (in Garden State).
FT                                /FTId=VAR_002803.
FT   VARIANT      85     85       S -> R (in Etobicoke; O(2) affinity up).
FT                                /FTId=VAR_002804.
FT   VARIANT      86     86       D -> V (in Inkster; O(2) affinity up).
FT                                /FTId=VAR_002805.
FT   VARIANT      86     86       D -> Y (in Atago; O(2) affinity up).
FT                                /FTId=VAR_002806.
FT   VARIANT      87     87       L -> R (in Moabit; unstable).
FT                                /FTId=VAR_002807.
FT   VARIANT      88     88       H -> N (in Auckland; unstable).
FT                                /FTId=VAR_002808.
FT   VARIANT      88     88       H -> R (in Iwata; unstable).
FT                                /FTId=VAR_002809.
FT   VARIANT      89     89       A -> S (in Loire; O(2) affinity up).
FT                                /FTId=VAR_002810.
FT   VARIANT      91     91       K -> M (in Handa; O(2) affinity up).
FT                                /FTId=VAR_002811.
FT   VARIANT      92     92       L -> F (in dbSNP:rs17407508).
FT                                /FTId=VAR_049272.
FT   VARIANT      92     92       L -> P (in Port Phillip; unstable;
FT                                dbSNP:rs17407508).
FT                                /FTId=VAR_002812.
FT   VARIANT      93     93       R -> Q (in J-Cape Town; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002813.
FT   VARIANT      93     93       R -> W (in Cemenelum; O(2) affinity up).
FT                                /FTId=VAR_020775.
FT   VARIANT      95     95       D -> A (in Bassett; markedly reduced
FT                                oxygen affinity).
FT                                /FTId=VAR_025389.
FT   VARIANT      95     95       D -> Y (in Setif; unstable).
FT                                /FTId=VAR_002814.
FT   VARIANT      96     96       P -> A (in Denmark Hill; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002815.
FT   VARIANT      96     96       P -> T (in Godavari; O(2) affinity up).
FT                                /FTId=VAR_002816.
FT   VARIANT      98     98       N -> K (in Dallas; O(2) affinity up).
FT                                /FTId=VAR_002817.
FT   VARIANT     100    100       K -> E (in Turriff).
FT                                /FTId=VAR_002818.
FT   VARIANT     103    103       S -> R (in Manitoba; slightly unstable;
FT                                dbSNP:rs41344646).
FT                                /FTId=VAR_002819.
FT   VARIANT     104    104       H -> R (in Contaldo; unstable).
FT                                /FTId=VAR_002820.
FT   VARIANT     104    104       H -> Y (in Charolles).
FT                                /FTId=VAR_025390.
FT   VARIANT     110    110       L -> R (in Suan-Dok; unstable; causes
FT                                alpha-thalassemia).
FT                                /FTId=VAR_002821.
FT   VARIANT     111    111       A -> D (in Petah Tikva; unstable; causes
FT                                alpha-thalassemia).
FT                                /FTId=VAR_002822.
FT   VARIANT     113    113       H -> D (in Hopkins-II; unstable).
FT                                /FTId=VAR_002823.
FT   VARIANT     114    114       L -> H (in Twin Peaks).
FT                                /FTId=VAR_002824.
FT   VARIANT     115    115       P -> L (in Nouakchott).
FT                                /FTId=VAR_002825.
FT   VARIANT     115    115       P -> R (in Chiapas).
FT                                /FTId=VAR_002826.
FT   VARIANT     115    115       P -> S (in Melusine).
FT                                /FTId=VAR_002827.
FT   VARIANT     116    116       A -> D (in J-Tongariki).
FT                                /FTId=VAR_002828.
FT   VARIANT     117    117       E -> A (in Ube-4).
FT                                /FTId=VAR_002829.
FT   VARIANT     117    117       E -> EHLPAE (in Zaire).
FT                                /FTId=VAR_002830.
FT   VARIANT     118    118       F -> FI (in Phnom Penh).
FT                                /FTId=VAR_002831.
FT   VARIANT     119    119       T -> TEFT (in Grady).
FT                                /FTId=VAR_002832.
FT   VARIANT     121    121       A -> E (in J-Meerut/J-Birmingham).
FT                                /FTId=VAR_002833.
FT   VARIANT     122    122       V -> M (in Owari).
FT                                /FTId=VAR_002834.
FT   VARIANT     123    123       H -> Q (in Westmead).
FT                                /FTId=VAR_002835.
FT   VARIANT     126    126       L -> P (in Quong Sze; causes alpha-
FT                                thalassemia).
FT                                /FTId=VAR_002836.
FT   VARIANT     126    126       L -> R (in Plasencia; family with
FT                                moderate microcytosis and hypochromia).
FT                                /FTId=VAR_025391.
FT   VARIANT     127    127       D -> G (in West One).
FT                                /FTId=VAR_025392.
FT   VARIANT     127    127       D -> V (in Fukutomi; O(2) affinity up).
FT                                /FTId=VAR_002837.
FT   VARIANT     127    127       D -> Y (in Monteriore; O(2) affinity up).
FT                                /FTId=VAR_002838.
FT   VARIANT     128    128       K -> N (in Jackson).
FT                                /FTId=VAR_002839.
FT   VARIANT     130    130       L -> P (in Tunis-Bizerte; unstable;
FT                                causes alpha-thalassemia).
FT                                /FTId=VAR_002840.
FT   VARIANT     131    131       A -> D (in Yuda; O(2) affinity down).
FT                                /FTId=VAR_002842.
FT   VARIANT     131    131       A -> P (in Sun Prairie; unstable).
FT                                /FTId=VAR_002841.
FT   VARIANT     132    132       S -> P (in Questembert; highly unstable;
FT                                causes alpha-thalassemia).
FT                                /FTId=VAR_002843.
FT   VARIANT     134    134       S -> R (in Val de Marne; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002844.
FT   VARIANT     136    136       V -> E (in Pavie).
FT                                /FTId=VAR_002845.
FT   VARIANT     137    137       L -> M (in Chicago).
FT                                /FTId=VAR_002846.
FT   VARIANT     137    137       L -> P (in Bibba; unstable; causes alpha-
FT                                thalassemia).
FT                                /FTId=VAR_002847.
FT   VARIANT     137    137       L -> R (in Toyama).
FT                                /FTId=VAR_035242.
FT   VARIANT     139    139       S -> P (in Attleboro; O(2) affinity up).
FT                                /FTId=VAR_002848.
FT   VARIANT     140    140       K -> E (in Hanamaki; O(2) affinity up).
FT                                /FTId=VAR_002849.
FT   VARIANT     140    140       K -> T (in Tokoname; O(2) affinity up).
FT                                /FTId=VAR_002850.
FT   VARIANT     141    141       Y -> H (in Rouen/Ethiopia; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002851.
FT   VARIANT     142    142       R -> C (in Nunobiki; O(2) affinity up).
FT                                /FTId=VAR_002852.
FT   VARIANT     142    142       R -> H (in Suresnes; O(2) affinity up).
FT                                /FTId=VAR_002854.
FT   VARIANT     142    142       R -> L (in Legnano; O(2) affinity up).
FT                                /FTId=VAR_002853.
FT   VARIANT     142    142       R -> P (in Singapore).
FT                                /FTId=VAR_002855.
FT   CONFLICT     10     10       N -> H (in Ref. 13; BAD97112).
FT   HELIX         5     16
FT   HELIX        17     21
FT   HELIX        22     36
FT   HELIX        38     43
FT   HELIX        54     72
FT   HELIX        74     76
FT   HELIX        77     80
FT   HELIX        82     90
FT   HELIX        97    113
FT   TURN        115    117
FT   HELIX       120    137
FT   TURN        138    140
SQ   SEQUENCE   142 AA;  15258 MW;  15E13666573BBBAE CRC64;
     MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
     KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
     AVHASLDKFL ASVSTVLTSK YR
//
ID   HBA_PANPA               Reviewed;         142 AA.
AC   P69906; P01922;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 47.
DE   RecName: Full=Hemoglobin subunit alpha;
DE   AltName: Full=Alpha-globin;
DE   AltName: Full=Hemoglobin alpha chain;
GN   Name=HBA1;
GN   and
GN   Name=HBA2;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-142.
RX   MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0;
RA   Goodman M., Braunitzer G., Stangl A., Schrank B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA); two alpha chains and two delta chains in
CC       adult hemoglobin A2 (HbA2); two alpha chains and two epsilon
CC       chains in early embryonic hemoglobin Gower-2; two alpha chains and
CC       two gamma chains in fetal hemoglobin F (HbF).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: Gives blood its red color.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; C93303; HACZP.
DR   ProteinModelPortal; P69906; -.
DR   SMR; P69906; 2-142.
DR   IntAct; P69906; 2.
DR   PRIDE; P69906; -.
DR   HOVERGEN; HBG009709; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR012292; Globin_dom.
DR   InterPro; IPR002338; Haemoglobin_a.
DR   InterPro; IPR018331; Haemoglobin_alpha_chain.
DR   InterPro; IPR002339; Haemoglobin_pi.
DR   PANTHER; PTHR11442:SF14; Pi_haem; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
DR   SUPFAM; SSF46458; Globin_like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    142       Hemoglobin subunit alpha.
FT                                /FTId=PRO_0000052717.
FT   METAL        59     59       Iron (heme distal ligand).
FT   METAL        88     88       Iron (heme proximal ligand).
SQ   SEQUENCE   142 AA;  15258 MW;  15E13666573BBBAE CRC64;
     MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
     KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
     AVHASLDKFL ASVSTVLTSK YR
//
ID   HBA_PANTR               Reviewed;         142 AA.
AC   P69907; P01922;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 57.
DE   RecName: Full=Hemoglobin subunit alpha;
DE   AltName: Full=Alpha-globin;
DE   AltName: Full=Hemoglobin alpha chain;
GN   Name=HBA1;
GN   and
GN   Name=HBA2;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=84169526; PubMed=6689503; DOI=10.1093/nar/11.24.8915;
RA   Liebhaber S.A., Begley K.A.;
RT   "Structural and evolutionary analysis of the two chimpanzee alpha-
RT   globin mRNAs.";
RL   Nucleic Acids Res. 11:8915-8929(1983).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-142.
RX   MEDLINE=66071496; PubMed=5855051;
RA   Rifkin D.B., Konigsberg W.;
RT   "The characterization of the tryptic peptides from the hemoglobin of
RT   the chimpanzee (Pan troglodytes).";
RL   Biochim. Biophys. Acta 104:457-461(1965).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-142.
RX   MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0;
RA   Goodman M., Braunitzer G., Stangl A., Schrank B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA); two alpha chains and two delta chains in
CC       adult hemoglobin A2 (HbA2); two alpha chains and two epsilon
CC       chains in early embryonic hemoglobin Gower-2; two alpha chains and
CC       two gamma chains in fetal hemoglobin F (HbF).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: Gives blood its red color.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X00226; CAA25044.1; -; mRNA.
DR   EMBL; X00227; CAA25045.1; -; mRNA.
DR   PIR; I58217; HACZ.
DR   RefSeq; NP_001036091.1; NM_001042626.1.
DR   RefSeq; NP_001036092.1; NM_001042627.1.
DR   UniGene; Ptr.6291; -.
DR   UniGene; Ptr.6292; -.
DR   ProteinModelPortal; P69907; -.
DR   SMR; P69907; 2-142.
DR   PRIDE; P69907; -.
DR   GeneID; 732485; -.
DR   GeneID; 732486; -.
DR   KEGG; ptr:732485; -.
DR   KEGG; ptr:732486; -.
DR   CTD; 3039; -.
DR   CTD; 3040; -.
DR   HOVERGEN; HBG009709; -.
DR   KO; K13822; -.
DR   NextBio; 20902653; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR012292; Globin_dom.
DR   InterPro; IPR002338; Haemoglobin_a.
DR   InterPro; IPR018331; Haemoglobin_alpha_chain.
DR   InterPro; IPR002339; Haemoglobin_pi.
DR   PANTHER; PTHR11442:SF14; Pi_haem; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
DR   SUPFAM; SSF46458; Globin_like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    142       Hemoglobin subunit alpha.
FT                                /FTId=PRO_0000052720.
FT   METAL        59     59       Iron (heme distal ligand).
FT   METAL        88     88       Iron (heme proximal ligand).
SQ   SEQUENCE   142 AA;  15258 MW;  15E13666573BBBAE CRC64;
     MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
     KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP
     AVHASLDKFL ASVSTVLTSK YR
//
ID   HBB_HUMAN               Reviewed;         147 AA.
AC   P68871; A4GX73; B2ZUE0; P02023; Q13852; Q14481; Q14510; Q45KT0;
AC   Q549N7; Q6FI08; Q6R7N2; Q8IZI1; Q9BX96; Q9UCD6; Q9UCP8; Q9UCP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 108.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
DE   Contains:
DE     RecName: Full=LVV-hemorphin-7;
GN   Name=HBB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=77126403; PubMed=1019344;
RA   Marotta C., Forget B., Cohen-Solal M., Weissman S.M.;
RT   "Nucleotide sequence analysis of coding and noncoding regions of human
RT   beta-globin mRNA.";
RL   Prog. Nucleic Acid Res. Mol. Biol. 19:165-175(1976).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=81064667; PubMed=6254664; DOI=10.1016/0092-8674(80)90428-6;
RA   Lawn R.M., Efstratiadis A., O'Connell C., Maniatis T.;
RT   "The nucleotide sequence of the human beta-globin gene.";
RL   Cell 21:647-651(1980).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-7.
RX   PubMed=16175509; DOI=10.1086/491748;
RA   Wood E.T., Stover D.A., Slatkin M., Nachman M.W., Hammer M.F.;
RT   "The beta-globin recombinational hotspot reduces the effects of strong
RT   selection around HbC, a recently arisen mutation providing resistance
RT   to malaria.";
RL   Am. J. Hum. Genet. 77:637-642(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lu L., Hu Z.H., Du C.S., Fu Y.S.;
RT   "DNA sequence of the human beta-globin gene isolated from a healthy
RT   Chinese.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-113.
RA   Cabeda J.M., Correia C., Estevinho A., Cardoso C., Amorim M.L.,
RA   Cleto E., Vale L., Coimbra E., Pinho L., Justica B.;
RT   "Unexpected patterns of globin mutations in thalassemia patients from
RT   north of Portugal.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LOUISVILLE LEU-43.
RC   TISSUE=Blood;
RA   Kutlar F., Harbin J., Brisco J., Kutlar A.;
RT   "Rapid detection of electrophoretically silent, unstable human
RT   hemoglobin 'Louisville', (Beta; Phe 42 Leu/TTT to CTT) by cDNA
RT   sequencing of mRNA.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT DURHAM-N.C. PRO-115.
RC   TISSUE=Blood;
RA   Kutlar F., Abboud M., Leithner C., Holley L., Brisco J., Kutlar A.;
RT   "Electrophoretically silent, very unstable, thalassemic mutation at
RT   codon 114 of beta globin (hemoglobin Durham-N.C.) detected by cDNA
RT   sequencing of mRNA, from a Russian women.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TY GARD GLN-125.
RC   TISSUE=Blood;
RA   Kutlar F., Holley L., Leithner C., Kutlar A.;
RT   "A rare beta chain variant 'Hemoglobin Ty Gard:Pro 124 Gln' found in a
RT   Caucasian female with erythrocytosis.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kutlar A., Vercellotti G.M., Glendenning M., Holley L., Elam D.,
RA   Kutlar F.;
RT   "Heterozygote C->A beta-thalassemia mutation at the intron-2/848
RT   nucleotide of beta globin gene was detected on a Northern European
RT   (Caucasian) individual.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-7 AND SER-140.
RC   TISSUE=Blood;
RA   Kutlar F., Lallinger R.R., Holley L., Glendenning M., Kutlar A.;
RT   "A new hemoglobin, beta chain variant 'Hb S-Wake' confirmed to be on
RT   the same chromosome with hemoglobin S mutation, detected in an
RT   African-American family.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT O-ARAB.
RC   TISSUE=Blood;
RA   Kutlar F., Elam D., Glendenning M., Kutlar A., Dincol G.;
RT   "Coexistence of the hemoglobin O-Arab (Glu 121 Lys) and beta-
RT   thalassemia (intron-2; nucleotide 745 C->G) was detected in a Turkish
RT   patient.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Li W.J.;
RT   "Thalassaemic trait cause by C-T substitution at position -90 in
RT   proximal CACCC box of beta-globin gene in China family.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PHE-50 AND PRO-76.
RC   TISSUE=Lymphocyte;
RA   Fan B., Xie L., Guan X.;
RT   "The differently expressed genes in the lymphocyte of recovered SARS
RT   patients.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RA   Mehta S., Li T., Davis D.H., Nechtman J., Kutlar F.;
RT   "Beta-thalassemia G->C mutation at the nucleotide 5 position of intron
RT   1 of beta globin gene was detected in Asian-Indian female with two
RT   polymorphisms in cis.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hilliard L.M., Patel N., Li T., Zhang H., Kutlar A., Kutlar F.;
RT   "Hb Dothan: a novel beta chain variant due to (-GTG) deletion between
RT   the codons 25/26 of beta globin gene detected in a Caucasian male
RT   baby.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [16]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [17]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [18]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [19]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [20]
RP   PROTEIN SEQUENCE OF 2-147.
RX   PubMed=13872627;
RA   Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G.,
RA   Rudloff V., Wittmann-Liebold B.;
RT   "The constitution of normal adult human haemoglobin.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961).
RN   [21]
RP   PROTEIN SEQUENCE OF 33-42, AND MASS SPECTROMETRY.
RX   PubMed=1575724; DOI=10.1016/0006-291X(92)90699-L;
RA   Glaemsta E.-L., Meyerson B., Silberring J., Terenius L., Nyberg F.;
RT   "Isolation of a hemoglobin-derived opioid peptide from cerebrospinal
RT   fluid of patients with cerebrovascular bleedings.";
RL   Biochem. Biophys. Res. Commun. 184:1060-1066(1992).
RN   [22]
RP   PROTEIN SEQUENCE OF 33-42.
RA   Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S.,
RA   de Camargo A.C.M., Pimenta D.C.;
RL   Submitted (JUN-2007) to UniProtKB.
RN   [23]
RP   PROTEIN SEQUENCE OF 97-121, NUCLEOTIDE SEQUENCE [MRNA] OF 106-113, AND
RP   VARIANT BURKE ARG-108.
RX   MEDLINE=94004581; PubMed=8401300;
RA   Suzuki H., Wada C., Kamata K., Takahashi E., Sato N., Kunitomo T.;
RT   "Globin chain synthesis in hemolytic anemia reticulocytes. A case of
RT   hemoglobin Burke.";
RL   Biochem. Mol. Biol. Int. 30:425-431(1993).
RN   [24]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 122-147.
RX   MEDLINE=85205333; PubMed=2581851; DOI=10.1016/0378-1119(85)90093-9;
RA   Lang K.M., Spritz R.A.;
RT   "Cloning specific complete polyadenylylated 3'-terminal cDNA
RT   segments.";
RL   Gene 33:191-196(1985).
RN   [25]
RP   BISPHOSPHOGLYCERATE BINDING.
RX   PubMed=4555506; DOI=10.1038/237146a0;
RA   Arnone A.;
RT   "X-ray diffraction study of binding of 2,3-diphosphoglycerate to human
RT   deoxyhaemoglobin.";
RL   Nature 237:146-149(1972).
RN   [26]
RP   ACETYLATION AT LYS-145.
RX   PubMed=4531009; DOI=10.1073/pnas.71.12.4693;
RA   Shamsuddin M., Mason R.G., Ritchey J.M., Honig G.R., Klotz I.M.;
RT   "Sites of acetylation of sickle cell hemoglobin by aspirin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 71:4693-4697(1974).
RN   [27]
RP   GLYCATION AT VAL-2.
RX   MEDLINE=78138698; PubMed=635569; DOI=10.1126/science.635569;
RA   Bunn H.F., Gabbay K.H., Gallop P.M.;
RT   "The glycosylation of hemoglobin: relevance to diabetes mellitus.";
RL   Science 200:21-27(1978).
RN   [28]
RP   GLYCATION AT LYS-9; LYS-18; LYS-67; LYS-121 AND LYS-145, AND LACK OF
RP   GLYCATION AT LYS-60; LYS-83 AND LYS-96.
RX   PubMed=7358733;
RA   Shapiro R., McManus M.J., Zalut C., Bunn H.F.;
RT   "Sites of nonenzymatic glycosylation of human hemoglobin A.";
RL   J. Biol. Chem. 255:3120-3127(1980).
RN   [29]
RP   INTERACTION WITH HAPTOGLOBIN.
RX   MEDLINE=86242088; PubMed=3718478;
RA   Yoshioka N., Atassi M.Z.;
RT   "Haemoglobin binding with haptoglobin. Localization of the
RT   haptoglobin-binding sites on the beta-chain of human haemoglobin by
RT   synthetic overlapping peptides encompassing the entire chain.";
RL   Biochem. J. 234:453-456(1986).
RN   [30]
RP   OXIDATION AT LEU-142.
RX   PubMed=1520632; DOI=10.1111/j.1365-2141.1992.tb08179.x;
RA   Brennan S.O., Shaw J., Allen J., George P.M.;
RT   "Beta 141 Leu is not deleted in the unstable haemoglobin Atlanta-
RT   Coventry but is replaced by a novel amino acid of mass 129 daltons.";
RL   Br. J. Haematol. 81:99-103(1992).
RN   [31]
RP   S-NITROSYLATION AT CYS-94.
RX   PubMed=8637569; DOI=10.1038/380221a0;
RA   Jia L., Bonaventura C., Bonaventura J., Stamler J.S.;
RT   "S-nitrosohaemoglobin: a dynamic activity of blood involved in
RT   vascular control.";
RL   Nature 380:221-226(1996).
RN   [32]
RP   S-NITROSYLATION AT CYS-94.
RX   MEDLINE=99060083; PubMed=9843411; DOI=10.1021/bi9816711;
RA   Chan N.L., Rogers P.H., Arnone A.;
RT   "Crystal structure of the S-nitroso form of liganded human
RT   hemoglobin.";
RL   Biochemistry 37:16459-16464(1998).
RN   [33]
RP   NITRIC OXIDE-BINDING.
RX   MEDLINE=20056222; PubMed=10588683; DOI=10.1073/pnas.96.25.14206;
RA   Durner J., Gow A.J., Stamler J.S., Glazebrook J.;
RT   "Ancient origins of nitric oxide signaling in biological systems.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14206-14207(1999).
RN   [34]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [35]
RP   SYNTHESIS OF 33-42, AND FUNCTION.
RX   PubMed=16904236; DOI=10.1016/j.peptides.2006.06.009;
RA   Ianzer D., Konno K., Xavier C.H., Stoecklin R., Santos R.A.S.,
RA   de Camargo A.C.M., Pimenta D.C.;
RT   "Hemorphin and hemorphin-like peptides isolated from dog pancreas and
RT   sheep brain are able to potentiate bradykinin activity in vivo.";
RL   Peptides 27:2957-2966(2006).
RN   [36]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Lung carcinoma;
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [37]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [38]
RP   ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS.
RX   PubMed=4123689; DOI=10.1073/pnas.70.3.718;
RA   Finch J.T., Perutz M.F., Bertles J.F., Doebler J.;
RT   "Structure of sickled erythrocytes and of sickle-cell hemoglobin
RT   fibers.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:718-722(1973).
RN   [39]
RP   X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF MUTANT VAL-7.
RX   PubMed=1195378; DOI=10.1016/S0022-2836(75)80108-2;
RA   Wishner B.C., Ward K.B., Lattman E.E., Love W.E.;
RT   "Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution.";
RL   J. Mol. Biol. 98:179-194(1975).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RX   MEDLINE=76027820; PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4;
RA   Fermi G.;
RT   "Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2.5-
RT   A resolution: refinement of the atomic model.";
RL   J. Mol. Biol. 97:237-256(1975).
RN   [41]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN.
RX   PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3;
RA   Baldwin J.M.;
RT   "The structure of human carbonmonoxy haemoglobin at 2.7-A
RT   resolution.";
RL   J. Mol. Biol. 136:103-128(1980).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN.
RX   PubMed=6726807; DOI=10.1016/0022-2836(84)90472-8;
RA   Fermi G., Perutz M.F., Shaanan B., Fourme R.;
RT   "The crystal structure of human deoxyhaemoglobin at 1.74 A
RT   resolution.";
RL   J. Mol. Biol. 175:159-174(1984).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38.
RX   MEDLINE=92232710; PubMed=1567857; DOI=10.1021/bi00131a030;
RA   Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A.;
RT   "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta
RT   Trp-->Arg: a mutation that creates an intersubunit chloride-binding
RT   site.";
RL   Biochemistry 31:4111-4121(1992).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75.
RX   PubMed=1507231; DOI=10.1016/0022-2836(92)90638-Z;
RA   Fermi G., Perutz M.F., Williamson D., Stein P., Shih D.T.;
RT   "Structure-function relationships in the low-affinity mutant
RT   haemoglobin Aalborg (Gly74 (E18)beta-->Arg).";
RL   J. Mol. Biol. 226:883-888(1992).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND BISPHOSPHOGLYCERATE
RP   BINDING.
RX   PubMed=8377203; DOI=10.1006/jmbi.1993.1505;
RA   Richard V., Dodson G.G., Mauguen Y.;
RT   "Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low-salt
RT   structure at 2.5 A resolution.";
RL   J. Mol. Biol. 233:270-274(1993).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=8642597; DOI=10.1006/jmbi.1996.0124;
RA   Paoli M., Liddington R., Tame J., Wilkinson A., Dodson G.;
RT   "Crystal structure of T state haemoglobin with oxygen bound at all
RT   four haems.";
RL   J. Mol. Biol. 256:775-792(1996).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38;
RP   GLY-38 AND TYR-38.
RX   PubMed=9521756; DOI=10.1021/bi9708702;
RA   Kavanaugh J.S., Weydert J.A., Rogers P.H., Arnone A.;
RT   "High-resolution crystal structures of human hemoglobin with mutations
RT   at tryptophan 37beta: structural basis for a high-affinity T-state.";
RL   Biochemistry 37:4358-4373(1998).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-7.
RX   PubMed=9830011; DOI=10.1074/jbc.273.49.32690;
RA   Harrington D.J., Adachi K., Royer W.E. Jr.;
RT   "Crystal structure of deoxy-human hemoglobin beta6 Glu-->Trp.
RT   Implications for the structure and formation of the sickle cell
RT   fiber.";
RL   J. Biol. Chem. 273:32690-32696(1998).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT LYS-7.
RX   PubMed=12454462; DOI=10.1107/S0907444902016426;
RA   Dewan J.C., Feeling-Taylor A., Puius Y.A., Patskovska L.,
RA   Patskovsky Y., Nagel R.L., Almo S.C., Hirsch R.E.;
RT   "Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A
RT   resolution.";
RL   Acta Crystallogr. D 58:2038-2042(2002).
RN   [50]
RP   VARIANT ALABAMA LYS-40.
RX   MEDLINE=75109326; PubMed=1115799;
RA   Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G.,
RA   Atkins R.;
RT   "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys)
RT   and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg).";
RL   Biochim. Biophys. Acta 379:28-32(1975).
RN   [51]
RP   INVOLVEMENT IN HEIBAN, AND VARIANT ST LOUIS GLN-29.
RX   PubMed=186485; DOI=10.1172/JCI108561;
RA   Thillet J., Cohen-Solal M., Seligmann M., Rosa J.;
RT   "Functional and physicochemical studies of hemoglobin St. Louis beta
RT   28 (B10) Leu replaced by Gln: a variant with ferric beta heme iron.";
RL   J. Clin. Invest. 58:1098-1106(1976).
RN   [52]
RP   INVOLVEMENT IN B-THALIB.
RX   PubMed=1971109; DOI=10.1073/pnas.87.10.3924;
RA   Thein S.L., Hesketh C., Taylor P., Temperley I.J., Hutchinson R.M.,
RA   Old J.M., Wood W.G., Clegg J.B., Weatherall D.J.;
RT   "Molecular basis for dominantly inherited inclusion body beta-
RT   thalassemia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3924-3928(1990).
RN   [53]
RP   VARIANT ALESHA MET-68.
RX   MEDLINE=93322192; PubMed=8330974;
RA   Molchanova T.P., Postnikov Y.V., Pobedimskaya D.D., Smetanina N.S.,
RA   Moschan A.A., Kazanetz E.G., Tokarev Y.N., Huisman T.H.J.;
RT   "Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable
RT   hemoglobin variant identified through sequencing of amplified DNA.";
RL   Hemoglobin 17:217-225(1993).
RN   [54]
RP   VARIANT J-ALTGELDS GARDENS ASP-93.
RX   MEDLINE=79067354; PubMed=721609;
RA   Adams J.G. III, Przywara K.P., Heller P., Shamsuddin M.;
RT   "Hemoglobin J Altgeld Gardens. A hemoglobin variant with a
RT   substitution of the proximal histidine of the beta-chain.";
RL   Hemoglobin 2:403-415(1978).
RN   [55]
RP   VARIANT ANKARA ASP-11.
RX   MEDLINE=74297498; PubMed=4850241; DOI=10.1016/0014-5793(74)80766-0;
RA   Arcasoy A., Casey R., Lehmann H., Cavdar A.O., Berki A.;
RT   "A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp).";
RL   FEBS Lett. 42:121-123(1974).
RN   [56]
RP   VARIANTS J-ANTAKYA MET-66 AND COMPLUTENSE GLU-128.
RX   MEDLINE=86216227; PubMed=3707969; DOI=10.1016/0167-4838(86)90178-0;
RA   Huisman T.H.J., Wilson J.B., Kutlar A., Yang K.-G., Chen S.-S.,
RA   Webber B.B., Altay C., Martinez A.V.;
RT   "Hb J-Antakya or alpha 2 beta (2)65(E9)Lys-->Met in a Turkish family
RT   and Hb complutense or alpha 2 beta (2)127(H5)Gln-->Glu in a Spanish
RT   family; correction of a previously published identification.";
RL   Biochim. Biophys. Acta 871:229-231(1986).
RN   [57]
RP   VARIANT J-AUCKLAND ASP-26.
RX   MEDLINE=88006903; PubMed=3654265;
RA   Williamson D., Wells R.M.G., Anderson R., Matthews J.;
RT   "A new unstable and low oxygen affinity hemoglobin variant: Hb J-
RT   Auckland [beta 25(B7)Gly-->Asp].";
RL   Hemoglobin 11:221-230(1987).
RN   [58]
RP   VARIANT AURORA TYR-140.
RX   MEDLINE=96352910; PubMed=8718692;
RA   Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J.S.;
RT   "Identification of a new high oxygen affinity hemoglobin variant: Hb
RT   Aurora [beta 139(H17) Asn-->Tyr].";
RL   Hemoglobin 19:335-341(1995).
RN   [59]
RP   VARIANT BREST LYS-128.
RX   MEDLINE=88256755; PubMed=3384710;
RA   Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J.,
RA   Briere J., Galacteros F.;
RT   "Hemoglobin Brest [beta 127 (H5)Gln-->Lys] a new unstable human
RT   hemoglobin variant located at the alpha 1 beta 1 interface with
RT   specific electrophoretic behavior.";
RL   Hemoglobin 12:179-188(1988).
RN   [60]
RP   VARIANT BRISBANE HIS-69.
RX   MEDLINE=81239159; PubMed=6166590;
RA   Brennan S.O., Wells R.M., Smith H., Carrell R.W.;
RT   "Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen
RT   affinity variant.";
RL   Hemoglobin 5:325-335(1981).
RN   [61]
RP   VARIANT BUNBURY ASN-95.
RX   MEDLINE=84031649; PubMed=6629823;
RA   Como P.F., Kennett D., Wilkinson T., Kronenberg H.;
RT   "A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury:
RT   alpha 2 beta 2 [94 (FG1) Asp replaced by Asn].";
RL   Hemoglobin 7:413-421(1983).
RN   [62]
RP   VARIANT J-CAIRO GLN-66.
RX   MEDLINE=76114933; PubMed=1247583;
RA   Garel M.-C., Hassan W., Coquelet M.T., Goossens M., Rosa J., Arous N.;
RT   "Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin
RT   variant discovered in an Egyptian family.";
RL   Biochim. Biophys. Acta 420:97-104(1976).
RN   [63]
RP   VARIANT CAMPERDOWN SER-105.
RX   MEDLINE=75184109; PubMed=1138922;
RA   Wilkinson T., Chua C.G., Carrell R.W., Robin H., Exner T., Lee K.M.,
RA   Kronenberg H.;
RT   "A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6)
RT   arginine->serine).";
RL   Biochim. Biophys. Acta 393:195-200(1975).
RN   [64]
RP   VARIANT CARIBBEAN ARG-92.
RX   MEDLINE=77048866; PubMed=992050; DOI=10.1016/0014-5793(76)80662-X;
RA   Ahern E., Ahern V., Hilton T., Serjeant G.R., Serjeant B.E.,
RA   Seakins M., Lang A., Middleton A., Lehmann H.;
RT   "Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly
RT   haemoglobin with a low oxygen affinity.";
RL   FEBS Lett. 69:99-102(1976).
RN   [65]
RP   VARIANT CITY OF HOPE SER-70.
RX   MEDLINE=85006311; PubMed=6434492;
RA   Rahbar S., Asmerom Y., Blume K.G.;
RT   "A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope
RT   beta 69 (E13) Gly-->Ser.";
RL   Hemoglobin 8:333-342(1984).
RN   [66]
RP   VARIANT COIMBRA GLU-100.
RX   MEDLINE=92267852; PubMed=1814856;
RA   Tamagnini G.P., Ribeiro M.L., Valente V., Ramachandran M.,
RA   Wilson J.B., Baysal E., Gu L.H., Huisman T.H.J.;
RT   "Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered
RT   high oxygen affinity variant.";
RL   Hemoglobin 15:487-496(1991).
RN   [67]
RP   VARIANT COSTA RICA ARG-78.
RX   MEDLINE=96235282; PubMed=8641705; DOI=10.1007/s004390050145;
RA   Romero W.E.R., Castillo M., Chaves M.A., Saenz G.F., Gu L.-H.,
RA   Wilson J.B., Baysal E., Smetanina N.S., Leonova J.Y., Huisman T.H.J.;
RT   "Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first example
RT   of a somatic cell mutation in a globin gene.";
RL   Hum. Genet. 97:829-833(1996).
RN   [68]
RP   VARIANT DEBROUSSE PRO-97.
RX   MEDLINE=96180033; PubMed=8602627;
RX   DOI=10.1002/(SICI)1096-8652(199604)51:4<276::AID-AJH5>3.0.CO;2-T;
RA   Lacan P., Kister J., Francina A., Souillet G., Galacteros F.,
RA   Delaunay J., Wajcman H.;
RT   "Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable
RT   hemoglobin with twofold increased oxygen affinity.";
RL   Am. J. Hematol. 51:276-281(1996).
RN   [69]
RP   VARIANT DHONBURI GLY-127.
RX   MEDLINE=90379198; PubMed=2399911; DOI=10.1002/ajh.2830350206;
RA   Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J.,
RA   Lacombe C., Winichagoon P., Blouquit Y., Riou J., Wasi P.,
RA   Galacteros F.;
RT   "Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val-->Gly: a new unstable
RT   beta variant producing a beta-thalassemia intermedia phenotype in
RT   association with beta zero-thalassemia.";
RL   Am. J. Hematol. 35:96-99(1990).
RN   [70]
RP   VARIANTS NEWCASTLE PRO-93 AND CAMPERDOWN SER-105, AND DESCRIPTION OF
RP   VARIANT DUINO.
RX   MEDLINE=92380658; PubMed=1511986; DOI=10.1007/BF00221961;
RA   Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M.,
RA   Melevendi C., Rasore A., Galacteros F.;
RT   "Two new human hemoglobin variants caused by unusual mutational
RT   events: Hb Zaire contains a five residue repetition within the alpha-
RT   chain and Hb Duino has two residues substituted in the beta-chain.";
RL   Hum. Genet. 89:676-680(1992).
RN   [71]
RP   VARIANT DURHAM-N.C. PRO-115.
RX   MEDLINE=93244842; PubMed=1301199; DOI=10.1002/humu.1380010207;
RA   Murru S., Poddie D., Sciarratta G.V., Agosti S., Baffico M.,
RA   Melevendi C., Pirastu M., Cao A.;
RT   "A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro),
RT   causing a severe beta-thalassemia intermedia phenotype.";
RL   Hum. Mutat. 1:124-128(1992).
RN   [72]
RP   VARIANT DURHAM-N.C. PRO-115.
RX   MEDLINE=94154273; PubMed=8111050;
RA   de Castro C.M., Devlin B., Fleenor D.E., Lee M.E., Kaufman R.E.;
RT   "A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro],
RT   produces a dominant thalassemia-like phenotype.";
RL   Blood 83:1109-1116(1994).
RN   [73]
RP   VARIANT J-EUROPA ASP-63.
RX   MEDLINE=96407264; PubMed=8811317;
RA   Kiger L., Kister J., Groff P., Kalmes G., Prome D., Galacteros F.,
RA   Wajcman H.;
RT   "Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties
RT   in a new variant involving a residue located distal to the heme.";
RL   Hemoglobin 20:135-140(1996).
RN   [74]
RP   VARIANT GEELONG ASP-140.
RX   MEDLINE=92010939; PubMed=1917539;
RA   Como P.F., Hocking D.R., Swinton G.W., Trent R.J., Holland R.A.B.,
RA   Tibben E.A., Wilkinson T., Kronenberg H.;
RT   "Hb Geelong [beta 139(H17)Asn-->Asp].";
RL   Hemoglobin 15:85-95(1991).
RN   [75]
RP   VARIANT GRANGE-BLANCHE VAL-28.
RX   MEDLINE=88030044; PubMed=3666141; DOI=10.1016/0014-5793(87)80509-4;
RA   Baklouti F., Giraud Y., Francina A., Richard G., Perier C.,
RA   Geyssant A., Jaubert J., Brizard C., Delaunay J.;
RT   "Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant with
RT   normal expression and increased affinity for oxygen.";
RL   FEBS Lett. 223:59-62(1987).
RN   [76]
RP   VARIANT GRAZ LEU-3.
RX   MEDLINE=93138927; PubMed=1487420;
RA   Liu J.S., Molchanova T.P., Gu L.H., Wilson J.B., Hopmeier P.,
RA   Schnedl W., Balaun E., Krejs G.J., Huisman T.H.J.;
RT   "Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant
RT   observed in four families from southern Austria.";
RL   Hemoglobin 16:493-501(1992).
RN   [77]
RP   VARIANT HELSINKI MET-83.
RX   MEDLINE=77062201; PubMed=826083;
RA   Ikkala E., Koskela J., Pikkarainen P., Rahiala E.-L., El-Hazmi M.A.F.,
RA   Nagai K., Lang A., Lehmann H.;
RT   "Hb Helsinki: a variant with a high oxygen affinity and a substitution
RT   at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met).";
RL   Acta Haematol. 56:257-275(1976).
RN   [78]
RP   VARIANT HIMEJI ASP-141.
RX   MEDLINE=86167527; PubMed=3754244;
RA   Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M.,
RA   Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K.;
RT   "Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable hemoglobin
RT   with increased beta N-terminal glycation.";
RL   Hemoglobin 10:109-126(1986).
RN   [79]
RP   VARIANT HINSDALE LYS-140.
RX   MEDLINE=90093866; PubMed=2513289;
RA   Moo-Penn W.F., Johnson M.H., Jue D.L., Lonser R.;
RT   "Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central
RT   cavity showing reduced affinity for oxygen and 2,3-
RT   diphosphoglycerate.";
RL   Hemoglobin 13:455-464(1989).
RN   [80]
RP   VARIANT HINWIL ASN-39.
RX   MEDLINE=96351651; PubMed=8745430;
RA   Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M.C.,
RA   Cao A., Breitenstein U., Fehr J., Tuchschmid P.;
RT   "HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected
RT   in a Swiss family.";
RL   Hemoglobin 20:31-40(1996).
RN   [81]
RP   VARIANT HOWICK GLY-38.
RX   MEDLINE=94193408; PubMed=8144352;
RA   Owen M.C., Ockelford P.A., Wells R.M.G.;
RT   "Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant
RT   of the alpha 1 beta 2 contact.";
RL   Hemoglobin 17:513-521(1993).
RN   [82]
RP   VARIANT INDIANAPOLIS ARG-113.
RX   MEDLINE=79151109; PubMed=429365;
RA   Adams J.G. III, Steinberg M.H., Boxer L.A., Baehner R.L., Forget B.G.,
RA   Tsistrakis G.A.;
RT   "The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An
RT   unstable variant detectable only by isotopic labeling.";
RL   J. Biol. Chem. 254:3479-3482(1979).
RN   [83]
RP   VARIANT ISEHARA ASN-93.
RX   MEDLINE=92155974; PubMed=1787097;
RA   Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M.;
RT   "Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable
RT   variant with a proximal histidine substitution at the heme contact.";
RL   Hemoglobin 15:279-290(1991).
RN   [84]
RP   VARIANT ISTAMBUL GLN-93.
RX   MEDLINE=73054825; PubMed=4639022; DOI=10.1172/JCI107050;
RA   Aksoy M., Erdem S., Efremov G.D., Wilson J.B., Huisman T.H.J.,
RA   Schroeder W.A., Shelton J.R., Shelton J.B., Ulitin O.N., Muftuoglu A.;
RT   "Hemoglobin Istanbul: substitution of glutamine for histidine in a
RT   proximal histidine (F8(92)).";
RL   J. Clin. Invest. 51:2380-2387(1972).
RN   [85]
RP   VARIANT JACKSONVILLE ASP-55.
RX   MEDLINE=91331861; PubMed=2101840;
RA   Gaudry C.L. Jr., Pitel P.A., Jue D.L., Hine T.K., Johnson M.H.,
RA   Moo-Penn W.F.;
RT   "Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable
RT   variant found in a patient with hemolytic anemia.";
RL   Hemoglobin 14:653-659(1990).
RN   [86]
RP   VARIANT JIANGHUA ILE-121.
RX   MEDLINE=84007581; PubMed=6618888;
RA   Lu Y.Q., Fan J.L., Liu J.F., Hu H.L., Peng X.H., Huang C.-H.,
RA   Huang P.Y., Chen S.S., Jai P.C., Yang K.G.;
RT   "Hemoglobin Jianghua [beta 120(GH3) Lys leads to Ile]: a new fast-
RT   moving variant found in China.";
RL   Hemoglobin 7:321-326(1983).
RN   [87]
RP   VARIANT KARLSKOGA HIS-22.
RX   MEDLINE=93322190; PubMed=8330972;
RA   Landin B.;
RT   "Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving
RT   variant found in Sweden.";
RL   Hemoglobin 17:201-208(1993).
RN   [88]
RP   VARIANT KNOSSOS SER-28.
RX   MEDLINE=83079719; PubMed=7173395; DOI=10.1016/0014-5793(82)81052-1;
RA   Arous N., Galacteros F., Fessas P., Loukopoulos D., Blouquit Y.,
RA   Komis G., Sellaye M., Boussiou M., Rosa J.;
RT   "Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to
RT   Ser. A new abnormal hemoglobin present as a silent beta-thalassemia.";
RL   FEBS Lett. 147:247-250(1982).
RN   [89]
RP   VARIANT KODAIRA GLN-147.
RX   MEDLINE=92340295; PubMed=1634367;
RA   Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R.,
RA   Matsunaga T.;
RT   "Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with an
RT   amino acid substitution at the C-terminus.";
RL   Hemoglobin 16:85-91(1992).
RN   [90]
RP   VARIANT KOFU ILE-85.
RX   MEDLINE=86303641; PubMed=3744871;
RA   Harano T., Harano K., Ueda S., Imai N., Kitazumi T.;
RT   "A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu
RT   or alpha 2 beta 2 84 (EF8) Thr-->Ile.";
RL   Hemoglobin 10:417-420(1986).
RN   [91]
RP   VARIANT HRADEC KRALOVE ASP-116.
RX   MEDLINE=94042221; PubMed=7693620;
RA   Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T.P.,
RA   Huisman T.H.J.;
RT   "Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a
RT   severely unstable hemoglobin variant resulting in a dominant beta-
RT   thalassemia trait in a Czech family.";
RL   Hemoglobin 17:319-328(1993).
RN   [92]
RP   VARIANT LA DESIRADE VAL-130.
RX   MEDLINE=87165149; PubMed=3557994;
RA   Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N.,
RA   Galacteros F., Feingold J., Rosa J.;
RT   "Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new
RT   unstable hemoglobin.";
RL   Hemoglobin 10:593-605(1986).
RN   [93]
RP   VARIANT LA ROCHE-SUR-YON HIS-82.
RX   MEDLINE=92172947; PubMed=1540659; DOI=10.1016/0925-4439(92)90052-O;
RA   Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J.C.,
RA   Cottenceau D., Galacteros F.;
RT   "Structure of the EF corner favors deamidation of asparaginyl residues
RT   in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5)
RT   Leu-->His].";
RL   Biochim. Biophys. Acta 1138:127-132(1992).
RN   [94]
RP   VARIANT LAS PALMAS PHE-50.
RX   MEDLINE=88256753; PubMed=3384708;
RA   Malcorra-Azpiazu J.J., Balda-Aguirre M.I., Diaz-Chico J.C., Hu H.,
RA   Wilson J.B., Webber B.B., Kutlar F., Kutlar A., Huisman T.H.J.;
RT   "Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly unstable
RT   hemoglobin variant.";
RL   Hemoglobin 12:163-170(1988).
RN   [95]
RP   VARIANT LINKOPING THR-37.
RX   MEDLINE=88083482; PubMed=3691763;
RA   Berlin G., Wranne B., Jeppsson J.-O.;
RT   "Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity
RT   hemoglobin variant found in two families of Finnish origin.";
RL   Eur. J. Haematol. 39:452-456(1987).
RN   [96]
RP   VARIANT MAPUTO TYR-48.
RX   MEDLINE=84031650; PubMed=6629824;
RA   Marinucci M., Boissel J.P., Massa A., Wajcman H., Tentori L.,
RA   Labie D.;
RT   "Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6)
RT   Asp replaced by Tyr) in combination with hemoglobin S, identified by
RT   high performance liquid chromatography (HPLC).";
RL   Hemoglobin 7:423-433(1983).
RN   [97]
RP   VARIANT MATERA LYS-56.
RX   MEDLINE=90346586; PubMed=2384314;
RA   Sciarratta G.V., Ivaldi G.;
RT   "Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant
RT   in an Italian family.";
RL   Hemoglobin 14:79-85(1990).
RN   [98]
RP   VARIANT MIYASHIRO GLY-24.
RX   MEDLINE=82166873; PubMed=7338468;
RA   Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H.,
RA   Shinohara T., Hori T., Takayama J.;
RT   "Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an
RT   electrophoretically silent variant discovered by the isopropanol
RT   test.";
RL   Hemoglobin 5:653-666(1981).
RN   [99]
RP   VARIANT MIZUHO PRO-69.
RX   MEDLINE=77248961; PubMed=893142;
RA   Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T.;
RT   "Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new
RT   unstable variant associated with severe hemolytic anemia.";
RL   Hemoglobin 1:467-477(1977).
RN   [100]
RP   VARIANT MUSCAT VAL-33.
RX   MEDLINE=92387956; PubMed=1517102;
RA   Ramachandran M., Gu L.H., Wilson J.B., Kitundu M.N., Adekile A.D.,
RA   Liu J.C., McKie K.M., Huisman T.H.J.;
RT   "A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val] observed
RT   in association with HB S in an Arabian family.";
RL   Hemoglobin 16:259-266(1992).
RN   [101]
RP   VARIANT N-TIMONE GLU-9.
RX   MEDLINE=90236754; PubMed=2634671;
RA   Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C.,
RA   Blouquit Y., Craescu C.T., Galacteros F.;
RT   "Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving
RT   variant with normal stability and oxygen affinity.";
RL   Hemoglobin 13:743-747(1989).
RN   [102]
RP   VARIANT NAGOYA PRO-98.
RX   MEDLINE=85206960; PubMed=3838976;
RA   Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C.,
RA   Shibata K., Shimokata H., Kuzuya F., Miwa S.;
RT   "A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97
RT   (FG4) His-->Pro.";
RL   Hemoglobin 9:11-24(1985).
RN   [103]
RP   VARIANT D-NEATH ALA-122.
RX   MEDLINE=93322197; PubMed=8330979;
RA   Welch S.G., Bateman C.;
RT   "Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D
RT   family.";
RL   Hemoglobin 17:255-259(1993).
RN   [104]
RP   VARIANT NORTH CHICAGO SER-37.
RX   MEDLINE=86139289; PubMed=3937824;
RA   Rahbar S., Louis J., Lee T., Asmerom Y.;
RT   "Hemoglobin North Chicago (beta 36 [C2] proline-->serine): a new high
RT   affinity hemoglobin.";
RL   Hemoglobin 9:559-576(1985).
RN   [105]
RP   VARIANT NORTH SHORE-CARACAS GLU-135.
RX   MEDLINE=77246803; PubMed=891976; DOI=10.1016/0014-5793(77)80453-5;
RA   Arends T., Lehmann H., Plowman D., Stathopoulou R.;
RT   "Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by
RT   glutamic acid.";
RL   FEBS Lett. 80:261-265(1977).
RN   [106]
RP   VARIANT OLOMOUC ASP-87.
RX   MEDLINE=87307470; PubMed=3623975;
RA   Indrak K., Wiedermann B.F., Batek F., Wilson J.B., Webber B.B.,
RA   Kutlar A., Huisman T.H.J.;
RT   "Hb Olomouc or alpha 2 beta 2(86)(F2)Ala-->Asp, a new high oxygen
RT   affinity variant.";
RL   Hemoglobin 11:151-155(1987).
RN   [107]
RP   VARIANT PALMERSTON NORTH PHE-24.
RX   MEDLINE=83135041; PubMed=7161106;
RA   Brennan S.O., Williamson D., Whisson M.E., Carrell R.W.;
RT   "Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new
RT   variant identified in a patient with polycythemia.";
RL   Hemoglobin 6:569-575(1982).
RN   [108]
RP   VARIANT PIERRE-BENITE ASP-91.
RX   MEDLINE=88256754; PubMed=3384709;
RA   Baklouti F., Giraud Y., Francina A., Richard G., Favre-Gilly J.,
RA   Delaunay J.;
RT   "Hemoglobin Pierre-Benite [beta 90(F6)Glu-->Asp], a new high affinity
RT   variant found in a French family.";
RL   Hemoglobin 12:171-177(1988).
RN   [109]
RP   VARIANT PRESBYTERIAN LYS-109.
RX   MEDLINE=78215075; PubMed=668922; DOI=10.1016/0014-5793(78)80720-0;
RA   Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., Johnson M.H.;
RT   "Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A
RT   hemoglobin variant with low oxygen affinity.";
RL   FEBS Lett. 92:53-56(1978).
RN   [110]
RP   VARIANT PUTTELANGE VAL-141.
RX   MEDLINE=96101899; PubMed=8522332; DOI=10.1007/BF00210304;
RA   Wajcman H., Girodon E., Prome D., North M.L., Plassa F., Duwig I.,
RA   Kister J., Bergerat J.P., Oberling F., Lampert E., Lonsdorfer J.,
RA   Goossens M., Galacteros F.;
RT   "Germline mosaicism for an alanine to valine substitution at residue
RT   beta 140 in hemoglobin Puttelange, a new variant with high oxygen
RT   affinity.";
RL   Hum. Genet. 96:711-716(1995).
RN   [111]
RP   VARIANT QUIN-HAI ARG-79.
RX   MEDLINE=84031648; PubMed=6629822;
RA   Jen P.C., Chen L.C., Chen P.F., Wong Y., Chen L.F., Guo Y.Y.,
RA   Chang F.Q., Chow Y.C., Chiu Y.;
RT   "Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new
RT   abnormal hemoglobin found in Guangdong, China.";
RL   Hemoglobin 7:407-412(1983).
RN   [112]
RP   VARIANT RAMBAM ASP-70.
RX   MEDLINE=98432396; PubMed=9761252;
RA   Bisse E., Zorn N., Eigel A., Lizama M., Huamam-Guillen P., Marz W.,
RA   van Dorsselaer A., Wieland H.;
RT   "Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment
RT   of diabetic control: characterization by electrospray mass
RT   spectrometry and HPLC.";
RL   Clin. Chem. 44:2172-2177(1998).
RN   [113]
RP   VARIANT RANDWICK GLY-16.
RX   MEDLINE=88256752; PubMed=3384707;
RA   Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Ip F.,
RA   Kwan Y.L., Holland R.A.B.;
RT   "Hemoglobin Randwick or beta 15 (A12)Trp-->Gly: a new unstable beta-
RT   chain hemoglobin variant.";
RL   Hemoglobin 12:149-161(1988).
RN   [114]
RP   VARIANT RIO GRANDE THR-9.
RX   MEDLINE=83185445; PubMed=6857757;
RA   Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.,
RA   Therrell B.L. Jr.;
RT   "Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant
RT   found in a Mexican-American family.";
RL   Hemoglobin 7:91-95(1983).
RN   [115]
RP   VARIANT RUSH GLN-102.
RX   MEDLINE=74080282; PubMed=4129558;
RA   Adams J.G. III, Winter W.P., Tausk K., Heller P.;
RT   "Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin
RT   causing mild hemolytic anemia.";
RL   Blood 43:261-269(1974).
RN   [116]
RP   VARIANT SAITAMA PRO-118.
RX   MEDLINE=83185440; PubMed=6687721;
RA   Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y.,
RA   Miyaji T.;
RT   "Hemoglobin Saitama or beta 117 (G19) His leads to Pro, a new variant
RT   causing hemolytic disease.";
RL   Hemoglobin 7:47-56(1983).
RN   [117]
RP   VARIANT M-SASKATOON TYR-64.
RX   PubMed=13897827; DOI=10.1073/pnas.47.11.1758;
RA   Gerald P.S., Efron M.L.;
RT   "Chemical studies of several varieties of Hb M.";
RL   Proc. Natl. Acad. Sci. U.S.A. 47:1758-1767(1961).
RN   [118]
RP   VARIANT SHELBY/LESLIE/DEACONESS LYS-132.
RX   MEDLINE=85130256; PubMed=6526653;
RA   Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.;
RT   "Hemoglobin Shelby [beta 131(H9) Gln-->Lys] a correction to the
RT   structure of hemoglobin Deaconess and hemoglobin Leslie.";
RL   Hemoglobin 8:583-593(1984).
RN   [119]
RP   VARIANT J-SICILIA ASN-66.
RX   MEDLINE=74302182; PubMed=4852224; DOI=10.1016/0014-5793(74)80050-5;
RA   Ricco G., Pich P.G., Mazza U., Rossi G., Ajmar P., Arese P., Gallo E.;
RT   "Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia.";
RL   FEBS Lett. 39:200-204(1974).
RN   [120]
RP   VARIANT STANMORE ALA-112.
RX   MEDLINE=92010936; PubMed=1917537;
RA   Como P.F., Wylie B.R., Trent R.J., Bruce D., Volpato F., Wilkinson T.,
RA   Kronenberg H., Holland R.A.B., Tibben E.A.;
RT   "A new unstable and low oxygen affinity hemoglobin variant: Hb
RT   Stanmore [beta 111(G13)Val-->Ala].";
RL   Hemoglobin 15:53-65(1991).
RN   [121]
RP   VARIANT ST MANDE TYR-103.
RX   MEDLINE=81212764; PubMed=7238856; DOI=10.1016/0014-5793(81)81046-0;
RA   Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F.,
RA   Chevrier M., Bordahandy C., Rosa J.;
RT   "Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low
RT   oxygen affinity variant.";
RL   FEBS Lett. 126:114-116(1981).
RN   [122]
RP   VARIANT WINDSOR ASP-12.
RX   MEDLINE=90093865; PubMed=2599880;
RA   Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Holland R.A.B.,
RA   Tibben E.A.;
RT   "Hemoglobin Windsor or beta 11 (A8)Val-->Asp: a new unstable beta-
RT   chain hemoglobin variant producing a hemolytic anemia.";
RL   Hemoglobin 13:437-453(1989).
RN   [123]
RP   VARIANT YAHATA TYR-113.
RX   MEDLINE=92010926; PubMed=1917530;
RA   Harano T., Harano K., Kushida Y., Ueda S.;
RT   "A new abnormal variant, Hb Yahata or beta 112(G14)Cys-->Tyr, found in
RT   a Japanese: structural confirmation by DNA sequencing of the beta-
RT   globin gene.";
RL   Hemoglobin 15:109-113(1991).
RN   [124]
RP   VARIANT YOKOHAMA PRO-32.
RX   MEDLINE=82166874; PubMed=7338469;
RA   Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S.,
RA   Matsumoto N.;
RT   "A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting
RT   for Pro, causing hemolytic anemia.";
RL   Hemoglobin 5:667-678(1981).
RN   [125]
RP   INVOLVEMENT IN HEIBAN, AND VARIANT HAMMERSMITH SER-43.
RX   PubMed=6259091;
RA   Rahbar S., Feagler R.J., Beutler E.;
RT   "Hemoglobin Hammersmith (beta 42 (CD1) Phe replaced by Ser) associated
RT   with severe hemolytic anemia.";
RL   Hemoglobin 5:97-105(1981).
RN   [126]
RP   INVOLVEMENT IN HEIBAN, AND VARIANTS BRUXELLES PHE-42 DEL AND PHE-43
RP   DEL.
RX   PubMed=2599881;
RA   Blouquit Y., Bardakdjian J., Lena-Russo D., Arous N., Perrimond H.,
RA   Orsini A., Rosa J., Galacteros F.;
RT   "Hb Bruxelles: alpha 2A beta (2)41 or 42(C7 or CD1)Phe deleted.";
RL   Hemoglobin 13:465-474(1989).
RN   [127]
RP   VARIANT ZENGCHENG MET-115.
RX   MEDLINE=91177717; PubMed=2079435;
RA   Plaseska D., Wilson J.B., Gu L.H., Kutlar F., Huisman T.H.J.,
RA   Zeng Y.T., Shen M.;
RT   "Hb Zengcheng or alpha 2 beta(2)114(G16)Leu-->Met.";
RL   Hemoglobin 14:555-557(1990).
RN   [128]
RP   VARIANT NON-SPHEROCYTIC HAEMOLITIC ANEMIA GLY-68.
RX   PubMed=8280608; DOI=10.1111/j.1365-2141.1993.tb03178.x;
RA   Fay K.C., Brennan S.O., Costello J.M., Potter H.C., Williamson D.A.,
RA   Trent R.J., Ockelford P.A., Boswell D.R.;
RT   "Haemoglobin Manukau beta 67[E11] Val-->Gly: transfusion-dependent
RT   haemolytic anaemia ameliorated by coexisting alpha thalassaemia.";
RL   Br. J. Haematol. 85:352-355(1993).
RN   [129]
RP   INVOLVEMENT IN HEIBAN, AND VARIANT BRISTOL ASP-68.
RX   PubMed=8704193;
RA   Rees D.C., Rochette J., Schofield C., Green B., Morris M.,
RA   Parker N.E., Sasaki H., Tanaka A., Ohba Y., Clegg J.B.;
RT   "A novel silent posttranslational mechanism converts methionine to
RT   aspartate in hemoglobin Bristol (beta 67[E11] Val-Met->Asp).";
RL   Blood 88:341-348(1996).
RN   [130]
RP   VARIANT IRAQ-HALABJA VAL-11.
RX   PubMed=10398311;
RX   DOI=10.1002/(SICI)1096-8652(199907)61:3<187::AID-AJH5>3.0.CO;2-7;
RA   Deutsch S., Darbellay R., Offord R.E., Frutiger A., Kister J.,
RA   Wajcman H., Beris P.;
RT   "Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain
RT   silent variant in a family with multiple Hb disorders.";
RL   Am. J. Hematol. 61:187-193(1999).
RN   [131]
RP   VARIANT VILLEJUIF ILE-124.
RX   PubMed=11300351; DOI=10.1081/HEM-100103071;
RA   Carbone V., Salzano A.M., Pagano L., Buffardi S., De Rosa C.,
RA   Pucci P.;
RT   "Identification of Hb Villejuif [beta123(H1)Thr-->Ile] in Southern
RT   Italy.";
RL   Hemoglobin 25:67-78(2001).
RN   [132]
RP   VARIANT TSUKUMI TYR-118.
RX   PubMed=11300344; DOI=10.1081/HEM-100103076;
RA   North M.L., Duwig I., Riou J., Prome D., Yapo A.P., Kister J.,
RA   Bardakdjian-Michau J., Cazenave J.-P., Wajcman H.;
RT   "Hb Tsukumi [beta117(G19)His-->Tyr] found in a Moroccan woman.";
RL   Hemoglobin 25:107-110(2001).
RN   [133]
RP   VARIANT CANTERBURY PHE-113.
RX   PubMed=11939514; DOI=10.1081/HEM-120002942;
RA   Brennan S.O., Potter H.C., Kubala L.M., Carnoutsos S.A.,
RA   Ferguson M.M.;
RT   "Hb Canterbury [beta112(G14)Cys-->Phe]: a new, mildly unstable
RT   variant.";
RL   Hemoglobin 26:67-69(2002).
RN   [134]
RP   VARIANT PYRGOS ASP-84, AND VARIANT E LYS-27.
RX   PubMed=12144064; DOI=10.1081/HEM-120005459;
RA   Sawangareetrakul P., Svasti S., Yodsowon B., Winichagoon P.,
RA   Srisomsap C., Svasti J., Fucharoen S.;
RT   "Double heterozygosity for Hb Pyrgos [beta83(EF7)Gly-->Asp] and Hb E
RT   [beta26(B8)Glu-->Lys] found in association with alpha-thalassemia.";
RL   Hemoglobin 26:191-196(2002).
RN   [135]
RP   VARIANT SANTANDER ASP-35.
RX   PubMed=12603091; DOI=10.1081/HEM-120016378;
RA   Villegas A., Ropero P., Nogales A., Gonzalez F.A., Mateo M., Mazo E.,
RA   Rodrigo E., Arias M.;
RT   "Hb Santander [beta34(B16)Val-->Asp (GTC-->GAC)]: a new unstable
RT   variant found as a de novo mutation in a Spanish patient.";
RL   Hemoglobin 27:31-35(2003).
RN   [136]
RP   VARIANT NANTES LEU-35, AND VARIANT VEXIN LEU-117.
RX   PubMed=12908805; DOI=10.1081/HEM-120023384;
RA   Wajcman H., Bardakdjian-Michau J., Riou J., Prehu C., Kister J.,
RA   Baudin-Creuza V., Prome D., Richelme-David S., Harousseau J.L.,
RA   Galacteros F.;
RT   "Two new hemoglobin variants with increased oxygen affinity: Hb Nantes
RT   [beta34(B16)Val-->Leu] and Hb Vexin [beta116(G18)His-->Leu].";
RL   Hemoglobin 27:191-199(2003).
RN   [137]
RP   VARIANT LYS-27.
RX   PubMed=15481886; DOI=10.1081/HEM-120040334;
RA   Flatz G., Sanguansermsri T., Sengchanh S., Horst D., Horst J.;
RT   "The 'hot-spot' of Hb E [beta26(B8)Glu-->Lys] in Southeast Asia: beta-
RT   globin anomalies in the Lao Theung population of southern Laos.";
RL   Hemoglobin 28:197-204(2004).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- FUNCTION: LVV-hemorphin-7 potentiates the activity of bradykinin,
CC       causing a decrease in blood pressure.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA).
CC   -!- INTERACTION:
CC       P69905:HBA2; NbExp=19; IntAct=EBI-715554, EBI-714680;
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- PTM: Glucose reacts non-enzymatically with the N-terminus of the
CC       beta chain to form a stable ketoamine linkage. This takes place
CC       slowly and continuously throughout the 120-day life span of the
CC       red blood cell. The rate of glycation is increased in patients
CC       with diabetes mellitus.
CC   -!- PTM: S-nitrosylated; a nitric oxide group is first bound to Fe(2+)
CC       and then transferred to Cys-94 to allow capture of O(2).
CC   -!- PTM: Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin
CC       exposure. PubMed:16916647 reports the identification of HBB
CC       acetylated on Lys-145 in the cytosolic fraction of HeLa cells.
CC       This may have resulted from contamination of the sample.
CC   -!- MASS SPECTROMETRY: Mass=1310; Method=FAB; Range=33-42;
CC       Source=PubMed:1575724;
CC   -!- DISEASE: Defects in HBB may be a cause of Heinz body anemias
CC       (HEIBAN) [MIM:140700]. This is a form of non-spherocytic hemolytic
CC       anemia of Dacie type 1. After splenectomy, which has little
CC       benefit, basophilic inclusions called Heinz bodies are
CC       demonstrable in the erythrocytes. Before splenectomy, diffuse or
CC       punctate basophilia may be evident. Most of these cases are
CC       probably instances of hemoglobinopathy. The hemoglobin
CC       demonstrates heat lability. Heinz bodies are observed also with
CC       the Ivemark syndrome (asplenia with cardiovascular anomalies) and
CC       with glutathione peroxidase deficiency.
CC   -!- DISEASE: Defects in HBB are the cause of beta-thalassemia (B-THAL)
CC       [MIM:613985]. A form of thalassemia. Thalassemias are common
CC       monogenic diseases occurring mostly in Mediterranean and Southeast
CC       Asian populations. The hallmark of beta-thalassemia is an
CC       imbalance in globin-chain production in the adult HbA molecule.
CC       Absence of beta chain causes beta(0)-thalassemia, while reduced
CC       amounts of detectable beta globin causes beta(+)-thalassemia. In
CC       the severe forms of beta-thalassemia, the excess alpha globin
CC       chains accumulate in the developing erythroid precursors in the
CC       marrow. Their deposition leads to a vast increase in erythroid
CC       apoptosis that in turn causes ineffective erythropoiesis and
CC       severe microcytic hypochromic anemia. Clinically, beta-thalassemia
CC       is divided into thalassemia major which is transfusion dependent,
CC       thalassemia intermedia (of intermediate severity), and thalassemia
CC       minor that is asymptomatic.
CC   -!- DISEASE: Defects in HBB are the cause of sickle cell anemia (SKCA)
CC       [MIM:603903]; also known as sickle cell disease. Sickle cell
CC       anemia is characterized by abnormally shaped red cells resulting
CC       in chronic anemia and periodic episodes of pain, serious
CC       infections and damage to vital organs. Normal red blood cells are
CC       round and flexible and flow easily through blood vessels, but in
CC       sickle cell anemia, the abnormal hemoglobin (called Hb S) causes
CC       red blood cells to become stiff. They are C-shaped and resembles a
CC       sickle. These stiffer red blood cells can led to microvascular
CC       occlusion thus cutting off the blood supply to nearby tissues.
CC   -!- DISEASE: Defects in HBB are the cause of beta-thalassemia dominant
CC       inclusion body type (B-THALIB) [MIM:603902]. An autosomal dominant
CC       form of beta thalassemia characterized by moderate anemia,
CC       lifelong jaundice, cholelithiasis and splenomegaly, marked
CC       morphologic changes in the red cells, erythroid hyperplasia of the
CC       bone marrow with increased numbers of multinucleate red cell
CC       precursors, and the presence of large inclusion bodies in the
CC       normoblasts, both in the marrow and in the peripheral blood after
CC       splenectomy.
CC   -!- MISCELLANEOUS: One molecule of 2,3-bisphosphoglycerate can bind to
CC       two beta chains per hemoglobin tetramer.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -!- WEB RESOURCE: Name=HbVar; Note=Human hemoglobin variants and
CC       thalassemias;
CC       URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBB";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/HBB";
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBB";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Hemoglobin entry;
CC       URL="http://en.wikipedia.org/wiki/Hemoglobin";
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DR   EMBL; M25079; AAA35597.1; -; mRNA.
DR   EMBL; V00499; CAA23758.1; -; Genomic_DNA.
DR   EMBL; DQ126270; AAZ39745.1; -; Genomic_DNA.
DR   EMBL; DQ126271; AAZ39746.1; -; Genomic_DNA.
DR   EMBL; DQ126272; AAZ39747.1; -; Genomic_DNA.
DR   EMBL; DQ126273; AAZ39748.1; -; Genomic_DNA.
DR   EMBL; DQ126274; AAZ39749.1; -; Genomic_DNA.
DR   EMBL; DQ126275; AAZ39750.1; -; Genomic_DNA.
DR   EMBL; DQ126276; AAZ39751.1; -; Genomic_DNA.
DR   EMBL; DQ126277; AAZ39752.1; -; Genomic_DNA.
DR   EMBL; DQ126278; AAZ39753.1; -; Genomic_DNA.
DR   EMBL; DQ126279; AAZ39754.1; -; Genomic_DNA.
DR   EMBL; DQ126280; AAZ39755.1; -; Genomic_DNA.
DR   EMBL; DQ126281; AAZ39756.1; -; Genomic_DNA.
DR   EMBL; DQ126282; AAZ39757.1; -; Genomic_DNA.
DR   EMBL; DQ126283; AAZ39758.1; -; Genomic_DNA.
DR   EMBL; DQ126284; AAZ39759.1; -; Genomic_DNA.
DR   EMBL; DQ126285; AAZ39760.1; -; Genomic_DNA.
DR   EMBL; DQ126286; AAZ39761.1; -; Genomic_DNA.
DR   EMBL; DQ126287; AAZ39762.1; -; Genomic_DNA.
DR   EMBL; DQ126288; AAZ39763.1; -; Genomic_DNA.
DR   EMBL; DQ126289; AAZ39764.1; -; Genomic_DNA.
DR   EMBL; DQ126290; AAZ39765.1; -; Genomic_DNA.
DR   EMBL; DQ126291; AAZ39766.1; -; Genomic_DNA.
DR   EMBL; DQ126292; AAZ39767.1; -; Genomic_DNA.
DR   EMBL; DQ126293; AAZ39768.1; -; Genomic_DNA.
DR   EMBL; DQ126294; AAZ39769.1; -; Genomic_DNA.
DR   EMBL; DQ126295; AAZ39770.1; -; Genomic_DNA.
DR   EMBL; DQ126296; AAZ39771.1; -; Genomic_DNA.
DR   EMBL; DQ126297; AAZ39772.1; -; Genomic_DNA.
DR   EMBL; DQ126298; AAZ39773.1; -; Genomic_DNA.
DR   EMBL; DQ126299; AAZ39774.1; -; Genomic_DNA.
DR   EMBL; DQ126300; AAZ39775.1; -; Genomic_DNA.
DR   EMBL; DQ126301; AAZ39776.1; -; Genomic_DNA.
DR   EMBL; DQ126302; AAZ39777.1; -; Genomic_DNA.
DR   EMBL; DQ126303; AAZ39778.1; -; Genomic_DNA.
DR   EMBL; DQ126304; AAZ39779.1; -; Genomic_DNA.
DR   EMBL; DQ126305; AAZ39780.1; -; Genomic_DNA.
DR   EMBL; DQ126306; AAZ39781.1; -; Genomic_DNA.
DR   EMBL; DQ126307; AAZ39782.1; -; Genomic_DNA.
DR   EMBL; DQ126308; AAZ39783.1; -; Genomic_DNA.
DR   EMBL; DQ126309; AAZ39784.1; -; Genomic_DNA.
DR   EMBL; DQ126310; AAZ39785.1; -; Genomic_DNA.
DR   EMBL; DQ126311; AAZ39786.1; -; Genomic_DNA.
DR   EMBL; DQ126312; AAZ39787.1; -; Genomic_DNA.
DR   EMBL; DQ126313; AAZ39788.1; -; Genomic_DNA.
DR   EMBL; DQ126314; AAZ39789.1; -; Genomic_DNA.
DR   EMBL; DQ126315; AAZ39790.1; -; Genomic_DNA.
DR   EMBL; DQ126316; AAZ39791.1; -; Genomic_DNA.
DR   EMBL; DQ126317; AAZ39792.1; -; Genomic_DNA.
DR   EMBL; DQ126318; AAZ39793.1; -; Genomic_DNA.
DR   EMBL; DQ126319; AAZ39794.1; -; Genomic_DNA.
DR   EMBL; DQ126320; AAZ39795.1; -; Genomic_DNA.
DR   EMBL; DQ126321; AAZ39796.1; -; Genomic_DNA.
DR   EMBL; DQ126322; AAZ39797.1; -; Genomic_DNA.
DR   EMBL; DQ126323; AAZ39798.1; -; Genomic_DNA.
DR   EMBL; DQ126324; AAZ39799.1; -; Genomic_DNA.
DR   EMBL; DQ126325; AAZ39800.1; -; Genomic_DNA.
DR   EMBL; AF007546; AAB62944.1; -; Genomic_DNA.
DR   EMBL; AF083883; AAL68978.1; -; Genomic_DNA.
DR   EMBL; AF117710; AAD19696.1; -; mRNA.
DR   EMBL; AF181989; AAF00489.1; -; mRNA.
DR   EMBL; AF349114; AAK29639.1; -; mRNA.
DR   EMBL; AF527577; AAM92001.1; -; Genomic_DNA.
DR   EMBL; AY136510; AAN11320.1; -; mRNA.
DR   EMBL; AY163866; AAN84548.1; -; Genomic_DNA.
DR   EMBL; AY260740; AAP21062.1; -; Genomic_DNA.
DR   EMBL; AY509193; AAR96398.1; -; mRNA.
DR   EMBL; EF450778; ABO36678.1; -; Genomic_DNA.
DR   EMBL; EU694432; ACD39349.1; -; mRNA.
DR   EMBL; AK311825; BAG34767.1; -; mRNA.
DR   EMBL; CR536530; CAG38767.1; -; mRNA.
DR   EMBL; CR541913; CAG46711.1; -; mRNA.
DR   EMBL; CH471064; EAW68806.1; -; Genomic_DNA.
DR   EMBL; BC007075; AAH07075.1; -; mRNA.
DR   EMBL; U01317; AAA16334.1; -; Genomic_DNA.
DR   EMBL; V00497; CAA23756.1; -; mRNA.
DR   EMBL; V00500; CAA23759.1; ALT_SEQ; mRNA.
DR   EMBL; L26462; AAA21100.1; -; Genomic_DNA.
DR   EMBL; L26463; AAA21101.1; -; Genomic_DNA.
DR   EMBL; L26464; AAA21102.1; -; Genomic_DNA.
DR   EMBL; L26465; AAA21103.1; -; Genomic_DNA.
DR   EMBL; L26466; AAA21104.1; -; Genomic_DNA.
DR   EMBL; L26467; AAA21105.1; -; Genomic_DNA.
DR   EMBL; L26468; AAA21106.1; -; Genomic_DNA.
DR   EMBL; L26469; AAA21107.1; -; Genomic_DNA.
DR   EMBL; L26470; AAA21108.1; -; Genomic_DNA.
DR   EMBL; L26471; AAA21109.1; -; Genomic_DNA.
DR   EMBL; L26472; AAA21110.1; -; Genomic_DNA.
DR   EMBL; L26473; AAA21111.1; -; Genomic_DNA.
DR   EMBL; L26474; AAA21112.1; -; Genomic_DNA.
DR   EMBL; L26475; AAA21113.1; -; Genomic_DNA.
DR   EMBL; L26476; AAA21114.1; -; Genomic_DNA.
DR   EMBL; L26477; AAA21115.1; -; Genomic_DNA.
DR   EMBL; L26478; AAA21116.1; -; Genomic_DNA.
DR   EMBL; L48213; AAA88063.1; -; Genomic_DNA.
DR   EMBL; L48214; AAA88061.1; -; Genomic_DNA.
DR   EMBL; L48215; AAA88059.1; -; Genomic_DNA.
DR   EMBL; L48216; AAA88065.1; -; Genomic_DNA.
DR   EMBL; L48217; AAA88067.1; -; Genomic_DNA.
DR   EMBL; M36640; AAA52634.1; -; Genomic_DNA.
DR   EMBL; M11428; AAA52633.1; -; mRNA.
DR   EMBL; M25113; AAA35966.1; -; mRNA.
DR   EMBL; L48932; AAA88054.1; -; Genomic_DNA.
DR   IPI; IPI00654755; -.
DR   PIR; A53136; HBHU.
DR   RefSeq; NP_000509.1; NM_000518.4.
DR   UniGene; Hs.523443; -.
DR   PDB; 1A00; X-ray; 2.00 A; B/D=3-147.
DR   PDB; 1A01; X-ray; 1.80 A; B/D=3-147.
DR   PDB; 1A0U; X-ray; 2.14 A; B/D=3-147.
DR   PDB; 1A0Z; X-ray; 2.00 A; B/D=3-147.
DR   PDB; 1A3N; X-ray; 1.80 A; B/D=2-147.
DR   PDB; 1A3O; X-ray; 1.80 A; B/D=2-147.
DR   PDB; 1ABW; X-ray; 2.00 A; B/D=3-147.
DR   PDB; 1ABY; X-ray; 2.60 A; B/D=3-147.
DR   PDB; 1AJ9; X-ray; 2.20 A; B=2-147.
DR   PDB; 1B86; X-ray; 2.50 A; B/D=2-147.
DR   PDB; 1BAB; X-ray; 1.50 A; B/D=2-147.
DR   PDB; 1BBB; X-ray; 1.70 A; B/D=2-147.
DR   PDB; 1BIJ; X-ray; 2.30 A; B/D=2-147.
DR   PDB; 1BUW; X-ray; 1.90 A; B/D=2-147.
DR   PDB; 1BZ0; X-ray; 1.50 A; B/D=2-147.
DR   PDB; 1BZ1; X-ray; 1.59 A; B/D=2-147.
DR   PDB; 1BZZ; X-ray; 1.59 A; B/D=2-147.
DR   PDB; 1C7B; X-ray; 1.80 A; B/D=3-147.
DR   PDB; 1C7C; X-ray; 1.80 A; B/D=3-147.
DR   PDB; 1C7D; X-ray; 1.80 A; B/D=3-147.
DR   PDB; 1CBL; X-ray; 1.80 A; A/B/C/D=2-147.
DR   PDB; 1CBM; X-ray; 1.74 A; A/B/C/D=1-147.
DR   PDB; 1CH4; X-ray; 2.50 A; A/B/C/D=2-107.
DR   PDB; 1CLS; X-ray; 1.90 A; B/D=1-147.
DR   PDB; 1CMY; X-ray; 3.00 A; B/D=1-147.
DR   PDB; 1COH; X-ray; 2.90 A; B/D=1-147.
DR   PDB; 1DKE; X-ray; 2.10 A; B/D=1-147.
DR   PDB; 1DXT; X-ray; 1.70 A; B/D=1-147.
DR   PDB; 1DXU; X-ray; 1.70 A; B/D=3-147.
DR   PDB; 1DXV; X-ray; 1.70 A; B/D=3-147.
DR   PDB; 1FN3; X-ray; 2.48 A; B/D=2-147.
DR   PDB; 1G9V; X-ray; 1.85 A; B/D=2-147.
DR   PDB; 1GBU; X-ray; 1.80 A; B/D=2-147.
DR   PDB; 1GBV; X-ray; 2.00 A; B/D=2-147.
DR   PDB; 1GLI; X-ray; 2.50 A; B/D=3-147.
DR   PDB; 1GZX; X-ray; 2.10 A; B/D=2-147.
DR   PDB; 1HAB; X-ray; 2.30 A; B/D=2-146.
DR   PDB; 1HAC; X-ray; 2.60 A; B/D=2-146.
DR   PDB; 1HBA; X-ray; 2.10 A; B/D=2-147.
DR   PDB; 1HBB; X-ray; 1.90 A; B/D=2-147.
DR   PDB; 1HBS; X-ray; 3.00 A; B/D/F/H=1-147.
DR   PDB; 1HCO; X-ray; 2.70 A; B=2-147.
DR   PDB; 1HDB; X-ray; 2.20 A; B/D=1-147.
DR   PDB; 1HGA; X-ray; 2.10 A; B/D=1-147.
DR   PDB; 1HGB; X-ray; 2.10 A; B/D=1-147.
DR   PDB; 1HGC; X-ray; 2.10 A; B/D=1-147.
DR   PDB; 1HHO; X-ray; 2.10 A; B=1-147.
DR   PDB; 1IRD; X-ray; 1.25 A; B=1-147.
DR   PDB; 1J3Y; X-ray; 1.55 A; B/D/F/H=1-147.
DR   PDB; 1J3Z; X-ray; 1.60 A; B/D/F/H=1-147.
DR   PDB; 1J40; X-ray; 1.45 A; B/D/F/H=1-147.
DR   PDB; 1J41; X-ray; 1.45 A; B/D/F/H=1-147.
DR   PDB; 1J7S; X-ray; 2.20 A; B/D=3-147.
DR   PDB; 1J7W; X-ray; 2.00 A; B/D=3-147.
DR   PDB; 1J7Y; X-ray; 1.70 A; B/D=3-147.
DR   PDB; 1JY7; X-ray; 3.20 A; B/D/Q/S/V/X=1-147.
DR   PDB; 1K0Y; X-ray; 1.87 A; B/D=1-147.
DR   PDB; 1K1K; X-ray; 2.00 A; B=1-147.
DR   PDB; 1KD2; X-ray; 1.87 A; B/D=1-147.
DR   PDB; 1LFL; X-ray; 2.70 A; B/D/Q/S=1-147.
DR   PDB; 1LFQ; X-ray; 2.60 A; B=1-147.
DR   PDB; 1LFT; X-ray; 2.60 A; B=1-147.
DR   PDB; 1LFV; X-ray; 2.80 A; B=1-147.
DR   PDB; 1LFY; X-ray; 3.30 A; B=1-147.
DR   PDB; 1LFZ; X-ray; 3.10 A; B=1-147.
DR   PDB; 1LJW; X-ray; 2.16 A; B=1-147.
DR   PDB; 1M9P; X-ray; 2.10 A; B/D=1-147.
DR   PDB; 1MKO; X-ray; 2.18 A; B/D=1-147.
DR   PDB; 1NEJ; X-ray; 2.10 A; B/D=1-147.
DR   PDB; 1NIH; X-ray; 2.60 A; B/D=1-147.
DR   PDB; 1NQP; X-ray; 1.73 A; B/D=1-147.
DR   PDB; 1O1I; X-ray; 2.30 A; B=1-147.
DR   PDB; 1O1J; X-ray; 1.90 A; B/D=1-147.
DR   PDB; 1O1K; X-ray; 2.00 A; B/D=1-147.
DR   PDB; 1O1L; X-ray; 1.80 A; B/D=1-147.
DR   PDB; 1O1M; X-ray; 1.85 A; B/D=1-147.
DR   PDB; 1O1N; X-ray; 1.80 A; B/D=1-147.
DR   PDB; 1O1O; X-ray; 1.80 A; B/D=1-147.
DR   PDB; 1O1P; X-ray; 1.80 A; B/D=1-147.
DR   PDB; 1QI8; X-ray; 1.80 A; B/D=3-147.
DR   PDB; 1QSH; X-ray; 1.70 A; B/D=1-147.
DR   PDB; 1QSI; X-ray; 1.70 A; B/D=1-147.
DR   PDB; 1QXD; X-ray; 2.25 A; B/D=1-147.
DR   PDB; 1QXE; X-ray; 1.85 A; B/D=1-147.
DR   PDB; 1R1X; X-ray; 2.15 A; B=1-147.
DR   PDB; 1R1Y; X-ray; 1.80 A; B/D=1-147.
DR   PDB; 1RPS; X-ray; 2.11 A; B/D=1-147.
DR   PDB; 1RQ3; X-ray; 1.91 A; B/D=1-147.
DR   PDB; 1RQ4; X-ray; 2.11 A; B/D=1-147.
DR   PDB; 1RQA; X-ray; 2.11 A; B/D=3-147.
DR   PDB; 1RVW; X-ray; 2.50 A; B=1-147.
DR   PDB; 1SDK; X-ray; 1.80 A; B/D=1-147.
DR   PDB; 1SDL; X-ray; 1.80 A; B/D=1-147.
DR   PDB; 1THB; X-ray; 1.50 A; B/D=1-147.
DR   PDB; 1UIW; X-ray; 1.50 A; B/D/F/H=1-147.
DR   PDB; 1VWT; X-ray; 1.90 A; B/D=1-147.
DR   PDB; 1XXT; X-ray; 1.91 A; B/D=1-147.
DR   PDB; 1XY0; X-ray; 1.99 A; B/D=1-147.
DR   PDB; 1XYE; X-ray; 2.13 A; B/D=1-147.
DR   PDB; 1XZ2; X-ray; 1.90 A; B/D=1-147.
DR   PDB; 1XZ4; X-ray; 2.00 A; B/D=1-147.
DR   PDB; 1XZ5; X-ray; 2.11 A; B/D=1-147.
DR   PDB; 1XZ7; X-ray; 1.90 A; B/D=1-147.
DR   PDB; 1XZU; X-ray; 2.16 A; B/D=1-147.
DR   PDB; 1XZV; X-ray; 2.11 A; B/D=1-147.
DR   PDB; 1Y09; X-ray; 2.25 A; B/D=1-147.
DR   PDB; 1Y0A; X-ray; 2.22 A; B/D=1-147.
DR   PDB; 1Y0C; X-ray; 2.30 A; B/D=1-147.
DR   PDB; 1Y0D; X-ray; 2.10 A; B/D=1-147.
DR   PDB; 1Y0T; X-ray; 2.14 A; B/D=3-147.
DR   PDB; 1Y0W; X-ray; 2.14 A; B/D=3-147.
DR   PDB; 1Y22; X-ray; 2.16 A; B/D=3-147.
DR   PDB; 1Y2Z; X-ray; 2.07 A; B/D=3-147.
DR   PDB; 1Y31; X-ray; 2.13 A; B/D=3-147.
DR   PDB; 1Y35; X-ray; 2.12 A; B/D=3-147.
DR   PDB; 1Y45; X-ray; 2.00 A; B/D=3-147.
DR   PDB; 1Y46; X-ray; 2.22 A; B/D=3-147.
DR   PDB; 1Y4B; X-ray; 2.10 A; B/D=3-147.
DR   PDB; 1Y4F; X-ray; 2.00 A; B/D=3-147.
DR   PDB; 1Y4G; X-ray; 1.91 A; B/D=3-147.
DR   PDB; 1Y4P; X-ray; 1.98 A; B/D=3-147.
DR   PDB; 1Y4Q; X-ray; 2.11 A; B/D=3-147.
DR   PDB; 1Y4R; X-ray; 2.22 A; B/D=3-147.
DR   PDB; 1Y4V; X-ray; 1.84 A; B/D=3-147.
DR   PDB; 1Y5F; X-ray; 2.14 A; B/D=3-147.
DR   PDB; 1Y5J; X-ray; 2.03 A; B/D=3-147.
DR   PDB; 1Y5K; X-ray; 2.20 A; B/D=3-147.
DR   PDB; 1Y7C; X-ray; 2.10 A; B/D=3-147.
DR   PDB; 1Y7D; X-ray; 1.90 A; B/D=3-147.
DR   PDB; 1Y7G; X-ray; 2.10 A; B/D=3-147.
DR   PDB; 1Y7Z; X-ray; 1.98 A; B/D=3-147.
DR   PDB; 1Y83; X-ray; 1.90 A; B/D=3-147.
DR   PDB; 1Y85; X-ray; 2.13 A; B/D=1-146.
DR   PDB; 1Y8W; X-ray; 2.90 A; B/D=1-147.
DR   PDB; 1YDZ; X-ray; 3.30 A; B/D=1-147.
DR   PDB; 1YE0; X-ray; 2.50 A; B/D=3-147.
DR   PDB; 1YE1; X-ray; 4.50 A; B/D=3-147.
DR   PDB; 1YE2; X-ray; 1.80 A; B/D=3-147.
DR   PDB; 1YEN; X-ray; 2.80 A; B/D=3-147.
DR   PDB; 1YEO; X-ray; 2.22 A; B/D=3-147.
DR   PDB; 1YEQ; X-ray; 2.75 A; B/D=3-147.
DR   PDB; 1YEU; X-ray; 2.12 A; B/D=3-147.
DR   PDB; 1YEV; X-ray; 2.11 A; B/D=3-147.
DR   PDB; 1YFF; X-ray; 2.40 A; B/D/F/H=1-147.
DR   PDB; 1YG5; X-ray; 2.70 A; B/D=3-147.
DR   PDB; 1YGD; X-ray; 2.73 A; B/D=3-147.
DR   PDB; 1YGF; X-ray; 2.70 A; B/D=3-147.
DR   PDB; 1YH9; X-ray; 2.20 A; B/D=1-147.
DR   PDB; 1YHE; X-ray; 2.10 A; B/D=1-147.
DR   PDB; 1YHR; X-ray; 2.60 A; B/D=1-147.
DR   PDB; 1YIE; X-ray; 2.40 A; B/D=3-147.
DR   PDB; 1YIH; X-ray; 2.00 A; B/D=3-147.
DR   PDB; 1YVQ; X-ray; 1.80 A; B/D=1-147.
DR   PDB; 1YVT; X-ray; 1.80 A; B=1-147.
DR   PDB; 1YZI; X-ray; 2.07 A; B=1-147.
DR   PDB; 2D5Z; X-ray; 1.45 A; B/D=1-147.
DR   PDB; 2D60; X-ray; 1.70 A; B/D=1-147.
DR   PDB; 2DN1; X-ray; 1.25 A; B=1-147.
DR   PDB; 2DN2; X-ray; 1.25 A; B/D=1-147.
DR   PDB; 2DN3; X-ray; 1.25 A; B=2-147.
DR   PDB; 2DXM; Neutron; 2.10 A; B/D=2-147.
DR   PDB; 2H35; NMR; -; B/D=2-147.
DR   PDB; 2HBC; X-ray; 2.10 A; B=1-147.
DR   PDB; 2HBD; X-ray; 2.20 A; B=1-147.
DR   PDB; 2HBE; X-ray; 2.00 A; B=1-147.
DR   PDB; 2HBF; X-ray; 2.20 A; B=1-147.
DR   PDB; 2HBS; X-ray; 2.05 A; B/D/F/H=1-147.
DR   PDB; 2HCO; X-ray; 2.70 A; B=2-147.
DR   PDB; 2HHB; X-ray; 1.74 A; B/D=2-147.
DR   PDB; 2HHD; X-ray; 2.20 A; B/D=1-147.
DR   PDB; 2HHE; X-ray; 2.20 A; B/D=4-147.
DR   PDB; 2W6V; X-ray; 1.80 A; B/D=2-147.
DR   PDB; 2W72; X-ray; 1.07 A; B/D=3-147.
DR   PDB; 2YRS; X-ray; 2.30 A; B/D/K/O=2-147.
DR   PDB; 3B75; X-ray; 2.30 A; B/D/F/H/T=2-147.
DR   PDB; 3D17; X-ray; 2.80 A; B/D=2-147.
DR   PDB; 3D7O; X-ray; 1.80 A; B=2-147.
DR   PDB; 3DUT; X-ray; 1.55 A; B/D=2-147.
DR   PDB; 3HHB; X-ray; 1.74 A; B/D=2-147.
DR   PDB; 3HXN; X-ray; 2.00 A; B/D=2-147.
DR   PDB; 3IC0; X-ray; 1.80 A; B/D=2-146.
DR   PDB; 3IC2; X-ray; 2.40 A; B/D=2-147.
DR   PDB; 3KMF; Neutron; 2.00 A; C/G=2-147.
DR   PDB; 3NL7; X-ray; 1.80 A; B=2-147.
DR   PDB; 3NMM; X-ray; 1.60 A; B/D=2-147.
DR   PDB; 3ODQ; X-ray; 3.10 A; B/D=2-147.
DR   PDB; 3ONZ; X-ray; 2.09 A; B=2-147.
DR   PDB; 3OO4; X-ray; 1.90 A; B=2-147.
DR   PDB; 3OO5; X-ray; 2.10 A; B=2-147.
DR   PDB; 3P5Q; X-ray; 2.00 A; B=2-147.
DR   PDB; 3QJB; X-ray; 1.80 A; B=2-147.
DR   PDB; 3QJC; X-ray; 2.00 A; B=2-147.
DR   PDB; 3QJD; X-ray; 1.56 A; B/D=2-147.
DR   PDB; 3QJE; X-ray; 1.80 A; B/D=2-147.
DR   PDB; 3R5I; X-ray; 2.20 A; B/D=2-147.
DR   PDB; 3S65; X-ray; 1.80 A; B/D=2-147.
DR   PDB; 3S66; X-ray; 1.40 A; B=2-147.
DR   PDB; 3SZK; X-ray; 3.01 A; B/E=2-147.
DR   PDB; 4HHB; X-ray; 1.74 A; B/D=2-147.
DR   PDB; 6HBW; X-ray; 2.00 A; B/D=2-147.
DR   PDBsum; 1A00; -.
DR   PDBsum; 1A01; -.
DR   PDBsum; 1A0U; -.
DR   PDBsum; 1A0Z; -.
DR   PDBsum; 1A3N; -.
DR   PDBsum; 1A3O; -.
DR   PDBsum; 1ABW; -.
DR   PDBsum; 1ABY; -.
DR   PDBsum; 1AJ9; -.
DR   PDBsum; 1B86; -.
DR   PDBsum; 1BAB; -.
DR   PDBsum; 1BBB; -.
DR   PDBsum; 1BIJ; -.
DR   PDBsum; 1BUW; -.
DR   PDBsum; 1BZ0; -.
DR   PDBsum; 1BZ1; -.
DR   PDBsum; 1BZZ; -.
DR   PDBsum; 1C7B; -.
DR   PDBsum; 1C7C; -.
DR   PDBsum; 1C7D; -.
DR   PDBsum; 1CBL; -.
DR   PDBsum; 1CBM; -.
DR   PDBsum; 1CH4; -.
DR   PDBsum; 1CLS; -.
DR   PDBsum; 1CMY; -.
DR   PDBsum; 1COH; -.
DR   PDBsum; 1DKE; -.
DR   PDBsum; 1DXT; -.
DR   PDBsum; 1DXU; -.
DR   PDBsum; 1DXV; -.
DR   PDBsum; 1FN3; -.
DR   PDBsum; 1G9V; -.
DR   PDBsum; 1GBU; -.
DR   PDBsum; 1GBV; -.
DR   PDBsum; 1GLI; -.
DR   PDBsum; 1GZX; -.
DR   PDBsum; 1HAB; -.
DR   PDBsum; 1HAC; -.
DR   PDBsum; 1HBA; -.
DR   PDBsum; 1HBB; -.
DR   PDBsum; 1HBS; -.
DR   PDBsum; 1HCO; -.
DR   PDBsum; 1HDB; -.
DR   PDBsum; 1HGA; -.
DR   PDBsum; 1HGB; -.
DR   PDBsum; 1HGC; -.
DR   PDBsum; 1HHO; -.
DR   PDBsum; 1IRD; -.
DR   PDBsum; 1J3Y; -.
DR   PDBsum; 1J3Z; -.
DR   PDBsum; 1J40; -.
DR   PDBsum; 1J41; -.
DR   PDBsum; 1J7S; -.
DR   PDBsum; 1J7W; -.
DR   PDBsum; 1J7Y; -.
DR   PDBsum; 1JY7; -.
DR   PDBsum; 1K0Y; -.
DR   PDBsum; 1K1K; -.
DR   PDBsum; 1KD2; -.
DR   PDBsum; 1LFL; -.
DR   PDBsum; 1LFQ; -.
DR   PDBsum; 1LFT; -.
DR   PDBsum; 1LFV; -.
DR   PDBsum; 1LFY; -.
DR   PDBsum; 1LFZ; -.
DR   PDBsum; 1LJW; -.
DR   PDBsum; 1M9P; -.
DR   PDBsum; 1MKO; -.
DR   PDBsum; 1NEJ; -.
DR   PDBsum; 1NIH; -.
DR   PDBsum; 1NQP; -.
DR   PDBsum; 1O1I; -.
DR   PDBsum; 1O1J; -.
DR   PDBsum; 1O1K; -.
DR   PDBsum; 1O1L; -.
DR   PDBsum; 1O1M; -.
DR   PDBsum; 1O1N; -.
DR   PDBsum; 1O1O; -.
DR   PDBsum; 1O1P; -.
DR   PDBsum; 1QI8; -.
DR   PDBsum; 1QSH; -.
DR   PDBsum; 1QSI; -.
DR   PDBsum; 1QXD; -.
DR   PDBsum; 1QXE; -.
DR   PDBsum; 1R1X; -.
DR   PDBsum; 1R1Y; -.
DR   PDBsum; 1RPS; -.
DR   PDBsum; 1RQ3; -.
DR   PDBsum; 1RQ4; -.
DR   PDBsum; 1RQA; -.
DR   PDBsum; 1RVW; -.
DR   PDBsum; 1SDK; -.
DR   PDBsum; 1SDL; -.
DR   PDBsum; 1THB; -.
DR   PDBsum; 1UIW; -.
DR   PDBsum; 1VWT; -.
DR   PDBsum; 1XXT; -.
DR   PDBsum; 1XY0; -.
DR   PDBsum; 1XYE; -.
DR   PDBsum; 1XZ2; -.
DR   PDBsum; 1XZ4; -.
DR   PDBsum; 1XZ5; -.
DR   PDBsum; 1XZ7; -.
DR   PDBsum; 1XZU; -.
DR   PDBsum; 1XZV; -.
DR   PDBsum; 1Y09; -.
DR   PDBsum; 1Y0A; -.
DR   PDBsum; 1Y0C; -.
DR   PDBsum; 1Y0D; -.
DR   PDBsum; 1Y0T; -.
DR   PDBsum; 1Y0W; -.
DR   PDBsum; 1Y22; -.
DR   PDBsum; 1Y2Z; -.
DR   PDBsum; 1Y31; -.
DR   PDBsum; 1Y35; -.
DR   PDBsum; 1Y45; -.
DR   PDBsum; 1Y46; -.
DR   PDBsum; 1Y4B; -.
DR   PDBsum; 1Y4F; -.
DR   PDBsum; 1Y4G; -.
DR   PDBsum; 1Y4P; -.
DR   PDBsum; 1Y4Q; -.
DR   PDBsum; 1Y4R; -.
DR   PDBsum; 1Y4V; -.
DR   PDBsum; 1Y5F; -.
DR   PDBsum; 1Y5J; -.
DR   PDBsum; 1Y5K; -.
DR   PDBsum; 1Y7C; -.
DR   PDBsum; 1Y7D; -.
DR   PDBsum; 1Y7G; -.
DR   PDBsum; 1Y7Z; -.
DR   PDBsum; 1Y83; -.
DR   PDBsum; 1Y85; -.
DR   PDBsum; 1Y8W; -.
DR   PDBsum; 1YDZ; -.
DR   PDBsum; 1YE0; -.
DR   PDBsum; 1YE1; -.
DR   PDBsum; 1YE2; -.
DR   PDBsum; 1YEN; -.
DR   PDBsum; 1YEO; -.
DR   PDBsum; 1YEQ; -.
DR   PDBsum; 1YEU; -.
DR   PDBsum; 1YEV; -.
DR   PDBsum; 1YFF; -.
DR   PDBsum; 1YG5; -.
DR   PDBsum; 1YGD; -.
DR   PDBsum; 1YGF; -.
DR   PDBsum; 1YH9; -.
DR   PDBsum; 1YHE; -.
DR   PDBsum; 1YHR; -.
DR   PDBsum; 1YIE; -.
DR   PDBsum; 1YIH; -.
DR   PDBsum; 1YVQ; -.
DR   PDBsum; 1YVT; -.
DR   PDBsum; 1YZI; -.
DR   PDBsum; 2D5Z; -.
DR   PDBsum; 2D60; -.
DR   PDBsum; 2DN1; -.
DR   PDBsum; 2DN2; -.
DR   PDBsum; 2DN3; -.
DR   PDBsum; 2DXM; -.
DR   PDBsum; 2H35; -.
DR   PDBsum; 2HBC; -.
DR   PDBsum; 2HBD; -.
DR   PDBsum; 2HBE; -.
DR   PDBsum; 2HBF; -.
DR   PDBsum; 2HBS; -.
DR   PDBsum; 2HCO; -.
DR   PDBsum; 2HHB; -.
DR   PDBsum; 2HHD; -.
DR   PDBsum; 2HHE; -.
DR   PDBsum; 2W6V; -.
DR   PDBsum; 2W72; -.
DR   PDBsum; 2YRS; -.
DR   PDBsum; 3B75; -.
DR   PDBsum; 3D17; -.
DR   PDBsum; 3D7O; -.
DR   PDBsum; 3DUT; -.
DR   PDBsum; 3HHB; -.
DR   PDBsum; 3HXN; -.
DR   PDBsum; 3IC0; -.
DR   PDBsum; 3IC2; -.
DR   PDBsum; 3KMF; -.
DR   PDBsum; 3NL7; -.
DR   PDBsum; 3NMM; -.
DR   PDBsum; 3ODQ; -.
DR   PDBsum; 3ONZ; -.
DR   PDBsum; 3OO4; -.
DR   PDBsum; 3OO5; -.
DR   PDBsum; 3P5Q; -.
DR   PDBsum; 3QJB; -.
DR   PDBsum; 3QJC; -.
DR   PDBsum; 3QJD; -.
DR   PDBsum; 3QJE; -.
DR   PDBsum; 3R5I; -.
DR   PDBsum; 3S65; -.
DR   PDBsum; 3S66; -.
DR   PDBsum; 3SZK; -.
DR   PDBsum; 4HHB; -.
DR   PDBsum; 6HBW; -.
DR   ProteinModelPortal; P68871; -.
DR   SMR; P68871; 2-147.
DR   IntAct; P68871; 6.
DR   MINT; MINT-5000306; -.
DR   STRING; P68871; -.
DR   PhosphoSite; P68871; -.
DR   DMDM; 56749856; -.
DR   PMMA-2DPAGE; P68871; -.
DR   REPRODUCTION-2DPAGE; IPI00654755; -.
DR   REPRODUCTION-2DPAGE; P68871; -.
DR   Siena-2DPAGE; P68871; -.
DR   SWISS-2DPAGE; P68871; -.
DR   UCD-2DPAGE; P02023; -.
DR   UCD-2DPAGE; P68871; -.
DR   PeptideAtlas; P68871; -.
DR   PRIDE; P68871; -.
DR   DNASU; 3043; -.
DR   Ensembl; ENST00000335295; ENSP00000333994; ENSG00000244734.
DR   GeneID; 3043; -.
DR   KEGG; hsa:3043; -.
DR   UCSC; uc001mae.1; human.
DR   CTD; 3043; -.
DR   GeneCards; GC11M005250; -.
DR   HGNC; HGNC:4827; HBB.
DR   HPA; CAB009526; -.
DR   MIM; 140700; phenotype.
DR   MIM; 141900; gene+phenotype.
DR   MIM; 603902; phenotype.
DR   MIM; 603903; phenotype.
DR   MIM; 613985; phenotype.
DR   neXtProt; NX_P68871; -.
DR   Orphanet; 231214; Beta-thalassemia major.
DR   Orphanet; 178330; Heinz body anemia.
DR   Orphanet; 231242; Hemoglobin C - beta-thalassemia.
DR   Orphanet; 2132; Hemoglobin C disease.
DR   Orphanet; 46532; Hereditary persistence of fetal hemoglobin - beta-thalassemia.
DR   Orphanet; 251359; Sickle cell - beta-thalassemia disease.
DR   Orphanet; 232; Sickle cell anemia.
DR   PharmGKB; PA29202; -.
DR   eggNOG; NOG269316; -.
DR   GeneTree; ENSGT00650000093060; -.
DR   HOVERGEN; HBG009709; -.
DR   InParanoid; P68871; -.
DR   KO; K13823; -.
DR   OMA; DAVMNNP; -.
DR   OrthoDB; EOG4THVVF; -.
DR   Reactome; REACT_604; Hemostasis.
DR   DrugBank; DB00893; Iron Dextran.
DR   EvolutionaryTrace; P68871; -.
DR   NextBio; 12048; -.
DR   PMAP-CutDB; P68871; -.
DR   ArrayExpress; P68871; -.
DR   Bgee; P68871; -.
DR   Genevestigator; P68871; -.
DR   GermOnline; ENSG00000188170; Homo sapiens.
DR   GO; GO:0031838; C:haptoglobin-hemoglobin complex; IDA:BHF-UCL.
DR   GO; GO:0005833; C:hemoglobin complex; NAS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0030492; F:hemoglobin binding; IDA:UniProtKB.
DR   GO; GO:0019825; F:oxygen binding; IDA:UniProtKB.
DR   GO; GO:0005344; F:oxygen transporter activity; NAS:UniProtKB.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:BHF-UCL.
DR   GO; GO:0030185; P:nitric oxide transport; NAS:UniProtKB.
DR   GO; GO:0010942; P:positive regulation of cell death; IDA:BHF-UCL.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; NAS:UniProtKB.
DR   GO; GO:0051291; P:protein heterooligomerization; IDA:BHF-UCL.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR   GO; GO:0050880; P:regulation of blood vessel size; IEA:UniProtKB-KW.
DR   GO; GO:0070293; P:renal absorption; IMP:UniProtKB.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR012292; Globin_dom.
DR   InterPro; IPR002337; Haemoglobin_b.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; Globin_like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome;
KW   Congenital dyserythropoietic anemia; Direct protein sequencing;
KW   Disease mutation; Glycation; Glycoprotein; Heme;
KW   Hereditary hemolytic anemia; Hypotensive agent; Iron; Metal-binding;
KW   Oxygen transport; Phosphoprotein; Polymorphism; Pyruvate;
KW   Reference proteome; S-nitrosylation; Transport; Vasoactive.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    147       Hemoglobin subunit beta.
FT                                /FTId=PRO_0000052976.
FT   PEPTIDE      33     42       LVV-hemorphin-7.
FT                                /FTId=PRO_0000296641.
FT   METAL        64     64       Iron (heme distal ligand).
FT   METAL        93     93       Iron (heme proximal ligand).
FT   BINDING       2      2       2,3-bisphosphoglycerate; via amino
FT                                nitrogen.
FT   BINDING       3      3       2,3-bisphosphoglycerate.
FT   BINDING      83     83       2,3-bisphosphoglycerate.
FT   BINDING     144    144       2,3-bisphosphoglycerate.
FT   SITE         60     60       Not glycated.
FT   SITE         83     83       Not glycated.
FT   SITE         96     96       Not glycated.
FT   SITE        142    142       Susceptible to oxidation; associated with
FT                                variant Atlanta, variant non-spherocytic
FT                                haemolytic anemia and variant
FT                                Christchurch.
FT   SITE        145    145       Aspirin-acetylated lysine.
FT   MOD_RES       2      2       N-acetylalanine; in variant Raleigh.
FT   MOD_RES       2      2       N-pyruvate 2-iminyl-valine; in Hb A1b.
FT   MOD_RES      94     94       S-nitrosocysteine.
FT   MOD_RES     131    131       Phosphotyrosine.
FT   CARBOHYD      2      2       N-linked (Glc) (glycation); in Hb A1c.
FT   CARBOHYD      9      9       N-linked (Glc) (glycation).
FT   CARBOHYD     18     18       N-linked (Glc) (glycation).
FT   CARBOHYD     67     67       N-linked (Glc) (glycation).
FT   CARBOHYD    121    121       N-linked (Glc) (glycation).
FT   CARBOHYD    145    145       N-linked (Glc) (glycation).
FT   VARIANT       2      2       V -> A (in Raleigh; O(2) affinity down;
FT                                dbSNP:rs33949930).
FT                                /FTId=VAR_002856.
FT   VARIANT       3      3       H -> L (in Graz; dbSNP:rs35906307).
FT                                /FTId=VAR_002857.
FT   VARIANT       3      3       H -> Q (in Okayama; O(2) affinity up;
FT                                dbSNP:rs713040).
FT                                /FTId=VAR_002858.
FT   VARIANT       3      3       H -> R (in Deer Lodge; O(2) affinity up;
FT                                dbSNP:rs33983205).
FT                                /FTId=VAR_002859.
FT   VARIANT       3      3       H -> Y (in Fukuoka; dbSNP:rs35906307).
FT                                /FTId=VAR_002860.
FT   VARIANT       6      6       P -> R (in Warwickshire;
FT                                dbSNP:rs34769005).
FT                                /FTId=VAR_002861.
FT   VARIANT       7      7       E -> A (in G-Makassar).
FT                                /FTId=VAR_002862.
FT   VARIANT       7      7       E -> K (in C).
FT                                /FTId=VAR_002864.
FT   VARIANT       7      7       E -> Q (in Machida; dbSNP:rs33930165).
FT                                /FTId=VAR_002865.
FT   VARIANT       7      7       E -> V (in S; sickle cell anemia;
FT                                dbSNP:rs334).
FT                                /FTId=VAR_002863.
FT   VARIANT       8      8       E -> G (in G-San Jose; mildly unstable;
FT                                dbSNP:rs34948328).
FT                                /FTId=VAR_002866.
FT   VARIANT       8      8       E -> K (in G-Siriraj; dbSNP:rs34948328).
FT                                /FTId=VAR_002867.
FT   VARIANT       9      9       K -> E (in N-Timone; dbSNP:rs33932981).
FT                                /FTId=VAR_002868.
FT   VARIANT       9      9       K -> Q (in J-Luhe; dbSNP:rs33926764).
FT                                /FTId=VAR_002869.
FT   VARIANT       9      9       K -> T (in Rio Grande).
FT                                /FTId=VAR_002870.
FT   VARIANT      10     10       S -> C (in Porto Alegre; O(2) affinity
FT                                up; dbSNP:rs33918131).
FT                                /FTId=VAR_002871.
FT   VARIANT      11     11       A -> D (in Ankara; dbSNP:rs33947457).
FT                                /FTId=VAR_002872.
FT   VARIANT      11     11       A -> V (in Iraq-Halabja).
FT                                /FTId=VAR_025393.
FT   VARIANT      12     12       V -> D (in Windsor; O(2) affinity up;
FT                                unstable; dbSNP:rs33974228).
FT                                /FTId=VAR_002873.
FT   VARIANT      12     12       V -> I (in Hamilton).
FT                                /FTId=VAR_002874.
FT   VARIANT      14     14       A -> D (in J-Lens; dbSNP:rs35203747).
FT                                /FTId=VAR_002875.
FT   VARIANT      15     15       L -> P (in Saki; unstable).
FT                                /FTId=VAR_002876.
FT   VARIANT      15     15       L -> R (in Soegn; unstable;
FT                                dbSNP:rs33935445).
FT                                /FTId=VAR_002877.
FT   VARIANT      16     16       W -> G (in Randwick; unstable;
FT                                dbSNP:rs33946157).
FT                                /FTId=VAR_002878.
FT   VARIANT      16     16       W -> R (in Belfast; O(2) affinity up;
FT                                unstable; dbSNP:rs33946157).
FT                                /FTId=VAR_002879.
FT   VARIANT      17     17       G -> D (in J-Baltimore/J-Trinidad/J-
FT                                Ireland/J-Georgia/N-New Haven).
FT                                /FTId=VAR_002880.
FT   VARIANT      17     17       G -> R (in D-Bushman).
FT                                /FTId=VAR_002881.
FT   VARIANT      18     18       K -> E (in Nagasaki; dbSNP:rs33986703).
FT                                /FTId=VAR_002882.
FT   VARIANT      18     18       K -> N (in J-Amiens; dbSNP:rs36006214).
FT                                /FTId=VAR_002883.
FT   VARIANT      18     18       K -> Q (in Nikosia; dbSNP:rs33986703).
FT                                /FTId=VAR_002884.
FT   VARIANT      19     19       V -> M (in Baden; slightly unstable;
FT                                dbSNP:rs35802118).
FT                                /FTId=VAR_002885.
FT   VARIANT      20     20       N -> D (in Alamo; dbSNP:rs34866629).
FT                                /FTId=VAR_002886.
FT   VARIANT      20     20       N -> K (in D-Ouleh RABAH).
FT                                /FTId=VAR_002887.
FT   VARIANT      20     20       N -> S (in Malay; dbSNP:rs33972047).
FT                                /FTId=VAR_002888.
FT   VARIANT      21     21       V -> M (in Olympia; O(2) affinity up;
FT                                dbSNP:rs35890959).
FT                                /FTId=VAR_002889.
FT   VARIANT      22     22       D -> G (in Connecticut; O(2) affinity
FT                                down; dbSNP:rs33977536).
FT                                /FTId=VAR_002890.
FT   VARIANT      22     22       D -> H (in Karlskoga; dbSNP:rs33950093).
FT                                /FTId=VAR_002892.
FT   VARIANT      22     22       D -> N (in Cocody).
FT                                /FTId=VAR_002891.
FT   VARIANT      22     22       D -> Y (in Yusa).
FT                                /FTId=VAR_002893.
FT   VARIANT      23     23       E -> A (in G-Coushatta/G-Saskatoon/G-
FT                                Taegu/Hsin Chu; dbSNP:rs33936254).
FT                                /FTId=VAR_002894.
FT   VARIANT      23     23       E -> G (in G-Taipei).
FT                                /FTId=VAR_002895.
FT   VARIANT      23     23       E -> K (in E-Saskatoon; unstable).
FT                                /FTId=VAR_002896.
FT   VARIANT      23     23       E -> Q (in D-Iran).
FT                                /FTId=VAR_002897.
FT   VARIANT      23     23       E -> V (in D-Granada).
FT                                /FTId=VAR_002898.
FT   VARIANT      24     24       V -> D (in Strasbourg; O(2) affinity up).
FT                                /FTId=VAR_002899.
FT   VARIANT      24     24       V -> F (in Palmerston North; O(2)
FT                                affinity up; unstable).
FT                                /FTId=VAR_002900.
FT   VARIANT      24     24       V -> G (in Miyashiro; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002901.
FT   VARIANT      25     25       G -> D (in Moscva; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_002902.
FT   VARIANT      25     25       G -> R (in Riverdale-Bronx; O(2) affinity
FT                                up; unstable).
FT                                /FTId=VAR_002903.
FT   VARIANT      25     25       G -> V (in Savannah; unstable).
FT                                /FTId=VAR_002904.
FT   VARIANT      26     26       G -> D (in J-Auckland; unstable; O(2)
FT                                affinity down).
FT                                /FTId=VAR_002905.
FT   VARIANT      26     26       G -> R (in G-Taiwan Ami).
FT                                /FTId=VAR_002906.
FT   VARIANT      27     27       E -> K (in E).
FT                                /FTId=VAR_002907.
FT   VARIANT      27     27       E -> V (in Henri Mondor; slightly
FT                                unstable).
FT                                /FTId=VAR_002908.
FT   VARIANT      28     28       A -> D (in Volga/Drenthe; unstable).
FT                                /FTId=VAR_002909.
FT   VARIANT      28     28       A -> S (in Knossos).
FT                                /FTId=VAR_002910.
FT   VARIANT      28     28       A -> V (in Grange-blanche; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002911.
FT   VARIANT      29     29       L -> P (in Genova/Hyogo; unstable).
FT                                /FTId=VAR_002912.
FT   VARIANT      29     29       L -> Q (in St Louis).
FT                                /FTId=VAR_035236.
FT   VARIANT      30     30       G -> D (in Lufkin; unstable).
FT                                /FTId=VAR_002913.
FT   VARIANT      31     31       R -> S (in Tacoma; unstable).
FT                                /FTId=VAR_002914.
FT   VARIANT      32     32       L -> P (in Yokohama; unstable).
FT                                /FTId=VAR_002915.
FT   VARIANT      33     33       L -> R (in Castilla; unstable).
FT                                /FTId=VAR_002916.
FT   VARIANT      33     33       L -> V (in Muscat; slightly unstable).
FT                                /FTId=VAR_002917.
FT   VARIANT      35     35       V -> D (in Santander; unstable).
FT                                /FTId=VAR_025394.
FT   VARIANT      35     35       V -> F (in Pitie-Salpetriere; O(2)
FT                                affinity up).
FT                                /FTId=VAR_002918.
FT   VARIANT      35     35       V -> L (in Nantes; increased oxygen
FT                                affinity).
FT                                /FTId=VAR_025395.
FT   VARIANT      36     36       Y -> F (in Philly; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002919.
FT   VARIANT      37     37       P -> R (in Sunnybrook).
FT                                /FTId=VAR_002920.
FT   VARIANT      37     37       P -> S (in North Chicago; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002921.
FT   VARIANT      37     37       P -> T (in Linkoping/Finlandia; O(2)
FT                                affinity up).
FT                                /FTId=VAR_002922.
FT   VARIANT      38     38       W -> G (in Howick).
FT                                /FTId=VAR_002923.
FT   VARIANT      38     38       W -> R (in Rothschild; O(2) affinity
FT                                down).
FT                                /FTId=VAR_002925.
FT   VARIANT      38     38       W -> S (in Hirose; O(2) affinity up).
FT                                /FTId=VAR_002924.
FT   VARIANT      39     39       T -> N (in Hinwil; O(2) affinity up).
FT                                /FTId=VAR_002926.
FT   VARIANT      40     40       Q -> E (in Vaasa; unstable).
FT                                /FTId=VAR_002927.
FT   VARIANT      40     40       Q -> K (in Alabama).
FT                                /FTId=VAR_002928.
FT   VARIANT      40     40       Q -> R (in Tianshui).
FT                                /FTId=VAR_002929.
FT   VARIANT      42     42       F -> Y (in Mequon).
FT                                /FTId=VAR_002930.
FT   VARIANT      42     42       Missing (in Bruxelles).
FT                                /FTId=VAR_035237.
FT   VARIANT      43     43       F -> L (in Louisville; unstable).
FT                                /FTId=VAR_002931.
FT   VARIANT      43     43       F -> S (in Hammersmith).
FT                                /FTId=VAR_035239.
FT   VARIANT      43     43       Missing (in Bruxelles).
FT                                /FTId=VAR_035238.
FT   VARIANT      44     44       E -> Q (in Hoshida/Chaya).
FT                                /FTId=VAR_002932.
FT   VARIANT      45     45       S -> C (in Mississippi).
FT                                /FTId=VAR_002933.
FT   VARIANT      46     46       F -> S (in Cheverly; unstable).
FT                                /FTId=VAR_002934.
FT   VARIANT      47     47       G -> E (in K-Ibadan).
FT                                /FTId=VAR_002935.
FT   VARIANT      48     48       D -> A (in Avicenna).
FT                                /FTId=VAR_002936.
FT   VARIANT      48     48       D -> G (in Gavello).
FT                                /FTId=VAR_002937.
FT   VARIANT      48     48       D -> Y (in Maputo).
FT                                /FTId=VAR_002938.
FT   VARIANT      49     49       L -> P (in Bab-Saadoum; slightly
FT                                unstable).
FT                                /FTId=VAR_002939.
FT   VARIANT      50     50       S -> F (in Las Palmas; slightly
FT                                unstable).
FT                                /FTId=VAR_002940.
FT   VARIANT      51     51       T -> K (in Edmonton).
FT                                /FTId=VAR_002941.
FT   VARIANT      52     52       P -> R (in Willamette; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002942.
FT   VARIANT      53     53       D -> A (in Ocho Rios).
FT                                /FTId=VAR_002943.
FT   VARIANT      53     53       D -> H (in Summer Hill).
FT                                /FTId=VAR_002944.
FT   VARIANT      55     55       V -> D (in Jacksonville; O(2) affinity
FT                                up; unstable).
FT                                /FTId=VAR_002945.
FT   VARIANT      56     56       M -> K (in Matera; unstable).
FT                                /FTId=VAR_002946.
FT   VARIANT      57     57       G -> R (in Hamadan).
FT                                /FTId=VAR_002947.
FT   VARIANT      58     58       N -> K (in G-ferrara; unstable).
FT                                /FTId=VAR_002948.
FT   VARIANT      59     59       P -> R (in Dhofar/Yukuhashi).
FT                                /FTId=VAR_002949.
FT   VARIANT      60     60       K -> E (in I-High Wycombe).
FT                                /FTId=VAR_002950.
FT   VARIANT      61     61       V -> A (in Collingwood; unstable).
FT                                /FTId=VAR_002951.
FT   VARIANT      62     62       K -> E (in N-Seatlle).
FT                                /FTId=VAR_002952.
FT   VARIANT      62     62       K -> M (in Bologna; O(2) affinity down).
FT                                /FTId=VAR_002953.
FT   VARIANT      62     62       K -> N (in Hikari).
FT                                /FTId=VAR_002954.
FT   VARIANT      63     63       A -> D (in J-Europa).
FT                                /FTId=VAR_002955.
FT   VARIANT      63     63       A -> P (in Duarte; unstable).
FT                                /FTId=VAR_002956.
FT   VARIANT      64     64       H -> Y (in M-Saskatoon; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002957.
FT   VARIANT      66     66       K -> M (in J-Antakya).
FT                                /FTId=VAR_002958.
FT   VARIANT      66     66       K -> N (in J-Sicilia).
FT                                /FTId=VAR_002959.
FT   VARIANT      66     66       K -> Q (in J-Cairo).
FT                                /FTId=VAR_002960.
FT   VARIANT      67     67       K -> T (in Chico; O(2) affinity down).
FT                                /FTId=VAR_002961.
FT   VARIANT      68     68       V -> A (in Sydney; unstable).
FT                                /FTId=VAR_002962.
FT   VARIANT      68     68       V -> D (in Bristol).
FT                                /FTId=VAR_035240.
FT   VARIANT      68     68       V -> G (in non-spherocytic haemolytic
FT                                anemia; Manukau; dbSNP:rs33918343).
FT                                /FTId=VAR_040060.
FT   VARIANT      68     68       V -> M (in Alesha; unstable).
FT                                /FTId=VAR_002963.
FT   VARIANT      69     69       L -> H (in Brisbane; O(2) affinity up).
FT                                /FTId=VAR_002964.
FT   VARIANT      69     69       L -> P (in Mizuho; unstable).
FT                                /FTId=VAR_002965.
FT   VARIANT      70     70       G -> D (in Rambam).
FT                                /FTId=VAR_002966.
FT   VARIANT      70     70       G -> R (in Kenitra).
FT                                /FTId=VAR_002967.
FT   VARIANT      70     70       G -> S (in City of Hope).
FT                                /FTId=VAR_002968.
FT   VARIANT      71     71       A -> D (in Seattle; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_002969.
FT   VARIANT      72     72       F -> S (in Christchurch; unstable).
FT                                /FTId=VAR_002970.
FT   VARIANT      74     74       D -> G (in Tilburg; O(2) affinity down).
FT                                /FTId=VAR_002971.
FT   VARIANT      74     74       D -> V (in Mobile; O(2) affinity down).
FT                                /FTId=VAR_002972.
FT   VARIANT      74     74       D -> Y (in Vancouver; O(2) affinity
FT                                down).
FT                                /FTId=VAR_002973.
FT   VARIANT      75     75       G -> R (in Aalborg; unstable).
FT                                /FTId=VAR_002974.
FT   VARIANT      75     75       G -> V (in Bushwick; unstable).
FT                                /FTId=VAR_002975.
FT   VARIANT      76     76       L -> P (in Atlanta; unstable).
FT                                /FTId=VAR_002976.
FT   VARIANT      76     76       L -> R (in Pasadena; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_002977.
FT   VARIANT      77     77       A -> D (in J-Chicago).
FT                                /FTId=VAR_002978.
FT   VARIANT      78     78       H -> D (in J-Iran).
FT                                /FTId=VAR_002979.
FT   VARIANT      78     78       H -> R (in Costa Rica).
FT                                /FTId=VAR_002980.
FT   VARIANT      78     78       H -> Y (in Fukuyama).
FT                                /FTId=VAR_002981.
FT   VARIANT      79     79       L -> R (in Quin-hai).
FT                                /FTId=VAR_002982.
FT   VARIANT      80     80       D -> Y (in Tampa).
FT                                /FTId=VAR_002983.
FT   VARIANT      81     81       N -> K (in G-Szuhu/Gifu).
FT                                /FTId=VAR_002984.
FT   VARIANT      82     82       L -> H (in La Roche-sur-Yon; unstable and
FT                                O(2) affinity up).
FT                                /FTId=VAR_012663.
FT   VARIANT      82     82       L -> R (in Baylor; unstable).
FT                                /FTId=VAR_002985.
FT   VARIANT      82     82       L -> V (in dbSNP:rs11549406).
FT                                /FTId=VAR_049273.
FT   VARIANT      83     83       K -> M (in Helsinki; O(2) affinity up).
FT                                /FTId=VAR_002986.
FT   VARIANT      83     83       K -> N (in Providence).
FT                                /FTId=VAR_012664.
FT   VARIANT      84     84       G -> D (in Pyrgos).
FT                                /FTId=VAR_025396.
FT   VARIANT      84     84       G -> R (in Muskegon).
FT                                /FTId=VAR_002987.
FT   VARIANT      85     85       T -> I (in Kofu).
FT                                /FTId=VAR_002988.
FT   VARIANT      87     87       A -> D (in Olomouc; O(2) affinity up).
FT                                /FTId=VAR_002989.
FT   VARIANT      88     88       T -> I (in Quebec-Chori).
FT                                /FTId=VAR_002990.
FT   VARIANT      88     88       T -> K (in D-Ibadan).
FT                                /FTId=VAR_002991.
FT   VARIANT      88     88       T -> P (in Valletta).
FT                                /FTId=VAR_002992.
FT   VARIANT      89     89       L -> P (in Santa Ana; unstable).
FT                                /FTId=VAR_002993.
FT   VARIANT      89     89       L -> R (in Boras; unstable).
FT                                /FTId=VAR_002994.
FT   VARIANT      90     90       S -> N (in Creteil; O(2) affinity up).
FT                                /FTId=VAR_002995.
FT   VARIANT      90     90       S -> R (in Vanderbilt; O(2) affinity up).
FT                                /FTId=VAR_002996.
FT   VARIANT      91     91       E -> D (in Pierre-Benite; O(2) affinity
FT                                up).
FT                                /FTId=VAR_002997.
FT   VARIANT      91     91       E -> K (in Agenogi; O(2) affinity down).
FT                                /FTId=VAR_002998.
FT   VARIANT      92     92       L -> P (in Sabine; unstable).
FT                                /FTId=VAR_002999.
FT   VARIANT      92     92       L -> R (in Caribbean; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003000.
FT   VARIANT      93     93       H -> D (in J-Altgelds Gardens; unstable).
FT                                /FTId=VAR_003001.
FT   VARIANT      93     93       H -> N (in Isehara; unstable).
FT                                /FTId=VAR_003002.
FT   VARIANT      93     93       H -> P (in Newcastle and Duino;
FT                                associated with S-104 in Duino;
FT                                unstable).
FT                                /FTId=VAR_003003.
FT   VARIANT      93     93       H -> Q (in Istambul; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003004.
FT   VARIANT      94     94       C -> R (in Okazaki; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003005.
FT   VARIANT      95     95       D -> G (in Chandigarh).
FT                                /FTId=VAR_003006.
FT   VARIANT      95     95       D -> H (in Barcelona; O(2) affinity up).
FT                                /FTId=VAR_003007.
FT   VARIANT      95     95       D -> N (in Bunbury; O(2) affinity up).
FT                                /FTId=VAR_003008.
FT   VARIANT      96     96       K -> M (in J-Cordoba).
FT                                /FTId=VAR_003009.
FT   VARIANT      96     96       K -> N (in Detroit).
FT                                /FTId=VAR_003010.
FT   VARIANT      97     97       L -> P (in Debrousse; unstable; O(2)
FT                                affinity up).
FT                                /FTId=VAR_003011.
FT   VARIANT      97     97       L -> V (in Regina; O(2) affinity up).
FT                                /FTId=VAR_003012.
FT   VARIANT      98     98       H -> L (in Wood; O(2) affinity up).
FT                                /FTId=VAR_003013.
FT   VARIANT      98     98       H -> P (in Nagoya; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003014.
FT   VARIANT      98     98       H -> Q (in Malmoe; O(2) affinity up).
FT                                /FTId=VAR_003015.
FT   VARIANT      98     98       H -> Y (in Moriguchi).
FT                                /FTId=VAR_003016.
FT   VARIANT      99     99       V -> G (in Nottingham; unstable).
FT                                /FTId=VAR_003017.
FT   VARIANT     100    100       D -> E (in Coimbra; O(2) affinity up).
FT                                /FTId=VAR_003018.
FT   VARIANT     101    101       P -> L (in Brigham; O(2) affinity up).
FT                                /FTId=VAR_003019.
FT   VARIANT     101    101       P -> R (in New Mexico).
FT                                /FTId=VAR_003020.
FT   VARIANT     102    102       E -> D (in Potomac; O(2) affinity up).
FT                                /FTId=VAR_003021.
FT   VARIANT     102    102       E -> G (in Alberta; O(2) affinity up).
FT                                /FTId=VAR_003022.
FT   VARIANT     102    102       E -> K (in British Columbia; O(2)
FT                                affinity up).
FT                                /FTId=VAR_003023.
FT   VARIANT     102    102       E -> Q (in Rush; unstable).
FT                                /FTId=VAR_003024.
FT   VARIANT     103    103       N -> S (in Beth Israel; O(2) affinity
FT                                down; unstable).
FT                                /FTId=VAR_003025.
FT   VARIANT     103    103       N -> Y (in St Mande; O(2) affinity down).
FT                                /FTId=VAR_003026.
FT   VARIANT     104    104       F -> L (in Heathrow; O(2) affinity up).
FT                                /FTId=VAR_003027.
FT   VARIANT     105    105       R -> S (in Camperdown and Duino;
FT                                associated with P-92 in Duino; unstable).
FT                                /FTId=VAR_003028.
FT   VARIANT     105    105       R -> T (in Sherwood Forest).
FT                                /FTId=VAR_003029.
FT   VARIANT     108    108       G -> R (in Burke; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003030.
FT   VARIANT     109    109       N -> K (in Presbyterian; O(2) affinity
FT                                down; unstable).
FT                                /FTId=VAR_003031.
FT   VARIANT     110    110       V -> M (in San Diego; O(2) affinity up).
FT                                /FTId=VAR_003032.
FT   VARIANT     111    111       L -> P (in Showa-Yakushiji).
FT                                /FTId=VAR_003033.
FT   VARIANT     112    112       V -> A (in Stanmore; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003034.
FT   VARIANT     113    113       C -> F (in Canterbury).
FT                                /FTId=VAR_025397.
FT   VARIANT     113    113       C -> R (in Indianapolis).
FT                                /FTId=VAR_003035.
FT   VARIANT     113    113       C -> Y (in Yahata).
FT                                /FTId=VAR_003036.
FT   VARIANT     115    115       L -> M (in Zengcheng).
FT                                /FTId=VAR_010144.
FT   VARIANT     115    115       L -> P (in Durham-N.C./Brescia; causes
FT                                beta-thalassemia).
FT                                /FTId=VAR_010145.
FT   VARIANT     116    116       A -> D (in Hradec Kralove; unstable;
FT                                causes severe beta-thalassemia).
FT                                /FTId=VAR_003037.
FT   VARIANT     116    116       A -> P (in Madrid; unstable).
FT                                /FTId=VAR_003038.
FT   VARIANT     117    117       H -> L (in Vexin; increased oxygen
FT                                affinity).
FT                                /FTId=VAR_025398.
FT   VARIANT     117    117       H -> Q (in Hafnia).
FT                                /FTId=VAR_003039.
FT   VARIANT     118    118       H -> P (in Saitama; unstable).
FT                                /FTId=VAR_003040.
FT   VARIANT     118    118       H -> R (in P-Galveston).
FT                                /FTId=VAR_003041.
FT   VARIANT     118    118       H -> Y (in Tsukumi).
FT                                /FTId=VAR_025399.
FT   VARIANT     120    120       G -> A (in Iowa).
FT                                /FTId=VAR_003042.
FT   VARIANT     121    121       K -> E (in Hijiyama).
FT                                /FTId=VAR_003043.
FT   VARIANT     121    121       K -> I (in Jianghua).
FT                                /FTId=VAR_003044.
FT   VARIANT     121    121       K -> Q (in Takamatsu).
FT                                /FTId=VAR_003045.
FT   VARIANT     122    122       E -> A (in D-Neath).
FT                                /FTId=VAR_003046.
FT   VARIANT     122    122       E -> G (in St Francis).
FT                                /FTId=VAR_003047.
FT   VARIANT     122    122       E -> K (in O-Arab).
FT                                /FTId=VAR_003049.
FT   VARIANT     122    122       E -> Q (in D-Los Angeles/D-Punjab/D-
FT                                Portugal/D-Chicago/D-Oak Ridge).
FT                                /FTId=VAR_003048.
FT   VARIANT     122    122       E -> V (in D-Camperdown/Beograd).
FT                                /FTId=VAR_003050.
FT   VARIANT     124    124       T -> I (in Villejuif; asymptomatic
FT                                variant).
FT                                /FTId=VAR_003051.
FT   VARIANT     125    125       P -> Q (in Ty Gard; O(2) affinity up).
FT                                /FTId=VAR_003053.
FT   VARIANT     125    125       P -> R (in Khartoum; unstable).
FT                                /FTId=VAR_003052.
FT   VARIANT     125    125       P -> S (in Tunis).
FT                                /FTId=VAR_003054.
FT   VARIANT     127    127       V -> A (in Beirut).
FT                                /FTId=VAR_003055.
FT   VARIANT     127    127       V -> E (in Hofu; unstable).
FT                                /FTId=VAR_003057.
FT   VARIANT     127    127       V -> G (in Dhonburi/Neapolis; unstable;
FT                                beta-thalassemia).
FT                                /FTId=VAR_003056.
FT   VARIANT     128    128       Q -> E (in Complutense).
FT                                /FTId=VAR_003058.
FT   VARIANT     128    128       Q -> K (in Brest; unstable).
FT                                /FTId=VAR_003059.
FT   VARIANT     129    129       A -> D (in J-Guantanamo; unstable).
FT                                /FTId=VAR_003060.
FT   VARIANT     130    130       A -> P (in Crete; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003061.
FT   VARIANT     130    130       A -> V (in La Desirade; O(2) affinity
FT                                down; unstable).
FT                                /FTId=VAR_003062.
FT   VARIANT     131    131       Y -> D (in Wien; unstable).
FT                                /FTId=VAR_003063.
FT   VARIANT     131    131       Y -> S (in Nevers).
FT                                /FTId=VAR_003064.
FT   VARIANT     132    132       Q -> E (in Camden/Tokuchi/Motown).
FT                                /FTId=VAR_003065.
FT   VARIANT     132    132       Q -> K (in Shelby/Leslie/Deaconess;
FT                                unstable).
FT                                /FTId=VAR_003066.
FT   VARIANT     132    132       Q -> P (in Shangai; unstable).
FT                                /FTId=VAR_003067.
FT   VARIANT     132    132       Q -> R (in Sarrebourg; unstable).
FT                                /FTId=VAR_003068.
FT   VARIANT     133    133       K -> N (in Yamagata; O(2) affinity down).
FT                                /FTId=VAR_003069.
FT   VARIANT     133    133       K -> Q (in K-Woolwich).
FT                                /FTId=VAR_003070.
FT   VARIANT     134    134       V -> L (in Extredemura).
FT                                /FTId=VAR_003071.
FT   VARIANT     135    135       V -> E (in North Shore-Caracas;
FT                                unstable).
FT                                /FTId=VAR_003072.
FT   VARIANT     136    136       A -> E (in Beckman; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003073.
FT   VARIANT     136    136       A -> P (in Altdorf; O(2) affinity up;
FT                                unstable).
FT                                /FTId=VAR_003074.
FT   VARIANT     137    137       G -> D (in Hope; O(2) affinity down;
FT                                unstable).
FT                                /FTId=VAR_003075.
FT   VARIANT     139    139       A -> P (in Brockton; unstable).
FT                                /FTId=VAR_003076.
FT   VARIANT     140    140       N -> D (in Geelong; unstable).
FT                                /FTId=VAR_003077.
FT   VARIANT     140    140       N -> K (in Hinsdale; O(2) affinity down).
FT                                /FTId=VAR_003078.
FT   VARIANT     140    140       N -> S (in S-Wake; associated with V-6).
FT                                /FTId=VAR_025335.
FT   VARIANT     140    140       N -> Y (in Aurora; O(2) affinity up).
FT                                /FTId=VAR_003079.
FT   VARIANT     141    141       A -> D (in Himeji; unstable; O(2)
FT                                affinity down).
FT                                /FTId=VAR_003080.
FT   VARIANT     141    141       A -> T (in St Jacques: O(2) affinity up).
FT                                /FTId=VAR_003081.
FT   VARIANT     141    141       A -> V (in Puttelange; polycythemia; O(2)
FT                                affinity up).
FT                                /FTId=VAR_003082.
FT   VARIANT     142    142       L -> R (in Olmsted; unstable).
FT                                /FTId=VAR_003083.
FT   VARIANT     143    143       A -> D (in Ohio; O(2) affinity up).
FT                                /FTId=VAR_003084.
FT   VARIANT     144    144       H -> D (in Rancho Mirage).
FT                                /FTId=VAR_003085.
FT   VARIANT     144    144       H -> P (in Syracuse; O(2) affinity up).
FT                                /FTId=VAR_003087.
FT   VARIANT     144    144       H -> Q (in Little Rock; O(2) affinity
FT                                up).
FT                                /FTId=VAR_003086.
FT   VARIANT     144    144       H -> R (in Abruzzo; O(2) affinity up).
FT                                /FTId=VAR_003088.
FT   VARIANT     145    145       K -> E (in Mito; O(2) affinity up).
FT                                /FTId=VAR_003089.
FT   VARIANT     146    146       Y -> C (in Rainier; O(2) affinity up).
FT                                /FTId=VAR_003090.
FT   VARIANT     146    146       Y -> H (in Bethesda; O(2) affinity up).
FT                                /FTId=VAR_003091.
FT   VARIANT     147    147       H -> D (in Hiroshima; O(2) affinity up).
FT                                /FTId=VAR_003092.
FT   VARIANT     147    147       H -> L (in Cowtown; O(2) affinity up).
FT                                /FTId=VAR_003093.
FT   VARIANT     147    147       H -> P (in York; O(2) affinity up).
FT                                /FTId=VAR_003094.
FT   VARIANT     147    147       H -> Q (in Kodaira; O(2) affinity up).
FT                                /FTId=VAR_003095.
FT   CONFLICT     26     26       Missing (in Ref. 15; ACD39349).
FT   CONFLICT     42     42       F -> L (in Ref. 13; AAR96398).
FT   HELIX         6     16
FT   TURN         21     23
FT   HELIX        24     35
FT   HELIX        37     42
FT   HELIX        44     46
FT   HELIX        52     57
FT   HELIX        59     77
FT   TURN         78     80
FT   HELIX        82     94
FT   TURN         95     97
FT   HELIX       102    119
FT   HELIX       120    122
FT   HELIX       125    142
FT   HELIX       144    146
SQ   SEQUENCE   147 AA;  15998 MW;  A31F6D621C6556A1 CRC64;
     MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
     VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
     KEFTPPVQAA YQKVVAGVAN ALAHKYH
//
ID   HBB_PANPA               Reviewed;         147 AA.
AC   P68872; P02023; Q13852; Q14481; Q14510; Q9BX96; Q9UCP8; Q9UCP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 44.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9597;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-147.
RX   MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0;
RA   Goodman M., Braunitzer G., Stangl A., Schrank B.;
RT   "Evidence on human origins from haemoglobins of African apes.";
RL   Nature 303:546-548(1983).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family.
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DR   PIR; D93303; HBCZP.
DR   ProteinModelPortal; P68872; -.
DR   SMR; P68872; 2-147.
DR   PRIDE; P68872; -.
DR   HOVERGEN; HBG009709; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR012292; Globin_dom.
DR   InterPro; IPR002337; Haemoglobin_b.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; Globin_like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    147       Hemoglobin subunit beta.
FT                                /FTId=PRO_0000053056.
FT   METAL        64     64       Iron (heme distal ligand).
FT   METAL        93     93       Iron (heme proximal ligand).
SQ   SEQUENCE   147 AA;  15998 MW;  A31F6D621C6556A1 CRC64;
     MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
     VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
     KEFTPPVQAA YQKVVAGVAN ALAHKYH
//
ID   HBB_PANTR               Reviewed;         147 AA.
AC   P68873; P02023; Q13852; Q14481; Q14510; Q28799; Q9BX96; Q9UCP8;
AC   Q9UCP9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   13-JUN-2012, entry version 67.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RX   MEDLINE=85210896; PubMed=3999143; DOI=10.1016/0022-2836(85)90024-5;
RA   Savatier P., Trabuchet G., Faure C., Chebloune Y., Gouy M.,
RA   Verdier G., Nigon V.M.;
RT   "Evolution of the primate beta-globin gene region. High rate of
RT   variation in CpG dinucleotides and in short repeated sequences between
RT   man and chimpanzee.";
RL   J. Mol. Biol. 182:21-29(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-147.
RX   MEDLINE=66071496; PubMed=5855051;
RA   Rifkin D.B., Konigsberg W.;
RT   "The characterization of the tryptic peptides from the hemoglobin of
RT   the chimpanzee (Pan troglodytes).";
RL   Biochim. Biophys. Acta 104:457-461(1965).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in
CC       adult hemoglobin A (HbA).
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26204.1; Type=Erroneous gene model prediction;
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DR   EMBL; X02345; CAA26204.1; ALT_SEQ; Genomic_DNA.
DR   PIR; B93303; HBCZ.
DR   RefSeq; XP_003312929.1; XM_003312881.1.
DR   RefSeq; XP_508242.1; XM_508242.3.
DR   ProteinModelPortal; P68873; -.
DR   SMR; P68873; 2-147.
DR   STRING; P68873; -.
DR   PRIDE; P68873; -.
DR   Ensembl; ENSPTRT00000006177; ENSPTRP00000005700; ENSPTRG00000040047.
DR   GeneID; 450978; -.
DR   KEGG; ptr:450978; -.
DR   CTD; 3043; -.
DR   eggNOG; NOG269316; -.
DR   GeneTree; ENSGT00650000093060; -.
DR   HOVERGEN; HBG009709; -.
DR   KO; K13823; -.
DR   OMA; DAVMNNP; -.
DR   NextBio; 20833659; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR012292; Globin_dom.
DR   InterPro; IPR002337; Haemoglobin_b.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; Globin_like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    147       Hemoglobin subunit beta.
FT                                /FTId=PRO_0000053060.
FT   METAL        64     64       Iron (heme distal ligand).
FT   METAL        93     93       Iron (heme proximal ligand).
SQ   SEQUENCE   147 AA;  15998 MW;  A31F6D621C6556A1 CRC64;
     MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK
     VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG
     KEFTPPVQAA YQKVVAGVAN ALAHKYH
//
ID   HD_TAKRU                Reviewed;        3148 AA.
AC   P51112;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 64.
DE   RecName: Full=Huntingtin;
DE   AltName: Full=Huntington disease protein homolog;
DE            Short=HD protein homolog;
GN   Name=htt; Synonyms=hd;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95375788; PubMed=7647794; DOI=10.1038/ng0595-67;
RA   Baxendale S., Abdulla S., Elgar G., Buck D., Berks M., Micklem G.,
RA   Durbin R., Bates G., Brenner S., Beck S., Lehrach H.;
RT   "Comparative sequence analysis of the human and pufferfish
RT   Huntington's disease genes.";
RL   Nat. Genet. 10:67-76(1995).
CC   -!- FUNCTION: May play a role in microtubule-mediated transport or
CC       vesicle function.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- POLYMORPHISM: The poly-Gln region (four residues) does not appear
CC       to be polymorphic, explaining the absence of a HD-like disorder.
CC   -!- SIMILARITY: Belongs to the huntingtin family.
CC   -!- SIMILARITY: Contains 10 HEAT repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; X82939; CAA58112.1; -; Genomic_DNA.
DR   ProteinModelPortal; P51112; -.
DR   STRING; P51112; -.
DR   PRIDE; P51112; -.
DR   eggNOG; NOG82191; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:RefGenome.
DR   GO; GO:0005634; C:nucleus; ISS:RefGenome.
DR   GO; GO:0008134; F:transcription factor binding; ISS:RefGenome.
DR   GO; GO:0048513; P:organ development; ISS:RefGenome.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR000091; Huntingtin.
DR   InterPro; IPR024613; Huntingtin_middle-repeat.
DR   PANTHER; PTHR10170; Huntingtin; 1.
DR   Pfam; PF12372; DUF3652; 1.
DR   PRINTS; PR00375; HUNTINGTIN.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Nucleus; Reference proteome; Repeat.
FT   CHAIN         1   3148       Huntingtin.
FT                                /FTId=PRO_0000083941.
FT   REPEAT      149    186       HEAT 1.
FT   REPEAT      191    228       HEAT 2.
FT   REPEAT      760    797       HEAT 3.
FT   REPEAT      861    898       HEAT 4.
FT   REPEAT     1419   1456       HEAT 5.
FT   MOTIF      2398   2407       Nuclear export signal (By similarity).
FT   COMPBIAS     18     21       Poly-Gln.
FT   COMPBIAS    679    682       Poly-Ala.
FT   COMPBIAS   1104   1108       Poly-Ser.
SQ   SEQUENCE   3148 AA;  348937 MW;  D9358676B0345243 CRC64;
     MATMEKLMKA FESLKSFQQQ QGPPTAEEIV QRQKKEQATT KKDRVSHCLT ICENIVAQSL
     RTSPEFQKLL GIAMEMFLLC SDDSESDVRM VADECLNRII KALMDSNLPR LQLELYKEIK
     KNGASRSLRA ALWRFAELAH LIRPQKCRPY LVNLLPCLTR ITKRQEETIQ ETLAAAMPKI
     MAALGHFAND GEIKMLLKSF VANLKSSSPT IRRTAASSAV SVCQHSRRTS YFYTWLLNVL
     LGLLVPVDEE HHSHLILGVL LTLRYLMPLL QQQVNTISLK GSFGVMQKEA DVQPAPEQLL
     QVYELTLHYT QHWDHNVVTA ALELLQQTLR TPPPELLHVL ITAGSIQHAS VFRQDIESRA
     RSGSILELIA GGGSTCSPLL HRKHRGKMLS GEEDALEDDP EKTDVTTGYF TAVGADNSSA
     AQVDIITQQP RSSQHTIQPG DSVDLSASSE QGGRGGGASA SDTPESPNDE EDMLSRSSSC
     GANITPETVE DATPENPAQE GRPVGGSGAY DHSLPPSDSS QTTTEGPDSA VTPSDVAELV
     LDGSESQYSG MQIGTLQDEE DEGTATSSQE DPPDPFLRSA LALSKPHLFE SRGHNRQGSD
     SSVDRFIPKD EPPEPEPDNK MSRIKGAIGH YTDRGAEPVV HCVRLLSASF LLTGQKNGLT
     PDRDVRVSVK ALAVSCVGAA AALHPEAFFN SLYLEPLDGL RAEEQQYISD VLGFIDHGDP
     QIRGATAILC AAIIQAALSK MRYNIHSWLA SVQSKTGNPL SLVDLVPLLQ KALKDESSVT
     CKMACSAVRH CIMSLCGSTL SELGLRLVVD LFALKDSSYW LVRTELLETL AEMDFRLVNF
     LERKSEALHK GEHHYTGRLR LQERVLNDVV IQLLGDDDPR VRHVAASAVS RLVSRLFFDC
     DQGQADPVVA IARDQSSVYL QLLMHETQPP SQLTVSTITR TYRGFNLSNN VADVTVENNL
     SRVVTAVSHA FTSSTSRALT FGCCEALCLL AVHFPICTWT TGWHCGHISS QSSFSSRVGR
     SRGRTLSVSQ SGSTPASSTT SSAVDPERRT LTVGTANMVL SLLSSAWFPL DLSAHQDALL
     LCGNLLAAVA PKCLRNPWAG EDDSSSSSTN TSGGTHKMEE PWAALSDRAF VAMVEQLFSH
     LLKVLNICAH VLDDTPPGPP VKATLPSLTN TPSLSPIRRK GKDKDAVDSS SAPLSPKKGN
     EANTGRPTES TGSTAVHKST TLGSFYHLPP YLKLYDVLKA THANFKVMLD LHSNQEKFGS
     FLRAALDVLS QLLELATLND INKCVEEILG YLKSCFSREP TMATVCVQQL LKTLFGTNLA
     SQYEGFLSGP SRSQGKALRL GSSSLRPGLY HYCFMAPYTH FTQALADASL RNMVQAEHEQ
     DTSGWFDVMQ KTSNQLRSNI ANAARHRGDK NAIHNHIRLF EPLVIKALKQ YTTSTSVALQ
     RQVLDLLAQL VQLRVNYCLL DSDQVFIGFV LKQFEYIEVG QFRDSEAIIP NIFFFLVLLS
     YERYHSKQII SIPKIIQLCD GIMASGRKAV THAIPALQPI VHDLFVLRGS NKADAGKELE
     TQKEVVVSML LRLVQYHQVL EMFILVLQQC HKENEDKWKR LSRQIADVIL PMIAKQQMHL
     DSPEALGVLN TLFETVAPSS LRPVDMLLKS MFTTPVTMAS VATVQLWVSG ILAVLRVLVS
     QSTEDIVLSR IHELSLSPHL LSCHTIKRLQ QPNLSPSDQP AGDGQQNQEP NGEAQKSLPE
     ETFARFLIQL VGVLLDDISS RHVKVDITEQ QHTFYCQQLG TLLMCLIHVF KSGMFRRITV
     AASRLLKGES GSGHSGIEFY PLEGLNSMVH CLITTHPSLV LLWCQVLLII DYTNYSWWTE
     VHQTPKGHSL SCTKLLSPHS SGEGEEKPET RLAMINREIV RRGALILFCD YVCQNLHDSE
     HLTWLIVNHV RDLIDLSHEP PVQDFISAVH RNSAASGLFI QAIQSRCDNL NSPTMLKKTL
     QCLEGIHLSQ SGSLLMLYVD KLLSTPFRVL ARMVDTLACR RVEMLLAETL QNSVAQLPLE
     ELHRIQEYLQ TSGLAQRHQR FYSLLDRFRA TVSDTSSPST PVTSHPLDGD PPPAPELVIA
     DKEWYVALVK SQCCLHGDVS LLETTELLTK LPPADLLSVM SCKEFNLSLL CPCLSLGVQR
     LLRGQGSLLL ETALQVTLEQ LAGATGLLPV PHHSFIPTSH PQSHWKQLAE VYGDPGFYSR
     VLSLCRALSQ YLLTVKQLPS SLRIPSDKEH LITTFTCAAT EVVVWHLLQD QLPLSVDLQW
     ALSCLCLALQ QPCVWNKLST PEYNTHTCSL IYCLHHIILA VAVSPGDQLL HPERKKTKAL
     RHSDDEDQVD SVHDNHTLEW QACEIMAELV EGLQSVLSLG HHRNTAFPAF LTPTLRNIII
     SLSRLPLVNS HTRVPPLVWK LGWSPQPGGE FGTTLPEIPV DFLQEKDVFR EFLYRINTLG
     WSNRTQFEET WATLLGVLVT QPITMDQEEE TQQEEDLERT QLNVLAVQAI TSLVLSAMTL
     PTAGNPAVSC LEQQPRNKSL KALETRFGRK LAVIRGEVER EIQALVSKRD NVHTYHPYHA
     WDPVPSLSAA SPGTLISHEK LLLQINTERE LGNMDYKLGQ VSIHSVWLGN NITPLREEEW
     GEDEDDEADP PAPTSPPLSP INSRKHRAGV DIHSCSQFLL ELYSQWVIPG SPSNRKTPTI
     LISEVVRSLL AVSDLFTERN QFDMMFSTLM ELQKLHPPED EILNQYLVPA ICKAAAVLGM
     DKAIAEPVCR LLETTLRSTH LPSRMGALHG VLYVLECDLL DDTAKQLIPT VSEYLLSNLR
     AIAHCVNLHN QQHVLVMCAV AFYMMENYPL DVGTEFMAGI IQLCGVMVSA SEDSTPSIIY
     HCVLRGLERL LLSEQLSRVD GEALVKLSVD RVNMPSPHRA MAALGLMLTC MYTGKEKASP
     AARSAHSDPQ VPDSESIIVA MERVSVLFDR IRKGLPSEAR VVARILPQFL DDFFPPQDIM
     NKVIGEFLSN QQPYPQFMAT VVYKVFQTLH ATGQSSMVRD WVLLSLSNFT QRTPVAMAMW
     SLSCFFVSAS TSQWISALLP HVISRMGSSD VVDVNLFCLV AMDFYRHQID EELDRRAFQS
     VFETVASPGS PYFQLLACLQ SIHQDKSL
//
ID   HIRA_TAKRU              Reviewed;        1025 AA.
AC   O42611;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-MAY-2012, entry version 79.
DE   RecName: Full=Protein HIRA;
DE   AltName: Full=TUP1-like enhancer of split protein 1;
GN   Name=hira; Synonyms=tuple1;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=98201624; PubMed=9524281; DOI=10.1016/S0378-1119(98)00010-9;
RA   Llevadot R., Estivill X., Scambler P., Pritchard M.;
RT   "Isolation and genomic characterization of the TUPLE1/HIRA gene of the
RT   pufferfish Fugu rubripes.";
RL   Gene 208:279-283(1998).
CC   -!- FUNCTION: Required for replication-independent chromatin assembly
CC       and for the periodic repression of histone gene transcription
CC       during the cell cycle (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat HIR1 family.
CC   -!- SIMILARITY: Contains 9 WD repeats.
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DR   EMBL; U94325; AAC60370.1; -; Genomic_DNA.
DR   EMBL; U94324; AAC60369.1; -; mRNA.
DR   RefSeq; NP_001027852.1; NM_001032680.1.
DR   UniGene; Tru.1844; -.
DR   ProteinModelPortal; O42611; -.
DR   STRING; O42611; -.
DR   GeneID; 446054; -.
DR   CTD; 7290; -.
DR   eggNOG; COG2319; -.
DR   InParanoid; O42611; -.
DR   OrthoDB; EOG42NHZN; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   InterPro; IPR011494; Hira.
DR   InterPro; IPR019015; HIRA_B_motif.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   Pfam; PF07569; Hira; 1.
DR   Pfam; PF09453; HIRA_B; 1.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Complete proteome; Nucleus; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; WD repeat.
FT   CHAIN         1   1025       Protein HIRA.
FT                                /FTId=PRO_0000051021.
FT   REPEAT       11     53       WD 1.
FT   REPEAT       68    107       WD 2.
FT   REPEAT      129    168       WD 3.
FT   REPEAT      172    211       WD 4.
FT   REPEAT      220    263       WD 5.
FT   REPEAT      266    322       WD 6.
FT   REPEAT      326    367       WD 7.
FT   REPEAT      737    778       WD 8.
FT   REPEAT      779    817       WD 9.
SQ   SEQUENCE   1025 AA;  111857 MW;  A4212152D75B6A37 CRC64;
     MKLLKPSWVS HNGKPIFSVD IHPDGTKFAT GGQGEDSGKV MIWNMAPVLK EEDEKNENVP
     KMLCQMDNHL ACVNCVRWSN NGLYLASGGD DKLVMVWKRA ALIGPSTVFG SSNKLANVEQ
     WRCVTILRNH TGDVMDVSWS PHDVWLASCS VDNTIVIWNA RKFPEMVTCL RGHTGLVKGL
     TWDPVGKYIA SQADDHSLRV WRTVDWQMEA NITKPFSECG GTTHVLRLSW SPDGQYLVSA
     HAMNNSGPTA QIVERDGWRT NMDFVGHRKA VTVVKFNPKI FKKKQKNGGS PKPSCPYCCC
     AVGSKDRSLS VWLTSLKRPL VVIHDLFDKS IMDISWTLTG LGMLVCSMDG TVAYLDFSLD
     ELGDPLSEEE KNSIHQNIYG KSLAITNTEP QLSTTIIENP EMLKYQQERR NSTQANSGPG
     ATGSESATPK LNSVMNGESL EDIRKNLLKK QVETRTPDGR RRITPLCIAQ LDTGDFSPAL
     FNSAPILPSG SSMSNQLTSQ LSSDSSPGQA PPLGLRPSQD PMLISPPPSS AAKVLEDNKD
     GVKSCLLLTS ASKIEPMKAL DSRFTERSKA TPGATAAIAS STGLTPSERP KESTPMQKDV
     KSKEDTSSDS EDKMATINKN LAFNKRKPEL LMDGAEVVEK RKKGRPRKDK MAASIAQPLT
     QTTSPAEREP SRAAAAGAGA AAPTAAAALK LPTPSIKKAF TLQVSMDPSV VLEVENEVSV
     VAGSRLSQLR CSRDGRDWNT LLPSSVLTAA GSSDVVAVAS QDRMLSVFSS CGRRLLPAIQ
     LATPASALHC SAHFVMVLTS GATLSVWDVH KQKALVKNES LLTILSGAAV TVSQSMLTQQ
     GVPVVGLSNG KSYCFSLSLE TWTLIADTAD SLVQCADFRN CLPNQDAPMS SGPLAAMQGR
     NFNAGRLASR LSSTPHHLQQ SMTLAFLENQ LASALTLQSA QEYRYWLLIY ARFLVNEGSE
     YRLRELCKEL LGPVHKSATT SWEPTTLGLR KRDLLREVLP VVGENLRFQR LFTEYQDQLE
     LLRNK
//
ID   IFNA2_HUMAN             Reviewed;         188 AA.
AC   P01563; P01564; Q14606; Q96KI6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   16-MAY-2012, entry version 128.
DE   RecName: Full=Interferon alpha-2;
DE            Short=IFN-alpha-2;
DE   AltName: Full=Interferon alpha-A;
DE            Short=LeIF A;
DE   Flags: Precursor;
GN   Name=IFNA2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=81052322; PubMed=6159538; DOI=10.1038/287411a0;
RA   Goeddel D.V., Yelverton E., Ullrich A., Heyneker H.L., Miozzari G.,
RA   Holmes W., Seeburg P.H., Dull T.J., May L., Stebbing N., Crea R.,
RA   Maeda S., McCandliss R., Sloma A., Tabor J.M., Gross M.,
RA   Familletti P.C., Pestka S.;
RT   "Human leukocyte interferon produced by E. coli is biologically
RT   active.";
RL   Nature 287:411-416(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=81148795; PubMed=6163083; DOI=10.1038/290020a0;
RA   Goeddel D.V., Leung D.W., Dull T.J., Gross M., Lawn R.M.,
RA   McCandliss R., Seeburg P.H., Ullrich A., Yelverton E., Gray P.W.;
RT   "The structure of eight distinct cloned human leukocyte interferon
RT   cDNAs.";
RL   Nature 290:20-26(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=82060261; PubMed=6170983; DOI=10.1073/pnas.78.9.5435;
RA   Lawn R.M., Gross M., Houck C.M., Franke A.E., Gray P.V., Goeddel D.V.;
RT   "DNA sequence of a major human leukocyte interferon gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:5435-5439(1981).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Bone marrow tumor;
RX   MEDLINE=86069501; PubMed=3906813;
RA   Oliver G., Balbas P., Valle F., Soberon X., Bolivar F.;
RT   "Cloning of human leukocyte interferon cDNA and a strategy for its
RT   production in E. coli.";
RL   Rev. Latinoam. Microbiol. 27:141-150(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Placenta;
RX   MEDLINE=98357449; PubMed=9694076;
RA   Austruy E., Bagnis C., Carbuccia N., Maroc C., Birg F., Dubreuil P.,
RA   Mannoni P., Chabannon C.;
RT   "A defective retroviral vector encoding human interferon alpha 2 can
RT   transduce human leukemic cell lines.";
RL   Cancer Gene Ther. 5:247-256(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 7-188.
RX   MEDLINE=81015442; PubMed=6158094; DOI=10.1126/science.6158094;
RA   Streuli M., Nagata S., Weissmann C.;
RT   "At least three human type alpha interferons: structure of alpha 2.";
RL   Science 209:1343-1347(1980).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-188.
RX   MEDLINE=83299241; PubMed=6310510; DOI=10.1093/nar/11.16.5661;
RA   Weber H., Weissmann C.;
RT   "Formation of genes coding for hybrid proteins by recombination
RT   between related, cloned genes in E. coli.";
RL   Nucleic Acids Res. 11:5661-5669(1983).
RN   [8]
RP   PROTEIN SEQUENCE OF 24-112 AND 136-188.
RX   MEDLINE=81052321; PubMed=6159537; DOI=10.1038/287408a0;
RA   Allen G., Fantes K.H.;
RT   "A family of structural genes for human lymphoblastoid (leukocyte-
RT   type) interferon.";
RL   Nature 287:408-411(1980).
RN   [9]
RP   PROTEIN SEQUENCE OF 24-58.
RX   MEDLINE=98087498; PubMed=9425112;
RA   Nyman T.A., Toeloe H., Parkkinen J., Kalkkinen N.;
RT   "Identification of nine interferon-alpha subtypes produced by Sendai
RT   virus-induced human peripheral blood leucocytes.";
RL   Biochem. J. 329:295-302(1998).
RN   [10]
RP   DISULFIDE BONDS.
RX   MEDLINE=81123083; PubMed=6162107; DOI=10.1038/289606a0;
RA   Wetzel R.;
RT   "Assignment of the disulphide bonds of leukocyte interferon.";
RL   Nature 289:606-607(1981).
RN   [11]
RP   GLYCOSYLATION AT THR-129, AND VARIANTS ALPHA-2B AND ALPHA-2C.
RX   MEDLINE=91264809; PubMed=2049076;
RA   Adolf G.R., Kalsner I., Ahorn H., Maurer-Fogy I., Cantell K.;
RT   "Natural human interferon-alpha 2 is O-glycosylated.";
RL   Biochem. J. 276:511-518(1991).
RN   [12]
RP   POLYMORPHISM.
RX   MEDLINE=95353982; PubMed=7627809; DOI=10.1089/jir.1995.15.341;
RA   Lee N., Ni D., Brissette R., Chou M., Hussain M., Gill D.S.,
RA   Liao M.-J., Testa D.;
RT   "Interferon-alpha 2 variants in the human genome.";
RL   J. Interferon Cytokine Res. 15:341-349(1995).
RN   [13]
RP   3D-STRUCTURE MODELING.
RX   MEDLINE=94052087; PubMed=8234245; DOI=10.1002/prot.340170109;
RA   Murgolo N.J., Windsor W.T., Hruza A., Reichert P., Tsarbopoulos A.,
RA   Baldwin S., Huang E., Pramanik B., Ealick S., Trotta P.P.;
RT   "A homology model of human interferon alpha-2.";
RL   Proteins 17:62-74(1993).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RX   MEDLINE=97148339; PubMed=8994971; DOI=10.1016/S0969-2126(96)00152-9;
RA   Radhakrishnan R., Walter L.J., Hruza A., Reichert P., Trotta P.P.,
RA   Nagabhushan T.L., Walter M.R.;
RT   "Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray
RT   crystallography.";
RL   Structure 4:1453-1463(1996).
RN   [15]
RP   STRUCTURE BY NMR.
RX   MEDLINE=98118493; PubMed=9417943; DOI=10.1006/jmbi.1997.1396;
RA   Klaus W., Gsell B., Labhardt A.M., Wipf B., Senn H.;
RT   "The three-dimensional high resolution structure of human interferon
RT   alpha-2a determined by heteronuclear NMR spectroscopy in solution.";
RL   J. Mol. Biol. 274:661-675(1997).
RN   [16]
RP   STRUCTURE BY NMR OF 24-188 IN COMPLEX WITH IFNAR2, SUBUNIT, AND
RP   DISULFIDE BONDS.
RX   PubMed=17001036; DOI=10.1110/ps.062283006;
RA   Quadt-Akabayov S.R., Chill J.H., Levy R., Kessler N., Anglister J.;
RT   "Determination of the human type I interferon receptor binding site on
RT   human interferon-alpha2 by cross saturation and an NMR-based model of
RT   the complex.";
RL   Protein Sci. 15:2656-2668(2006).
RN   [17]
RP   STRUCTURE BY NMR OF 24-188 IN COMPLEX WITH IFNAR2, SUBUNIT, AND
RP   DISULFIDE BONDS.
RX   PubMed=20496919; DOI=10.1021/bi100041f;
RA   Nudelman I., Akabayov S.R., Schnur E., Biron Z., Levy R., Xu Y.,
RA   Yang D., Anglister J.;
RT   "Intermolecular interactions in a 44 kDa interferon-receptor complex
RT   detected by asymmetric reverse-protonation and two-dimensional
RT   NOESY.";
RL   Biochemistry 49:5117-5133(2010).
RN   [18]
RP   VARIANT [LARGE SCALE ANALYSIS] LEU-177.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral
CC       activities.
CC   -!- SUBUNIT: Interacts with IFNAR2.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- POLYMORPHISM: Three forms exist; alpha-2a (shown here), alpha-2b
CC       and alpha-2c.
CC   -!- PHARMACEUTICAL: Available under the names Roferon-A (Roche) or
CC       Intron-A (Schering-Plough). Used as an anticancer drug for its
CC       antiproliferative activity.
CC   -!- SIMILARITY: Belongs to the alpha/beta interferon family.
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DR   EMBL; J00207; AAB59402.1; -; Genomic_DNA.
DR   EMBL; V00544; CAA23805.1; -; mRNA.
DR   EMBL; V00548; CAA23809.1; -; mRNA.
DR   EMBL; V00549; CAA23810.1; -; mRNA.
DR   EMBL; Y11834; CAA72532.1; -; Genomic_DNA.
DR   EMBL; M54886; AAA59181.1; -; mRNA.
DR   EMBL; M29883; AAA52715.1; -; Genomic_DNA.
DR   IPI; IPI00307184; -.
DR   PIR; A93234; IVHUA2.
DR   PIR; I78570; I78570.
DR   RefSeq; NP_000596.2; NM_000605.3.
DR   UniGene; Hs.211575; -.
DR   PDB; 1ITF; NMR; -; A=24-188.
DR   PDB; 1RH2; X-ray; 2.90 A; A/B/C/D/E/F=24-188.
DR   PDB; 2HIE; Model; -; A=24-188.
DR   PDB; 2HYM; NMR; -; B=24-188.
DR   PDB; 2KZ1; NMR; -; A=24-188.
DR   PDB; 2LAG; NMR; -; A=24-188.
DR   PDB; 3S9D; X-ray; 2.00 A; A/C=24-188.
DR   PDB; 3SE3; X-ray; 4.00 A; B=24-188.
DR   PDBsum; 1ITF; -.
DR   PDBsum; 1RH2; -.
DR   PDBsum; 2HIE; -.
DR   PDBsum; 2HYM; -.
DR   PDBsum; 2KZ1; -.
DR   PDBsum; 2LAG; -.
DR   PDBsum; 3S9D; -.
DR   PDBsum; 3SE3; -.
DR   ProteinModelPortal; P01563; -.
DR   SMR; P01563; 24-188.
DR   DIP; DIP-3784N; -.
DR   DIP; DIP-481N; -.
DR   IntAct; P01563; 1.
DR   STRING; P01563; -.
DR   Allergome; 9876; Hom s IFN alpha.
DR   GlycoSuiteDB; P01563; -.
DR   DMDM; 124449; -.
DR   PRIDE; P01563; -.
DR   DNASU; 3440; -.
DR   Ensembl; ENST00000380206; ENSP00000369554; ENSG00000188379.
DR   GeneID; 3440; -.
DR   KEGG; hsa:3440; -.
DR   CTD; 3440; -.
DR   GeneCards; GC09M021374; -.
DR   H-InvDB; HIX0034810; -.
DR   HGNC; HGNC:5423; IFNA2.
DR   MIM; 147562; gene.
DR   neXtProt; NX_P01563; -.
DR   PharmGKB; PA29662; -.
DR   eggNOG; NOG246451; -.
DR   HOGENOM; HOG000230500; -.
DR   HOVERGEN; HBG052086; -.
DR   InParanoid; P01563; -.
DR   KO; K05414; -.
DR   OrthoDB; EOG4KH2W5; -.
DR   Pathway_Interaction_DB; cd8tcrdownstreampathway; Downstream signaling in naive CD8+ T cells.
DR   Reactome; REACT_604; Hemostasis.
DR   Reactome; REACT_6900; Immune System.
DR   DrugBank; DB00034; Interferon Alfa-2a, Recombinant.
DR   DrugBank; DB00105; Interferon Alfa-2b, Recombinant.
DR   DrugBank; DB00011; Interferon alfa-n1.
DR   DrugBank; DB00008; Peginterferon alfa-2a.
DR   DrugBank; DB00022; Peginterferon alfa-2b.
DR   EvolutionaryTrace; P01563; -.
DR   NextBio; 13556; -.
DR   ArrayExpress; P01563; -.
DR   Bgee; P01563; -.
DR   CleanEx; HS_IFNA2; -.
DR   Genevestigator; P01563; -.
DR   GermOnline; ENSG00000188379; Homo sapiens.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005132; F:interferon-alpha/beta receptor binding; TAS:ProtInc.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0006917; P:induction of apoptosis; TAS:ProtInc.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR   GO; GO:2000666; P:negative regulation of interleukin-13 secretion; IDA:UniProtKB.
DR   GO; GO:2000663; P:negative regulation of interleukin-5 secretion; IDA:UniProtKB.
DR   GO; GO:0045581; P:negative regulation of T cell differentiation; IDA:UniProtKB.
DR   GO; GO:2000552; P:negative regulation of T-helper 2 cell cytokine production; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR   GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0009615; P:response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome.
DR   Gene3D; G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR012351; 4_helix_cytokine_core.
DR   InterPro; IPR000471; Interferon_alpha/beta/delta.
DR   PANTHER; PTHR11691; Interferon_abd; 1.
DR   Pfam; PF00143; Interferon; 1.
DR   PRINTS; PR00266; INTERFERONAB.
DR   SMART; SM00076; IFabd; 1.
DR   SUPFAM; SSF47266; 4_helix_cytokine; 1.
DR   PROSITE; PS00252; INTERFERON_A_B_D; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Complete proteome; Cytokine;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Pharmaceutical; Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     23
FT   CHAIN        24    188       Interferon alpha-2.
FT                                /FTId=PRO_0000016360.
FT   CARBOHYD    129    129       O-linked (GalNAc...).
FT                                /FTId=CAR_000049.
FT   DISULFID     24    121
FT   DISULFID     52    161
FT   VARIANT       6      6       A -> D (in dbSNP:rs35971916).
FT                                /FTId=VAR_055972.
FT   VARIANT      46     46       K -> R (in alpha-2B and alpha-2C;
FT                                dbSNP:rs1061959).
FT                                /FTId=VAR_004012.
FT   VARIANT      57     57       H -> R (in alpha-2C).
FT                                /FTId=VAR_013001.
FT   VARIANT     177    177       S -> L (in a breast cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036329.
FT   HELIX        33     44
FT   TURN         49     54
FT   HELIX        63     66
FT   STRAND       67     69
FT   STRAND       71     75
FT   HELIX        76     91
FT   HELIX        93     98
FT   HELIX       101    123
FT   HELIX       134    155
FT   HELIX       160    178
FT   TURN        179    182
SQ   SEQUENCE   188 AA;  21550 MW;  101DD21D394CBF97 CRC64;
     MALTFALLVA LLVLSCKSSC SVGCDLPQTH SLGSRRTLML LAQMRKISLF SCLKDRHDFG
     FPQEEFGNQF QKAETIPVLH EMIQQIFNLF STKDSSAAWD ETLLDKFYTE LYQQLNDLEA
     CVIQGVGVTE TPLMKEDSIL AVRKYFQRIT LYLKEKKYSP CAWEVVRAEI MRSFSLSTNL
     QESLRSKE
//
ID   LACI_ECOLI              Reviewed;         360 AA.
AC   P03023; O09196; P71309; Q2MC79; Q47338;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 3.
DT   13-JUN-2012, entry version 136.
DE   RecName: Full=Lactose operon repressor;
GN   Name=lacI; OrderedLocusNames=b0345, JW0336;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=78246991; PubMed=355891; DOI=10.1038/274765a0;
RA   Farabaugh P.J.;
RT   "Sequence of the lacI gene.";
RL   Nature 274:765-769(1978).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Chen J., Matthews K.K.S.M.;
RL   Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Marsh S.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-147; 159-230 AND 233-360.
RX   MEDLINE=76091932; PubMed=1107032;
RX   DOI=10.1111/j.1432-1033.1975.tb02477.x;
RA   Beyreuther K., Adler K., Fanning E., Murray C., Klemm A., Geisler N.;
RT   "Amino-acid sequence of lac repressor from Escherichia coli.
RT   Isolation, sequence analysis and sequence assembly of tryptic peptides
RT   and cyanogen-bromide fragments.";
RL   Eur. J. Biochem. 59:491-509(1975).
RN   [8]
RP   PROTEIN SEQUENCE OF 1-59; 96-101; 206-215 AND 328-347.
RX   MEDLINE=73143730; PubMed=4571224;
RA   Platt T., Files J.G., Weber K.;
RT   "Lac repressor. Specific proteolytic destruction of the NH 2 -terminal
RT   region and loss of the deoxyribonucleic acid-binding activity.";
RL   J. Biol. Chem. 248:110-121(1973).
RN   [9]
RP   PROTEIN SEQUENCE OF 60-70; 73-78 AND 83-86.
RX   MEDLINE=74126378; PubMed=4594037; DOI=10.1073/pnas.70.11.3165;
RA   Ganem D., Miller J.H., Files J.G., Platt T., Weber K.;
RT   "Reinitiation of a lac repressor fragment at a condon other than
RT   AUG.";
RL   Proc. Natl. Acad. Sci. U.S.A. 70:3165-3169(1973).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
RX   MEDLINE=88230449; PubMed=3286877; DOI=10.1016/0022-2836(88)90237-9;
RA   Gordon A.J.E., Burns P.A., Fix D.F., Yatagai F., Allen F.L.,
RA   Horsfall M.J., Halliday J.A., Gray J., Bernelot-Moens C.,
RA   Glickman B.W.;
RT   "Missense mutation in the lacI gene of Escherichia coli. Inferences on
RT   the structure of the repressor protein.";
RL   J. Mol. Biol. 200:239-251(1988).
RN   [11]
RP   PROTEIN SEQUENCE OF 1-35.
RX   MEDLINE=96087076; PubMed=7498473; DOI=10.1016/0014-5793(95)01153-6;
RA   Kamashev D.E., Esipova N.G., Ebralidse K.K., Mirzabekov A.D.;
RT   "Mechanism of Lac repressor switch-off: orientation of the Lac
RT   repressor DNA-binding domain is reversed upon inducer binding.";
RL   FEBS Lett. 375:27-30(1995).
RN   [12]
RP   MUTAGENESIS.
RX   MEDLINE=90183956; PubMed=2178920;
RA   Lehming N., Sartorius J., Kisters-Woike B., von Wilcken-Bergmann B.,
RA   Mueller-Hill B.;
RT   "Mutant lac repressors with new specificities hint at rules for
RT   protein-DNA recognition.";
RL   EMBO J. 9:615-621(1990).
RN   [13]
RP   MUTAGENESIS.
RX   MEDLINE=94322386; PubMed=8046748; DOI=10.1006/jmbi.1994.1458;
RA   Markiewicz P., Kleina L.G., Cruz C., Ehret S., Miller J.H.;
RT   "Genetic studies of the lac repressor. XIV. Analysis of 4000 altered
RT   Escherichia coli lac repressors reveals essential and non-essential
RT   residues, as well as 'spacers' which do not require a specific
RT   sequence.";
RL   J. Mol. Biol. 240:421-433(1994).
RN   [14]
RP   3D-STRUCTURE MODELING.
RX   MEDLINE=91249837; PubMed=2040302;
RX   DOI=10.1111/j.1432-1033.1991.tb16030.x;
RA   Kisters-Woike B., Lehming N., Sartorius J., von Wilcken-Bergmann B.,
RA   Mueller-Hill B.;
RT   "A model of the lac repressor-operator complex based on physical and
RT   genetic data.";
RL   Eur. J. Biochem. 198:411-419(1991).
RN   [15]
RP   3D-STRUCTURE MODELING OF 1-56.
RX   MEDLINE=92020210; PubMed=1923807; DOI=10.1093/nar/19.19.5233;
RA   Shin J.A., Ebright R.H., Dervan P.B.;
RT   "Orientation of the Lac repressor DNA binding domain in complex with
RT   the left lac operator half site characterized by affinity cleaving.";
RL   Nucleic Acids Res. 19:5233-5236(1991).
RN   [16]
RP   STRUCTURE BY NMR.
RX   MEDLINE=89113344; PubMed=3064080;
RA   Boelens R., Lamerichs R.M.J.N., Rullmann J.A.C., van Boom J.H.,
RA   Kaptein R.;
RT   "The interaction of lac repressor headpiece with its operator: an NMR
RT   view.";
RL   Protein Seq. Data Anal. 1:487-498(1988).
RN   [17]
RP   STRUCTURE BY NMR.
RX   MEDLINE=89302886; PubMed=2742823; DOI=10.1021/bi00433a037;
RA   Lamerichs R.M.J.N., Boelens R., van der Marel G.A., van Boom J.H.,
RA   Kaptein R., Buck F., Fera B., Rueterjans H.;
RT   "H NMR study of a complex between the lac repressor headpiece and a 22
RT   base pair symmetric lac operator.";
RL   Biochemistry 28:2985-2991(1989).
RN   [18]
RP   STRUCTURE BY NMR OF 1-56.
RX   MEDLINE=96275660; PubMed=8683581; DOI=10.1006/jmbi.1996.0356;
RA   Slijper M., Bonvin A.M., Boelens R., Kaptein R.;
RT   "Refined structure of lac repressor headpiece (1-56) determined by
RT   relaxation matrix calculations from 2D and 3D NOE data: change of
RT   tertiary structure upon binding to the lac operator.";
RL   J. Mol. Biol. 259:761-773(1996).
RN   [19]
RP   STRUCTURE BY NMR OF 1-62.
RX   MEDLINE=20113476; PubMed=10647179; DOI=10.1016/S0969-2126(00)88339-2;
RA   Spronk C.A., Bonvin A.M., Radha P.K., Melacini G., Boelens R.,
RA   Kaptein R.;
RT   "The solution structure of Lac repressor headpiece 62 complexed to a
RT   symmetrical lac operator.";
RL   Structure 7:1483-1492(1999).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS).
RX   MEDLINE=96239623; PubMed=8638105; DOI=10.1126/science.271.5253.1247;
RA   Lewis M., Chang G., Horton N.C., Kercher M.A., Pace H.C.,
RA   Schumacher M.A., Brennan R.G., Lu P.;
RT   "Crystal structure of the lactose operon repressor and its complexes
RT   with DNA and inducer.";
RL   Science 271:1247-1254(1996).
CC   -!- FUNCTION: Repressor of the lactose operon. Binds allolactose as an
CC       inducer.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: Removing residues 1-59 results in loss of DNA-
CC       binding activity but retains tetrameric structure and inducer-
CC       binding activity. Deleting residues 340-360 results in loss of
CC       tetramer formation, but retains dimer formation, inducer-binding
CC       activity, and DNA-binding activity (if residues 1-59 are present).
CC   -!- SIMILARITY: Contains 1 HTH lacI-type DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB18069.1; Type=Erroneous initiation;
CC       Sequence=AAB47270.1; Type=Erroneous initiation;
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DR   EMBL; V00294; CAA23569.1; -; Genomic_DNA.
DR   EMBL; X58469; CAA41383.1; -; Genomic_DNA.
DR   EMBL; U86347; AAB47270.1; ALT_INIT; Genomic_DNA.
DR   EMBL; J01636; AAA24052.1; -; Genomic_DNA.
DR   EMBL; U72488; AAB36549.1; -; Genomic_DNA.
DR   EMBL; U78872; AAB37348.1; -; Genomic_DNA.
DR   EMBL; U78873; AAB37351.1; -; Genomic_DNA.
DR   EMBL; U78874; AAB37354.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18069.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73448.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76127.1; -; Genomic_DNA.
DR   PIR; A93198; RPECL.
DR   RefSeq; NP_414879.3; NC_000913.2.
DR   PDB; 1CJG; NMR; -; A/B=1-62.
DR   PDB; 1EFA; X-ray; 2.60 A; A/B/C=1-333.
DR   PDB; 1JWL; X-ray; 4.00 A; A/B/C=1-333.
DR   PDB; 1JYE; X-ray; 1.70 A; A=1-349.
DR   PDB; 1JYF; X-ray; 3.00 A; A=1-349.
DR   PDB; 1L1M; NMR; -; A/B=1-62.
DR   PDB; 1LBG; X-ray; 4.80 A; A/B/C/D=1-360.
DR   PDB; 1LBH; X-ray; 3.20 A; A/B/C/D=1-360.
DR   PDB; 1LBI; X-ray; 2.70 A; A/B/C/D=1-360.
DR   PDB; 1LCC; NMR; -; A=1-51.
DR   PDB; 1LCD; NMR; -; A=1-51.
DR   PDB; 1LQC; NMR; -; A=1-56.
DR   PDB; 1LTP; Model; -; L=62-323.
DR   PDB; 1OSL; NMR; -; A/B=1-62.
DR   PDB; 1TLF; X-ray; 2.60 A; A/B/C/D=60-360.
DR   PDB; 1Z04; Model; -; A/B/C/D=1-357.
DR   PDB; 2BJC; NMR; -; A/B=1-62.
DR   PDB; 2KEI; NMR; -; A/B=1-62.
DR   PDB; 2KEJ; NMR; -; A/B=1-62.
DR   PDB; 2KEK; NMR; -; A/B=1-62.
DR   PDB; 2P9H; X-ray; 2.00 A; A/B=62-330.
DR   PDB; 2PAF; X-ray; 3.50 A; A/B=62-330.
DR   PDB; 2PE5; X-ray; 3.50 A; A/B/C=2-331.
DR   PDB; 3EDC; X-ray; 2.10 A; A/B/C/D=1-360.
DR   PDBsum; 1CJG; -.
DR   PDBsum; 1EFA; -.
DR   PDBsum; 1JWL; -.
DR   PDBsum; 1JYE; -.
DR   PDBsum; 1JYF; -.
DR   PDBsum; 1L1M; -.
DR   PDBsum; 1LBG; -.
DR   PDBsum; 1LBH; -.
DR   PDBsum; 1LBI; -.
DR   PDBsum; 1LCC; -.
DR   PDBsum; 1LCD; -.
DR   PDBsum; 1LQC; -.
DR   PDBsum; 1LTP; -.
DR   PDBsum; 1OSL; -.
DR   PDBsum; 1TLF; -.
DR   PDBsum; 1Z04; -.
DR   PDBsum; 2BJC; -.
DR   PDBsum; 2KEI; -.
DR   PDBsum; 2KEJ; -.
DR   PDBsum; 2KEK; -.
DR   PDBsum; 2P9H; -.
DR   PDBsum; 2PAF; -.
DR   PDBsum; 2PE5; -.
DR   PDBsum; 3EDC; -.
DR   DisProt; DP00433; -.
DR   ProteinModelPortal; P03023; -.
DR   SMR; P03023; 1-360.
DR   DIP; DIP-10079N; -.
DR   IntAct; P03023; 5.
DR   ECO2DBASE; H039.0; 6TH EDITION.
DR   EnsemblBacteria; EBESCT00000002264; EBESCP00000002264; EBESCG00000001853.
DR   EnsemblBacteria; EBESCT00000002265; EBESCP00000002265; EBESCG00000001853.
DR   EnsemblBacteria; EBESCT00000014841; EBESCP00000014132; EBESCG00000013901.
DR   GeneID; 945007; -.
DR   GenomeReviews; AP009048_GR; JW0336.
DR   GenomeReviews; U00096_GR; b0345.
DR   KEGG; eco:b0345; -.
DR   PATRIC; 32115823; VBIEscCol129921_0353.
DR   EchoBASE; EB0520; -.
DR   EcoGene; EG10525; lacI.
DR   eggNOG; COG1609; -.
DR   HOGENOM; HOG000220179; -.
DR   OMA; DIVPTAM; -.
DR   ProtClustDB; PRK09526; -.
DR   BioCyc; EcoCyc:PD00763; -.
DR   EvolutionaryTrace; P03023; -.
DR   Genevestigator; P03023; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.260.40; G3DSA:1.10.260.40; 1.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom.
DR   InterPro; IPR000843; Tscrpt_reg_HTH_LacI.
DR   Pfam; PF00356; LacI; 1.
DR   PRINTS; PR00036; HTHLACI.
DR   SMART; SM00354; HTH_LACI; 1.
DR   SUPFAM; SSF47413; Lambda_like_DNA; 1.
DR   PROSITE; PS00356; HTH_LACI_1; 1.
DR   PROSITE; PS50932; HTH_LACI_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Direct protein sequencing;
KW   DNA-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    360       Lactose operon repressor.
FT                                /FTId=PRO_0000107963.
FT   DOMAIN        1     58       HTH lacI-type.
FT   DNA_BIND      6     25       H-T-H motif.
FT   VARIANT     282    282       Y -> D (in T41 mutant).
FT   MUTAGEN      17     17       Y->H: Broadening of specificity.
FT   MUTAGEN      22     22       R->N: Recognizes an operator variant.
FT   CONFLICT    286    286       L -> S (in Ref. 1, 4 and 7).
FT   HELIX         6     11
FT   TURN         12     14
FT   HELIX        17     24
FT   HELIX        33     45
FT   HELIX        51     56
FT   STRAND       63     69
FT   HELIX        74     89
FT   STRAND       93     98
FT   STRAND      101    103
FT   HELIX       104    115
FT   TURN        116    118
FT   STRAND      122    126
FT   HELIX       130    139
FT   TURN        140    142
FT   STRAND      145    150
FT   STRAND      154    156
FT   STRAND      158    161
FT   HELIX       163    177
FT   STRAND      181    186
FT   HELIX       192    207
FT   STRAND      213    217
FT   HELIX       222    234
FT   STRAND      240    246
FT   HELIX       247    259
FT   TURN        265    267
FT   STRAND      268    271
FT   HELIX       277    281
FT   STRAND      282    284
FT   STRAND      287    290
FT   HELIX       293    308
FT   STRAND      314    319
FT   STRAND      322    324
FT   STRAND      334    338
FT   HELIX       343    353
FT   HELIX       354    356
SQ   SEQUENCE   360 AA;  38590 MW;  347A8DEE92D736CB CRC64;
     MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN RVAQQLAGKQ
     SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE RSGVEACKAA VHNLLAQRVS
     GLIINYPLDD QDAIAVEAAC TNVPALFLDV SDQTPINSII FSHEDGTRLG VEHLVALGHQ
     QIALLAGPLS SVSARLRLAG WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT
     AMLVANDQMA LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPLTTIK QDFRLLGQTS
     VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA RQVSRLESGQ
//
ID   LACY_ECOLI              Reviewed;         417 AA.
AC   P02920; Q2MC81;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   16-MAY-2012, entry version 124.
DE   RecName: Full=Lactose permease;
DE   AltName: Full=Lactose-proton symport;
GN   Name=lacY; OrderedLocusNames=b0343, JW0334;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0;
RA   Buechel D.E., Gronenborn B., Mueller-Hill B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Pastore J.C., Larigan J.D., Consler T.G., Kaback H.R.;
RL   Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   TOPOLOGY.
RX   PubMed=16453726;
RA   von Heijne G.;
RT   "The distribution of positively charged residues in bacterial inner
RT   membrane proteins correlates with the trans-membrane topology.";
RL   EMBO J. 5:3021-3027(1986).
RN   [7]
RP   TOPOLOGY.
RX   MEDLINE=90311318; PubMed=2164211; DOI=10.1073/pnas.87.13.4937;
RA   Calamia J., Manoil C.;
RT   "lac permease of Escherichia coli: topology and sequence elements
RT   promoting membrane insertion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4937-4941(1990).
RN   [8]
RP   TOPOLOGY.
RX   MEDLINE=96066665; PubMed=7578103; DOI=10.1021/bi00045a036;
RA   Ujwal M.L., Jung H., Bibi E., Manoil C., Altenbach C., Hubbell W.L.,
RA   Kaback H.R.;
RT   "Membrane topology of helices VII and XI in the lactose permease of
RT   Escherichia coli studied by lacY-phoA fusion analysis and site-
RT   directed spectroscopy.";
RL   Biochemistry 34:14909-14917(1995).
RN   [9]
RP   MUTAGENESIS.
RX   MEDLINE=91167519; PubMed=1848449; DOI=10.1016/0005-2736(91)90390-T;
RA   King S.C., Hansen C.L., Wilson T.H.;
RT   "The interaction between aspartic acid 237 and lysine 358 in the
RT   lactose carrier of Escherichia coli.";
RL   Biochim. Biophys. Acta 1062:177-186(1991).
RN   [10]
RP   MUTAGENESIS.
RX   MEDLINE=92355521; PubMed=1644770;
RA   Huang A.-M., Lee J.-I., King S.C., Wilson T.H.;
RT   "Amino acid substitution in the lactose carrier protein with the use
RT   of amber suppressors.";
RL   J. Bacteriol. 174:5436-5441(1992).
RN   [11]
RP   REVIEW.
RX   MEDLINE=90366577; PubMed=2203471; DOI=10.1016/0005-2728(90)90239-Z;
RA   Kaback H.R.;
RT   "The lac permease of Escherichia coli: a prototypic energy-transducing
RT   membrane protein.";
RL   Biochim. Biophys. Acta 1018:160-162(1990).
RN   [12]
RP   MASS SPECTROMETRY OF FORMYLATED FORM.
RX   MEDLINE=99415921; PubMed=10485888; DOI=10.1073/pnas.96.19.10695;
RA   Whitelegge J.P., le Coutre J., Lee J.C., Engel C.K., Prive G.G.,
RA   Faull K.F., Kaback H.R.;
RT   "Toward the bilayer proteome, electrospray ionization-mass
RT   spectrometry of large, intact transmembrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10695-10698(1999).
RN   [13]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15919996; DOI=10.1126/science.1109730;
RA   Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT   "Global topology analysis of the Escherichia coli inner membrane
RT   proteome.";
RL   Science 308:1321-1323(2005).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF MUTANT GLY-154.
RX   MEDLINE=22776143; PubMed=12893935; DOI=10.1126/science.1088196;
RA   Abramson J., Smirnova I., Kasho V., Verner G., Kaback H.R., Iwata S.;
RT   "Structure and mechanism of the lactose permease of Escherichia
RT   coli.";
RL   Science 301:610-615(2003).
CC   -!- FUNCTION: Responsible for transport of beta-galactosides into the
CC       cell, with the concomitant import of a proton (symport system).
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein.
CC   -!- MASS SPECTROMETRY: Mass=47357; Method=Electrospray; Range=1-417;
CC       Source=PubMed:10485888;
CC   -!- SIMILARITY: Belongs to the lacY/rafB permease family.
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DR   EMBL; J01636; AAA24054.1; -; Genomic_DNA.
DR   EMBL; V00295; CAA23571.1; -; Genomic_DNA.
DR   EMBL; X56095; CAA39575.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18067.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73446.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76125.1; -; Genomic_DNA.
DR   PIR; A03418; GREC.
DR   RefSeq; NP_414877.1; NC_000913.2.
DR   PDB; 1M2U; Model; -; A=1-417.
DR   PDB; 1PV6; X-ray; 3.50 A; A/B=1-417.
DR   PDB; 1PV7; X-ray; 3.60 A; A/B=1-417.
DR   PDB; 2CFP; X-ray; 3.30 A; A=1-417.
DR   PDB; 2CFQ; X-ray; 2.95 A; A=1-417.
DR   PDB; 2V8N; X-ray; 3.60 A; A/B=1-417.
DR   PDB; 2Y5Y; X-ray; 3.38 A; A/B=1-417.
DR   PDBsum; 1M2U; -.
DR   PDBsum; 1PV6; -.
DR   PDBsum; 1PV7; -.
DR   PDBsum; 2CFP; -.
DR   PDBsum; 2CFQ; -.
DR   PDBsum; 2V8N; -.
DR   PDBsum; 2Y5Y; -.
DR   ProteinModelPortal; P02920; -.
DR   SMR; P02920; 1-417.
DR   DIP; DIP-10080N; -.
DR   TCDB; 2.A.1.5.1; major facilitator superfamily (MFS).
DR   EnsemblBacteria; EBESCT00000004293; EBESCP00000004293; EBESCG00000003502.
DR   EnsemblBacteria; EBESCT00000004294; EBESCP00000004294; EBESCG00000003502.
DR   EnsemblBacteria; EBESCT00000004295; EBESCP00000004295; EBESCG00000003502.
DR   EnsemblBacteria; EBESCT00000004296; EBESCP00000004296; EBESCG00000003502.
DR   EnsemblBacteria; EBESCT00000017446; EBESCP00000016737; EBESCG00000016502.
DR   GeneID; 949083; -.
DR   GenomeReviews; AP009048_GR; JW0334.
DR   GenomeReviews; U00096_GR; b0343.
DR   KEGG; eco:b0343; -.
DR   PATRIC; 32115819; VBIEscCol129921_0351.
DR   EchoBASE; EB0521; -.
DR   EcoGene; EG10526; lacY.
DR   eggNOG; COG0477; -.
DR   HOGENOM; HOG000114363; -.
DR   KO; K02532; -.
DR   OMA; WAICASI; -.
DR   ProtClustDB; PRK09528; -.
DR   BioCyc; EcoCyc:LACY-MONOMER; -.
DR   EvolutionaryTrace; P02920; -.
DR   Genevestigator; P02920; -.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:EcoCyc.
DR   GO; GO:0030395; F:lactose binding; IDA:EcoliWiki.
DR   GO; GO:0015528; F:lactose:hydrogen symporter activity; IDA:EcoCyc.
DR   InterPro; IPR022814; LacY_symp.
DR   InterPro; IPR000576; LacY_symport_bac.
DR   InterPro; IPR018457; LacY_symport_CS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR016196; MFS_dom_general_subst_transpt.
DR   PANTHER; PTHR24003:SF271; PTHR24003:SF271; 1.
DR   Pfam; PF01306; LacY_symp; 1.
DR   PRINTS; PR00174; LACYSMPORT.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00882; 2A0105; 1.
DR   PROSITE; PS00896; LACY_1; 1.
DR   PROSITE; PS00897; LACY_2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Complete proteome;
KW   Formylation; Membrane; Reference proteome; Sugar transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    417       Lactose permease.
FT                                /FTId=PRO_0000196184.
FT   TOPO_DOM      1      7       Cytoplasmic.
FT   TRANSMEM      8     34       Helical; Name=1.
FT   TOPO_DOM     35     41       Periplasmic.
FT   TRANSMEM     42     70       Helical; Name=2.
FT   TOPO_DOM     71     74       Cytoplasmic.
FT   TRANSMEM     75    100       Helical; Name=3.
FT   TOPO_DOM    101    104       Periplasmic.
FT   TRANSMEM    105    129       Helical; Name=4.
FT   TOPO_DOM    130    140       Cytoplasmic.
FT   TRANSMEM    141    163       Helical; Name=5.
FT   TOPO_DOM    164    166       Periplasmic.
FT   TRANSMEM    167    186       Helical; Name=6.
FT   TOPO_DOM    187    220       Cytoplasmic.
FT   TRANSMEM    221    249       Helical; Name=7.
FT   TOPO_DOM    250    253       Periplasmic.
FT   TRANSMEM    254    278       Helical; Name=8.
FT   TOPO_DOM    279    288       Cytoplasmic.
FT   TRANSMEM    289    308       Helical; Name=9.
FT   TOPO_DOM    309    311       Periplasmic.
FT   TRANSMEM    312    334       Helical; Name=10.
FT   TOPO_DOM    335    346       Cytoplasmic.
FT   TRANSMEM    347    374       Helical; Name=11.
FT   TOPO_DOM    375    377       Periplasmic.
FT   TRANSMEM    378    398       Helical; Name=12.
FT   TOPO_DOM    399    417       Cytoplasmic.
FT   SITE        126    126       Substrate binding.
FT   SITE        144    144       Substrate binding.
FT   SITE        269    269       Substrate binding and proton
FT                                translocation.
FT   SITE        302    302       Proton translocation.
FT   SITE        322    322       Proton translocation.
FT   SITE        325    325       Proton translocation.
FT   MOD_RES       1      1       N-formylmethionine; partial.
FT   MUTAGEN     237    237       D->N,G: Defect in melibiose transport.
FT   MUTAGEN     358    358       K->T: Defect in melibiose transport.
FT   TURN          2      4
FT   HELIX         8     12
FT   TURN         13     16
FT   HELIX        17     23
FT   TURN         24     28
FT   HELIX        31     38
FT   HELIX        42     54
FT   TURN         55     57
FT   HELIX        60     67
FT   HELIX        68     70
FT   HELIX        76     79
FT   TURN         80     83
FT   STRAND       84     87
FT   HELIX        88     93
FT   HELIX        96     99
FT   TURN        100    102
FT   HELIX       105    109
FT   TURN        114    120
FT   HELIX       121    135
FT   HELIX       140    142
FT   HELIX       144    164
FT   HELIX       168    171
FT   HELIX       173    177
FT   HELIX       178    183
FT   STRAND      201    203
FT   HELIX       210    216
FT   HELIX       220    231
FT   TURN        232    235
FT   HELIX       236    242
FT   HELIX       245    249
FT   STRAND      251    254
FT   HELIX       257    267
FT   HELIX       270    276
FT   HELIX       279    286
FT   HELIX       289    307
FT   HELIX       312    320
FT   HELIX       322    324
FT   HELIX       326    340
FT   TURN        343    345
FT   HELIX       346    349
FT   HELIX       351    356
FT   HELIX       357    399
FT   STRAND      408    411
FT   TURN        414    416
SQ   SEQUENCE   417 AA;  46503 MW;  24A8062F628CDA32 CRC64;
     MYYLKNTNFW MFGLFFFFYF FIMGAYFPFF PIWLHDINHI SKSDTGIIFA AISLFSLLFQ
     PLFGLLSDKL GLRKYLLWII TGMLVMFAPF FIFIFGPLLQ YNILVGSIVG GIYLGFCFNA
     GAPAVEAFIE KVSRRSNFEF GRARMFGCVG WALCASIVGI MFTINNQFVF WLGSGCALIL
     AVLLFFAKTD APSSATVANA VGANHSAFSL KLALELFRQP KLWFLSLYVI GVSCTYDVFD
     QQFANFFTSF FATGEQGTRV FGYVTTMGEL LNASIMFFAP LIINRIGGKN ALLLAGTIMS
     VRIIGSSFAT SALEVVILKT LHMFEVPFLL VGCFKYITSQ FEVRFSATIY LVCFCFFKQL
     AMIFMSVLAG NMYESIGFQG AYLVLGLVAL GFTLISVFTL SGPGPLSLLR RQVNEVA
//
ID   OPS2_DROME              Reviewed;         381 AA.
AC   P08099; Q9VE29;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   22-FEB-2012, entry version 112.
DE   RecName: Full=Opsin Rh2;
DE   AltName: Full=Ocellar opsin;
GN   Name=Rh2; ORFNames=CG16740;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86133563; PubMed=2936466; DOI=10.1016/0092-8674(86)90836-6;
RA   Cowman A.F., Zuker C.S., Rubin G.M.;
RT   "An opsin gene expressed in only one photoreceptor cell type of the
RT   Drosophila eye.";
RL   Cell 44:705-710(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   LOCALIZATION OF OPSIN RH2, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   MEDLINE=88261498; PubMed=2455230; DOI=10.1038/333737a0;
RA   Feiler R., Harris W.A., Kirschfeld K., Wehrhahn C., Zuker C.S.;
RT   "Targeted misexpression of a Drosophila opsin gene leads to altered
RT   visual function.";
RL   Nature 333:737-741(1988).
RN   [5]
RP   LOCALIZATION OF OPSIN RH2.
RX   MEDLINE=88261503; PubMed=2968518; DOI=10.1038/333779a0;
RA   Pollock J.A., Benzer S.;
RT   "Transcript localization of four opsin genes in the three visual
RT   organs of Drosophila; RH2 is ocellus specific.";
RL   Nature 333:779-782(1988).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=420 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Predominant opsin expressed in the dorsal
CC       ocelli.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M12896; AAA28734.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55601.1; -; Genomic_DNA.
DR   PIR; A24058; OOFF2.
DR   RefSeq; NP_524398.1; NM_079674.3.
DR   ProteinModelPortal; P08099; -.
DR   SMR; P08099; 39-360.
DR   DIP; DIP-22447N; -.
DR   IntAct; P08099; 1.
DR   MINT; MINT-844888; -.
DR   STRING; P08099; -.
DR   PRIDE; P08099; -.
DR   EnsemblMetazoa; FBtr0083697; FBpp0083111; FBgn0003248.
DR   GeneID; 42261; -.
DR   KEGG; dme:Dmel_CG16740; -.
DR   CTD; 42261; -.
DR   FlyBase; FBgn0003248; Rh2.
DR   eggNOG; NOG255465; -.
DR   GeneTree; ENSGT00550000074069; -.
DR   InParanoid; P08099; -.
DR   KO; K04255; -.
DR   OMA; RSSEDCD; -.
DR   OrthoDB; EOG451C6G; -.
DR   PhylomeDB; P08099; -.
DR   NextBio; 827942; -.
DR   Bgee; P08099; -.
DR   GermOnline; CG16740; Drosophila melanogaster.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008020; F:G-protein coupled photoreceptor activity; IDA:FlyBase.
DR   GO; GO:0007602; P:phototransduction; IGI:FlyBase.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR001735; Opsin_RH1/RH2.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00576; OPSINRH1RH2.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN         1    381       Opsin Rh2.
FT                                /FTId=PRO_0000197625.
FT   TOPO_DOM      1     56       Extracellular.
FT   TRANSMEM     57     81       Helical; Name=1; (Potential).
FT   TOPO_DOM     82     93       Cytoplasmic.
FT   TRANSMEM     94    119       Helical; Name=2; (Potential).
FT   TOPO_DOM    120    133       Extracellular.
FT   TRANSMEM    134    153       Helical; Name=3; (Potential).
FT   TOPO_DOM    154    172       Cytoplasmic.
FT   TRANSMEM    173    196       Helical; Name=4; (Potential).
FT   TOPO_DOM    197    220       Extracellular.
FT   TRANSMEM    221    248       Helical; Name=5; (Potential).
FT   TOPO_DOM    249    283       Cytoplasmic.
FT   TRANSMEM    284    307       Helical; Name=6; (Potential).
FT   TOPO_DOM    308    314       Extracellular.
FT   TRANSMEM    315    339       Helical; Name=7; (Potential).
FT   TOPO_DOM    340    381       Cytoplasmic.
FT   MOD_RES     326    326       N6-(retinylidene)lysine.
FT   CARBOHYD     27     27       N-linked (GlcNAc...) (Probable).
FT   DISULFID    130    207       Potential.
SQ   SEQUENCE   381 AA;  42722 MW;  628322D228396F9D CRC64;
     MERSHLPETP FDLAHSGPRF QAQSSGNGSV LDNVLPDMAH LVNPYWSRFA PMDPMMSKIL
     GLFTLAIMII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY
     ETWVLGPLWC DIYAGCGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKILFI
     WMMAVFWTVM PLIGWSAYVP EGNLTACSID YMTRMWNPRS YLITYSLFVY YTPLFLICYS
     YWFIIAAVAA HEKAMREQAK KMNVKSLRSS EDCDKSAEGK LAKVALTTIS LWFMAWTPYL
     VICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRIVLKEK CPMCVFGNTD
     EPKPDAPASD TETTSEADSK A
//
ID   OPS2_DROPS              Reviewed;         381 AA.
AC   P28679; Q298F1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 3.
DT   18-APR-2012, entry version 85.
DE   RecName: Full=Opsin Rh2;
DE   AltName: Full=Ocellar opsin;
GN   Name=Rh2; ORFNames=GA14120;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Apple Hill;
RX   MEDLINE=93012921; PubMed=1398053;
RA   Carulli J.P., Hartl D.L.;
RT   "Variable rates of evolution among Drosophila opsin genes.";
RL   Genetics 132:193-204(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P.,
RA   Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J.,
RA   van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E.,
RA   Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D.,
RA   Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D.,
RA   Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R.,
RA   Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L.,
RA   Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura:
RT   chromosomal, gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=420 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Some or all of the Ser/Thr residues present in the C-terminal
CC       part may be phosphorylated.
CC   -!- MISCELLANEOUS: Opsin Rh2 is the predominant opsin expressed in the
CC       dorsal ocelli.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL28004.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X65878; CAA46709.1; -; Genomic_DNA.
DR   EMBL; CM000070; EAL28004.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S40692; S40692.
DR   RefSeq; XP_001358861.1; XM_001358824.2.
DR   ProteinModelPortal; P28679; -.
DR   GeneID; 4801828; -.
DR   GenomeReviews; CM000070_GR; Rh2.
DR   KEGG; dpo:Dpse_GA14120; -.
DR   FlyBase; FBgn0012708; Dpse\Rh2.
DR   eggNOG; NOG255465; -.
DR   InParanoid; P28679; -.
DR   KO; K04255; -.
DR   OMA; RSSEDCD; -.
DR   OrthoDB; EOG451C6G; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR001735; Opsin_RH1/RH2.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00576; OPSINRH1RH2.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Reference proteome; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN         1    381       Opsin Rh2.
FT                                /FTId=PRO_0000197626.
FT   TOPO_DOM      1     56       Extracellular.
FT   TRANSMEM     57     81       Helical; Name=1; (Potential).
FT   TOPO_DOM     82     93       Cytoplasmic.
FT   TRANSMEM     94    119       Helical; Name=2; (Potential).
FT   TOPO_DOM    120    133       Extracellular.
FT   TRANSMEM    134    153       Helical; Name=3; (Potential).
FT   TOPO_DOM    154    172       Cytoplasmic.
FT   TRANSMEM    173    196       Helical; Name=4; (Potential).
FT   TOPO_DOM    197    220       Extracellular.
FT   TRANSMEM    221    248       Helical; Name=5; (Potential).
FT   TOPO_DOM    249    283       Cytoplasmic.
FT   TRANSMEM    284    307       Helical; Name=6; (Potential).
FT   TOPO_DOM    308    314       Extracellular.
FT   TRANSMEM    315    339       Helical; Name=7; (Potential).
FT   TOPO_DOM    340    381       Cytoplasmic.
FT   MOD_RES     326    326       N6-(retinylidene)lysine.
FT   CARBOHYD     27     27       N-linked (GlcNAc...) (Probable).
FT   DISULFID    130    207       Potential.
FT   CONFLICT     45     45       Y -> H (in Ref. 1; CAA46709).
FT   CONFLICT    342    343       KY -> ND (in Ref. 1; CAA46709).
FT   CONFLICT    358    358       S -> T (in Ref. 1; CAA46709).
FT   CONFLICT    381    381       A -> D (in Ref. 1; CAA46709).
SQ   SEQUENCE   381 AA;  42733 MW;  2033C05C4503FEAF CRC64;
     MERSLLPEPP LAMALLGPRF EAQTGGNRSV LDNVLPDMAP LVNPYWSRFA PMDPTMSKIL
     GLFTLVILII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY
     ETWVLGPLWC DIYAACGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKIAFI
     WMMAVFWTIM PLIGWSSYVP EGNLTACSID YMTRQWNPRS YLITYSLFVY YTPLFMICYS
     YWFIIATVAA HEKAMRDQAK KMNVKSLRSS EDCDKSAENK LAKVALTTIS LWFMAWTPYL
     IICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRLVLKEK CPMCVCGSTD
     EPKPDAPPSD TETTSEAESK A
//
ID   OPS2_SCHGR              Reviewed;         380 AA.
AC   Q26495;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   21-SEP-2011, entry version 61.
DE   RecName: Full=Opsin-2;
GN   Name=Lo2;
OS   Schistocerca gregaria (Desert locust).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Orthopteroidea; Orthoptera; Caelifera; Acridomorpha;
OC   Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca.
OX   NCBI_TaxID=7010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97301174; PubMed=9156194; DOI=10.1016/S0042-6989(96)00198-8;
RA   Towner P., Harris P., Wolstenholme A.J., Hill C., Worm K., Gartner W.;
RT   "Primary structure of locust opsins: a speculative model which may
RT   account for ultraviolet wavelength light detection.";
RL   Vision Res. 37:495-503(1997).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80072; CAA56378.1; -; mRNA.
DR   ProteinModelPortal; Q26495; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000856; Opsin_RH3/RH4.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00577; OPSINRH3RH4.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   2: Evidence at transcript level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN         1    380       Opsin-2.
FT                                /FTId=PRO_0000197636.
FT   TOPO_DOM      1     51       Extracellular.
FT   TRANSMEM     52     76       Helical; Name=1; (Potential).
FT   TOPO_DOM     77     88       Cytoplasmic.
FT   TRANSMEM     89    115       Helical; Name=2; (Potential).
FT   TOPO_DOM    116    128       Extracellular.
FT   TRANSMEM    129    148       Helical; Name=3; (Potential).
FT   TOPO_DOM    149    166       Cytoplasmic.
FT   TRANSMEM    167    191       Helical; Name=4; (Potential).
FT   TOPO_DOM    192    215       Extracellular.
FT   TRANSMEM    216    243       Helical; Name=5; (Potential).
FT   TOPO_DOM    244    279       Cytoplasmic.
FT   TRANSMEM    280    303       Helical; Name=6; (Potential).
FT   TOPO_DOM    304    311       Extracellular.
FT   TRANSMEM    312    336       Helical; Name=7; (Potential).
FT   TOPO_DOM    337    380       Cytoplasmic.
FT   MOD_RES     323    323       N6-(retinylidene)lysine (By similarity).
FT   CARBOHYD      3      3       N-linked (GlcNAc...) (Potential).
FT   DISULFID    125    202       Potential.
SQ   SEQUENCE   380 AA;  42531 MW;  113504F71027C07A CRC64;
     MVNTTDFYPV PAAMAYESSV GLPLLGWNVP TEHLDLVHPH WRSFQVPNKY WHFGLAFVYF
     MLMCMSSLGN GIVLWIYATT KSIRTPSNMF IVNLALFDVL MLLEMPMLVV SSLFYQRPVG
     WELGCDIYAA LGSVAGIGSA INNAAIAFDR YRTISCPIDG RLTQGQVLAL IAGTWVWTLP
     FTLMPLLRIW SRFTAEGFLT TCSFDYLTDD EDTKVFVGCI FAWSYAFPLC LICCFYYRLI
     GAVREHEKML RDQAKKMNVK SLQSNADTEA QSAEIRIAKV ALTIFFLFLC SWTPYAVVAM
     IGAFGNRAAL TPLSTMIPAV TAKIVSCIDP WVYAINHPRF RAEVQKRMKW LHLGEDARSS
     KSDTSSTATD RTVGNVSASA
//
ID   OPSC2_HEMSA             Reviewed;         377 AA.
AC   Q25158;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   21-SEP-2011, entry version 60.
DE   RecName: Full=Compound eye opsin BCRH2;
OS   Hemigrapsus sanguineus (Asian shore crab).
OC   Eukaryota; Metazoa; Arthropoda; Crustacea; Malacostraca;
OC   Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura;
OC   Eubrachyura; Grapsoidea; Varunidae; Hemigrapsus.
OX   NCBI_TaxID=40176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   PubMed=9318091;
RA   Sakamoto K., Hisatomi O., Tokunaga F., Eguchi E.;
RT   "Two opsins from the compound eye of the crab Hemigrapsus
RT   sanguineus.";
RL   J. Exp. Biol. 199:441-450(1996).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal. This opsin produces visual pigments with
CC       maximal absorption in the blue-green region of the spectrum.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in all of the seven retinular cells
CC       (R1-R7) forming the main rhabdom in each ommatidium.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D50584; BAA09133.1; -; mRNA.
DR   ProteinModelPortal; Q25158; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000856; Opsin_RH3/RH4.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00577; OPSINRH3RH4.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   2: Evidence at transcript level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN         1    377       Compound eye opsin BCRH2.
FT                                /FTId=PRO_0000197750.
FT   TOPO_DOM      1     53       Extracellular.
FT   TRANSMEM     54     78       Helical; Name=1; (Potential).
FT   TOPO_DOM     79     90       Cytoplasmic.
FT   TRANSMEM     91    115       Helical; Name=2; (Potential).
FT   TOPO_DOM    116    131       Extracellular.
FT   TRANSMEM    132    151       Helical; Name=3; (Potential).
FT   TOPO_DOM    152    170       Cytoplasmic.
FT   TRANSMEM    171    194       Helical; Name=4; (Potential).
FT   TOPO_DOM    195    218       Extracellular.
FT   TRANSMEM    219    246       Helical; Name=5; (Potential).
FT   TOPO_DOM    247    281       Cytoplasmic.
FT   TRANSMEM    282    305       Helical; Name=6; (Potential).
FT   TOPO_DOM    306    313       Extracellular.
FT   TRANSMEM    314    338       Helical; Name=7; (Potential).
FT   TOPO_DOM    339    377       Cytoplasmic.
FT   MOD_RES     325    325       N6-(retinylidene)lysine (By similarity).
FT   CARBOHYD      3      3       N-linked (GlcNAc...) (Potential).
FT   DISULFID    128    205       By similarity.
SQ   SEQUENCE   377 AA;  42114 MW;  FD6CC2E0E199A256 CRC64;
     MTNATGPQMA YYGAASMDFG YPEGVSIVDF VRPEIKPYVH QHWYNYPPVN PMWHYLLGVI
     YLFLGTVSIF GNGLVIYLFN KSAALRTPAN ILVVNLALSD LIMLTTNVPF FTYNCFSGGV
     WMFSPQYCEI YACLGAITGV CSIWLLCMIS FDRYNIICNG FNGPKLTTGK AVVFALISWV
     IAIGCALPPF FGWGNYILEG ILDSCSYDYL TQDFNTFSYN IFIFVFDYFL PAAIIVFSYV
     FIVKAIFAHE AAMRAQAKKM NVSTLRSNEA DAQRAEIRIA KTALVNVSLW FICWTPYALI
     SLKGVMGDTS GITPLVSTLP ALLAKSCSCY NPFVYAISHP KYRLAITQHL PWFCVHETET
     KSNDDSQSNS TVAQDKA
//
ID   OPSD2_MIZYE             Reviewed;         399 AA.
AC   O15974;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   21-SEP-2011, entry version 58.
DE   RecName: Full=Rhodopsin, G0-coupled;
DE   AltName: Full=G0-rhodopsin;
GN   Name=SCOP2;
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Pectinoida;
OC   Pectinoidea; Pectinidae; Mizuhopecten.
OX   NCBI_TaxID=6573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   MEDLINE=97435252; PubMed=9287291; DOI=10.1074/jbc.272.37.22979;
RA   Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A.,
RA   Shichida Y.;
RT   "A novel Go-mediated phototransduction cascade in scallop visual
RT   cells.";
RL   J. Biol. Chem. 272:22979-22982(1997).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Retina. Expressed in the hyperpolarizing cell
CC       layer of the photoreceptor cells with its photoreceptive region
CC       adjacent to the lens.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB006455; BAA22218.1; -; mRNA.
DR   ProteinModelPortal; O15974; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR002962; Peropsin.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01244; PEROPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN         1    399       Rhodopsin, G0-coupled.
FT                                /FTId=PRO_0000197736.
FT   TOPO_DOM      1     17       Extracellular.
FT   TRANSMEM     18     43       Helical; Name=1; (Potential).
FT   TOPO_DOM     44     55       Cytoplasmic.
FT   TRANSMEM     56     81       Helical; Name=2; (Potential).
FT   TOPO_DOM     82     95       Extracellular.
FT   TRANSMEM     96    115       Helical; Name=3; (Potential).
FT   TOPO_DOM    116    134       Cytoplasmic.
FT   TRANSMEM    135    158       Helical; Name=4; (Potential).
FT   TOPO_DOM    159    182       Extracellular.
FT   TRANSMEM    183    210       Helical; Name=5; (Potential).
FT   TOPO_DOM    211    240       Cytoplasmic.
FT   TRANSMEM    241    263       Helical; Name=6; (Potential).
FT   TOPO_DOM    264    271       Extracellular.
FT   TRANSMEM    272    295       Helical; Name=7; (Potential).
FT   TOPO_DOM    296    399       Cytoplasmic.
FT   MOD_RES     282    282       N6-(retinylidene)lysine.
FT   CARBOHYD      6      6       N-linked (GlcNAc...) (Potential).
FT   DISULFID     92    169       By similarity.
SQ   SEQUENCE   399 AA;  45097 MW;  5AA6857ABC912100 CRC64;
     MPFPLNRTDT ALVISPSEFR IIGIFISICC IIGVLGNLLI IIVFAKRRSV RRPINFFVLN
     LAVSDLIVAL LGYPMTAASA FSNRWIFDNI GCKIYAFLCF NSGVISIMTH AALSFCRYII
     ICQYGYRKKI TQTTVLRTLF SIWSFAMFWT LSPLFGWSSY VIEVVPVSCS VNWYGHGLGD
     VSYTISVIVA VYVFPLSIIV FSYGMILQEK VCKDSRKNGI RAQQRYTPRF IQDIEQRVTF
     ISFLMMAAFM VAWTPYAIMS ALAIGSFNVE NSFAALPTLF AKASCAYNPF IYAFTNANFR
     DTVVEIMAPW TTRRVGVSTL PWPQVTYYPR RRTSAVNTTD IEFPDDNIFI VNSSVNGPTV
     KREKIVQRNP INVRLGIKIE PRDSRAATEN TFTADFSVI
//
ID   OPSD_HUMAN              Reviewed;         348 AA.
AC   P08100; Q16414; Q2M249;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   13-JUN-2012, entry version 145.
DE   RecName: Full=Rhodopsin;
DE   AltName: Full=Opsin-2;
GN   Name=RHO; Synonyms=OPN2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84272729; PubMed=6589631; DOI=10.1073/pnas.81.15.4851;
RA   Nathans J., Hogness D.S.;
RT   "Isolation and nucleotide sequence of the gene encoding human
RT   rhodopsin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
RA   Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
RT   "Genome-wide discovery and analysis of human seven transmembrane helix
RT   receptor genes.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120.
RX   PubMed=8566799; DOI=10.1016/0378-1119(95)00688-5;
RA   Bennett J., Beller B., Sun D., Kariko K.;
RT   "Sequence analysis of the 5.34-kb 5' flanking region of the human
RT   rhodopsin-encoding gene.";
RL   Gene 167:317-320(1995).
RN   [6]
RP   REVIEW ON RP4 VARIANTS.
RX   MEDLINE=94004905; PubMed=8401533; DOI=10.1002/humu.1380020403;
RA   Al-Maghtheh M., Gregory C., Inglehearn C., Hardcastle A.,
RA   Bhattacharya S.;
RT   "Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
RL   Hum. Mutat. 2:249-255(1993).
RN   [7]
RP   VARIANTS RP4.
RX   MEDLINE=91051574; PubMed=2239971;
RA   Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G.,
RA   Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M.,
RA   Watty A., Ludwig M., Schinzel A., Samanns C., Gal A.,
RA   Bhattacharya S.S., Humphries P.;
RT   "Autosomal dominant retinitis pigmentosa: absence of the rhodopsin
RT   proline-->histidine substitution (codon 23) in pedigrees from
RT   Europe.";
RL   Am. J. Hum. Genet. 47:941-945(1990).
RN   [8]
RP   VARIANT RP4 HIS-23.
RX   MEDLINE=90136922; PubMed=2137202; DOI=10.1038/343364a0;
RA   Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S.,
RA   Yandell D.W., Sandberg M.A., Berson E.L.;
RT   "A point mutation of the rhodopsin gene in one form of retinitis
RT   pigmentosa.";
RL   Nature 343:364-366(1990).
RN   [9]
RP   VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347.
RX   MEDLINE=91015273; PubMed=2215617;
RA   Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E.,
RA   Reichel E., Sandberg M.A., Berson E.L.;
RT   "Mutations within the rhodopsin gene in patients with autosomal
RT   dominant retinitis pigmentosa.";
RL   N. Engl. J. Med. 323:1302-1307(1990).
RN   [10]
RP   VARIANT RP4 ILE-255 DEL.
RX   MEDLINE=91090106; PubMed=1985460;
RA   Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C.,
RA   Bhattacharya S.S.;
RT   "A 3-bp deletion in the rhodopsin gene in a family with autosomal
RT   dominant retinitis pigmentosa.";
RL   Am. J. Hum. Genet. 48:26-30(1991).
RN   [11]
RP   VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267.
RX   MEDLINE=91377732; PubMed=1897520;
RA   Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M.;
RT   "Identification of novel rhodopsin mutations associated with retinitis
RT   pigmentosa by GC-clamped denaturing gradient gel electrophoresis.";
RL   Am. J. Hum. Genet. 49:699-706(1991).
RN   [12]
RP   VARIANT RP4 ARG-347.
RX   MEDLINE=92120672; PubMed=1840561;
RA   Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E.,
RA   Schinzel A.;
RT   "Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant
RT   retinitis pigmentosa.";
RL   Genomics 11:468-470(1991).
RN   [13]
RP   VARIANTS RP4.
RX   MEDLINE=91319709; PubMed=1862076; DOI=10.1073/pnas.88.15.6481;
RA   Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H.,
RA   Jacobson S.G., Heckenlively J.R., Nowakowski R., Fishman G.,
RA   Gouras P., Nathans J.;
RT   "Rhodopsin mutations in autosomal dominant retinitis pigmentosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991).
RN   [14]
RP   VARIANTS RP4.
RX   MEDLINE=92021049; PubMed=1833777; DOI=10.1073/pnas.88.20.9370;
RA   Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L.;
RT   "Mutation spectrum of the rhodopsin gene among patients with autosomal
RT   dominant retinitis pigmentosa.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991).
RN   [15]
RP   VARIANT RP4 ARG-207.
RX   MEDLINE=93258325; PubMed=1302614; DOI=10.1093/hmg/1.9.769;
RA   Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M.,
RA   Sharpe E., Humphries P.;
RT   "Autosomal dominant retinitis pigmentosa: a novel mutation in the
RT   rhodopsin gene in the original 3q linked family.";
RL   Hum. Mol. Genet. 1:769-771(1992).
RN   [16]
RP   VARIANTS RP4 MET-17 AND LEU-347.
RX   MEDLINE=93004784; PubMed=1391967; DOI=10.1007/BF01899733;
RA   Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M.,
RA   Sakuma T., Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A.,
RA   Kanai A.;
RT   "Point mutations of rhodopsin gene found in Japanese families with
RT   autosomal dominant retinitis pigmentosa (ADRP).";
RL   Jpn. J. Hum. Genet. 37:125-132(1992).
RN   [17]
RP   VARIANTS RP4 ARG-106; GLY-135; SER-140; GLU-188 AND ARG-211, AND
RP   VARIANTS ALA-51; ILE-104 AND MET-209.
RX   MEDLINE=93304432; PubMed=8317502;
RA   Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C.,
RA   Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R.,
RA   Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J.;
RT   "Identification of novel rhodopsin mutations responsible for retinitis
RT   pigmentosa: implications for the structure and function of
RT   rhodopsin.";
RL   Am. J. Hum. Genet. 53:80-89(1993).
RN   [18]
RP   VARIANT RP4 SER-15.
RX   MEDLINE=93357759; PubMed=8353500; DOI=10.1093/hmg/2.6.813;
RA   Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P.,
RA   Duvigneau C., Gal A.;
RT   "Autosomal dominant 'sector' retinitis pigmentosa due to a point
RT   mutation predicting an Asn-15-Ser substitution of rhodopsin.";
RL   Hum. Mol. Genet. 2:813-814(1993).
RN   [19]
RP   VARIANT CSNBAD1 GLU-292.
RX   MEDLINE=93364423; PubMed=8358437; DOI=10.1038/ng0793-280;
RA   Dryja T.P., Berson E.L., Rao V.R., Oprian D.D.;
RT   "Heterozygous missense mutation in the rhodopsin gene as a cause of
RT   congenital stationary night blindness.";
RL   Nat. Genet. 4:280-283(1993).
RN   [20]
RP   VARIANTS RP4.
RX   MEDLINE=94375083; PubMed=8088850; DOI=10.1006/geno.1994.1301;
RA   Vaithinathan R., Berson E.L., Dryja T.P.;
RT   "Further screening of the rhodopsin gene in patients with autosomal
RT   dominant retinitis pigmentosa.";
RL   Genomics 21:461-463(1994).
RN   [21]
RP   VARIANT RP4 THR-44.
RX   MEDLINE=94357587; PubMed=8076945; DOI=10.1007/BF00208284;
RA   Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C.,
RA   Carballo M.;
RT   "Identification of a novel rhodopsin mutation (Met-44-Thr) in a
RT   simplex case of retinitis pigmentosa.";
RL   Hum. Genet. 94:283-286(1994).
RN   [22]
RP   VARIANTS RP4 PHE-110; PRO-131 AND VAL-164.
RX   MEDLINE=95072600; PubMed=7981701; DOI=10.1093/hmg/3.7.1203;
RA   Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S.,
RA   Humphries P., Gal A.;
RT   "Three novel rhodopsin mutations (C110F, L131P, A164V) in patients
RT   with autosomal dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1203-1203(1994).
RN   [23]
RP   VARIANT RP4 GLN-171.
RX   MEDLINE=95078852; PubMed=7987326; DOI=10.1093/hmg/3.8.1421;
RA   Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P.,
RA   Cabeza J.C.;
RT   "Identification of a new mutation at codon 171 of rhodopsin gene
RT   causing autosomal dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1421-1421(1994).
RN   [24]
RP   VARIANTS RP4 PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297.
RX   MEDLINE=95078858; PubMed=7987331; DOI=10.1093/hmg/3.8.1433;
RA   Souied E., Gerber S., Rozet J.-M., Bonneau D., Dufier J.-L., Ghazi I.,
RA   Philip N., Soubrane G., Coscas G., Munnich A.;
RT   "Five novel missense mutations of the rhodopsin gene in autosomal
RT   dominant retinitis pigmentosa.";
RL   Hum. Mol. Genet. 3:1433-1434(1994).
RN   [25]
RP   VARIANTS RP4 ARG-40 AND LYS-216.
RX   MEDLINE=94362717; PubMed=8081400; DOI=10.1002/humu.1380030417;
RA   Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A.,
RA   Bhattacharya S.;
RT   "Two new rhodopsin transversion mutations (L40R; M216K) in families
RT   with autosomal dominant retinitis pigmentosa.";
RL   Hum. Mutat. 3:409-410(1994).
RN   [26]
RP   VARIANT RP4 LEU-345.
RX   MEDLINE=94321123; PubMed=8045708;
RA   Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J.;
RT   "Autosomal dominant retinitis pigmentosa in a large family: a clinical
RT   and molecular genetic study.";
RL   Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994).
RN   [27]
RP   VARIANT ARRP LYS-150.
RX   MEDLINE=95078913; PubMed=7987385; DOI=10.1038/ng0994-10;
RA   Kumaramanickavel G., Maw M., Denton M.J., John S., Srikumari C.R.,
RA   Orth U., Oehlmann R., Gal A.;
RT   "Missense rhodopsin mutation in a family with recessive RP.";
RL   Nat. Genet. 8:10-11(1994).
RN   [28]
RP   VARIANT RP4 ALA-347.
RX   MEDLINE=95359993; PubMed=7633434; DOI=10.1093/hmg/4.4.775;
RA   Macke J.P., Hennessey J.C., Nathans J.;
RT   "Rhodopsin mutation proline347-to-alanine in a family with autosomal
RT   dominant retinitis pigmentosa indicates an important role for proline
RT   at position 347.";
RL   Hum. Mol. Genet. 4:775-776(1995).
RN   [29]
RP   VARIANT CSNBAD1 ASP-90.
RX   MEDLINE=95148641; PubMed=7846071; DOI=10.1073/pnas.92.3.880;
RA   Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K.,
RA   Alpern M.;
RT   "Dark-light: model for nightblindness from the human rhodopsin Gly-
RT   90-->Asp mutation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995).
RN   [30]
RP   VARIANT RP4 TRP-135.
RX   MEDLINE=96142043; PubMed=8554077;
RA   Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S.,
RA   Munnich A., Kaplan J.;
RT   "Retinitis punctata albescens associated with the Arg135Trp mutation
RT   in the rhodopsin gene.";
RL   Am. J. Ophthalmol. 121:19-25(1996).
RN   [31]
RP   VARIANT RP4 ARG-109.
RX   MEDLINE=98112414; PubMed=9452035;
RA   Goliath R., Bardien S., September A., Martin R., Ramesar R.,
RA   Greenberg J.;
RT   "Rhodopsin mutation G109R in a family with autosomal dominant
RT   retinitis pigmentosa.";
RL   Hum. Mutat. Suppl. 1:S40-S41(1998).
RN   [32]
RP   VARIANT CSNBAD1 ILE-94.
RX   MEDLINE=99103467; PubMed=9888392;
RX   DOI=10.1002/(SICI)1098-1004(1999)13:1<75::AID-HUMU9>3.0.CO;2-4;
RA   Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N.,
RA   Findlay J.B.C., Humphries P., Kenna P.F.;
RT   "A novel mutation within the rhodopsin gene (Thr-94-Ile) causing
RT   autosomal dominant congenital stationary night blindness.";
RL   Hum. Mutat. 13:75-81(1999).
RN   [33]
RP   CHARACTERIZATION OF VARIANT RP4 HIS-23, AND SUBCELLULAR LOCATION.
RX   PubMed=19934218; DOI=10.1242/jcs.055228;
RA   Kosmaoglou M., Kanuga N., Aguila M., Garriga P., Cheetham M.E.;
RT   "A dual role for EDEM1 in the processing of rod opsin.";
RL   J. Cell Sci. 122:4465-4472(2009).
RN   [34]
RP   VARIANT RP4 LYS-150.
RX   PubMed=19960070;
RA   Azam M., Khan M.I., Gal A., Hussain A., Shah S.T., Khan M.S.,
RA   Sadeque A., Bokhari H., Collin R.W., Orth U., van Genderen M.M.,
RA   den Hollander A.I., Cremers F.P., Qamar R.;
RT   "A homozygous p.Glu150Lys mutation in the opsin gene of two Pakistani
RT   families with autosomal recessive retinitis pigmentosa.";
RL   Mol. Vis. 15:2526-2534(2009).
CC   -!- FUNCTION: Photoreceptor required for image-forming vision at low
CC       light intensity. Required for photoreceptor cell viability after
CC       birth. Light-induced isomerization of 11-cis to all-trans retinal
CC       triggers a conformational change leading to G-protein activation
CC       and release of all-trans retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=495 nm;
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- INTERACTION:
CC       O95405:ZFYVE9; NbExp=2; IntAct=EBI-1394177, EBI-296817;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC       Note=Synthesized in the inner segment (IS) of rod photoreceptor
CC       cells before vectorial transport to the rod outer segment (OS)
CC       photosensory cilia.
CC   -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates
CC       vision in dim light.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC   -!- PTM: Contains one covalently linked retinal chromophore (By
CC       similarity).
CC   -!- DISEASE: Defects in RHO are the cause of retinitis pigmentosa type
CC       4 (RP4) [MIM:613731]. RP leads to degeneration of retinal
CC       photoreceptor cells. Patients typically have night vision
CC       blindness and loss of midperipheral visual field. As their
CC       condition progresses, they lose their far peripheral visual field
CC       and eventually central vision as well.
CC   -!- DISEASE: Defects in RHO are the cause of congenital stationary
CC       night blindness autosomal dominant type 1 (CSNBAD1) [MIM:610445];
CC       also known as rhodopsin-related congenital stationary night
CC       blindness. Congenital stationary night blindness is a non-
CC       progressive retinal disorder characterized by impaired night
CC       vision.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -!- WEB RESOURCE: Name=Mutations of the RHO gene; Note=Retina
CC       International's Scientific Newsletter;
CC       URL="http://www.retina-international.org/files/sci-news/rhomut.htm";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/RHO";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Rhodopsin entry;
CC       URL="http://en.wikipedia.org/wiki/Rhodopsin";
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DR   EMBL; U49742; AAC31763.1; -; Genomic_DNA.
DR   EMBL; AB065668; BAC05894.1; -; Genomic_DNA.
DR   EMBL; BX537381; CAD97623.1; -; mRNA.
DR   EMBL; BC112104; AAI12105.1; -; mRNA.
DR   EMBL; BC112106; AAI12107.1; -; mRNA.
DR   EMBL; U16824; AAA97436.1; -; Genomic_DNA.
DR   EMBL; S81166; AAB35906.1; -; Genomic_DNA.
DR   IPI; IPI00027391; -.
DR   PIR; A41200; OOHU.
DR   RefSeq; NP_000530.1; NM_000539.3.
DR   UniGene; Hs.247565; -.
DR   ProteinModelPortal; P08100; -.
DR   SMR; P08100; 1-348.
DR   IntAct; P08100; 3.
DR   STRING; P08100; -.
DR   GlycoSuiteDB; P08100; -.
DR   PhosphoSite; P08100; -.
DR   DMDM; 129207; -.
DR   PRIDE; P08100; -.
DR   DNASU; 6010; -.
DR   Ensembl; ENST00000296271; ENSP00000296271; ENSG00000163914.
DR   GeneID; 6010; -.
DR   KEGG; hsa:6010; -.
DR   UCSC; uc003emt.3; human.
DR   CTD; 6010; -.
DR   GeneCards; GC03P129247; -.
DR   HGNC; HGNC:10012; RHO.
DR   MIM; 180380; gene.
DR   MIM; 610445; phenotype.
DR   MIM; 613731; phenotype.
DR   neXtProt; NX_P08100; -.
DR   Orphanet; 215; Congenital stationary night blindness.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   Orphanet; 52427; Retinitis punctata albescens.
DR   PharmGKB; PA34390; -.
DR   eggNOG; NOG311294; -.
DR   GeneTree; ENSGT00550000074069; -.
DR   HOGENOM; HOG000253932; -.
DR   HOVERGEN; HBG107442; -.
DR   InParanoid; P08100; -.
DR   KO; K04250; -.
DR   OMA; KSSSIYN; -.
DR   OrthoDB; EOG4P5K9D; -.
DR   PhylomeDB; P08100; -.
DR   Pathway_Interaction_DB; rhodopsin_pathway; Visual signal transduction: Rods.
DR   Reactome; REACT_111102; Signal Transduction.
DR   DrugBank; DB01159; Halothane.
DR   NextBio; 23449; -.
DR   ArrayExpress; P08100; -.
DR   Bgee; P08100; -.
DR   CleanEx; HS_RHO; -.
DR   Genevestigator; P08100; -.
DR   GermOnline; ENSG00000163914; Homo sapiens.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR   GO; GO:0060342; C:photoreceptor inner segment membrane; IDA:UniProtKB.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:UniProtKB.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:ProtInc.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000732; Rhodopsin.
DR   InterPro; IPR019477; Rhodopsin_N.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF10413; Rhodopsin_N; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromophore; Complete proteome;
KW   Congenital stationary night blindness; Disease mutation;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW   Membrane; Metal-binding; Palmitate; Phosphoprotein;
KW   Photoreceptor protein; Polymorphism; Receptor; Reference proteome;
KW   Retinal protein; Retinitis pigmentosa; Sensory transduction;
KW   Transducer; Transmembrane; Transmembrane helix; Vision; Zinc.
FT   CHAIN         1    348       Rhodopsin.
FT                                /FTId=PRO_0000197677.
FT   TOPO_DOM      1     36       Extracellular.
FT   TRANSMEM     37     61       Helical; Name=1; (Potential).
FT   TOPO_DOM     62     73       Cytoplasmic.
FT   TRANSMEM     74     98       Helical; Name=2; (Potential).
FT   TOPO_DOM     99    113       Extracellular.
FT   TRANSMEM    114    133       Helical; Name=3; (Potential).
FT   TOPO_DOM    134    152       Cytoplasmic.
FT   TRANSMEM    153    176       Helical; Name=4; (Potential).
FT   TOPO_DOM    177    202       Extracellular.
FT   TRANSMEM    203    230       Helical; Name=5; (Potential).
FT   TOPO_DOM    231    252       Cytoplasmic.
FT   TRANSMEM    253    276       Helical; Name=6; (Potential).
FT   TOPO_DOM    277    284       Extracellular.
FT   TRANSMEM    285    309       Helical; Name=7; (Potential).
FT   TOPO_DOM    310    348       Cytoplasmic.
FT   REGION      113    125       Retinal chromophore binding (By
FT                                similarity).
FT   REGION      207    212       Retinal chromophore binding (By
FT                                similarity).
FT   MOTIF       134    137       'Ionic lock' involved in activated form
FT                                stabilization.
FT   METAL       201    201       Zinc (By similarity).
FT   METAL       279    279       Zinc (By similarity).
FT   BINDING     265    265       Retinal chromophore (By similarity).
FT   BINDING     296    296       Retinal chromophore (covalent) (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     296    296       N6-(retinylidene)lysine.
FT   MOD_RES     334    334       Phosphoserine (By similarity).
FT   MOD_RES     336    336       Phosphothreonine (By similarity).
FT   MOD_RES     338    338       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphothreonine (By similarity).
FT   MOD_RES     342    342       Phosphothreonine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   LIPID       322    322       S-palmitoyl cysteine (By similarity).
FT   LIPID       323    323       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD      2      2       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD     15     15       N-linked (GlcNAc...) (By similarity).
FT   DISULFID    110    187       By similarity.
FT   VARIANT       4      4       T -> K (in RP4).
FT                                /FTId=VAR_004765.
FT   VARIANT      15     15       N -> S (in RP4).
FT                                /FTId=VAR_004766.
FT   VARIANT      17     17       T -> M (in RP4).
FT                                /FTId=VAR_004767.
FT   VARIANT      23     23       P -> H (in RP4; most common variant,
FT                                leads to interaction with EDEM1 followed
FT                                by degradation by the ERAD system).
FT                                /FTId=VAR_004768.
FT   VARIANT      23     23       P -> L (in RP4).
FT                                /FTId=VAR_004769.
FT   VARIANT      28     28       Q -> H (in RP4).
FT                                /FTId=VAR_004770.
FT   VARIANT      40     40       L -> R (in RP4).
FT                                /FTId=VAR_004771.
FT   VARIANT      44     44       M -> T (in RP4).
FT                                /FTId=VAR_004772.
FT   VARIANT      45     45       F -> L (in RP4).
FT                                /FTId=VAR_004773.
FT   VARIANT      46     46       L -> R (in RP4).
FT                                /FTId=VAR_004774.
FT   VARIANT      51     51       G -> A.
FT                                /FTId=VAR_004775.
FT   VARIANT      51     51       G -> R (in RP4).
FT                                /FTId=VAR_004776.
FT   VARIANT      51     51       G -> V (in RP4).
FT                                /FTId=VAR_004777.
FT   VARIANT      53     53       P -> R (in RP4; dbSNP:rs28933395).
FT                                /FTId=VAR_004778.
FT   VARIANT      58     58       T -> R (in RP4; dbSNP:rs28933394).
FT                                /FTId=VAR_004779.
FT   VARIANT      68     71       Missing (in RP4).
FT                                /FTId=VAR_004780.
FT   VARIANT      87     87       V -> D (in RP4).
FT                                /FTId=VAR_004781.
FT   VARIANT      89     89       G -> D (in RP4).
FT                                /FTId=VAR_004782.
FT   VARIANT      90     90       G -> D (in CSNBAD1).
FT                                /FTId=VAR_004783.
FT   VARIANT      94     94       T -> I (in CSNBAD1).
FT                                /FTId=VAR_004784.
FT   VARIANT     104    104       V -> I.
FT                                /FTId=VAR_004785.
FT   VARIANT     106    106       G -> R (in RP4; dbSNP:rs28933994).
FT                                /FTId=VAR_004786.
FT   VARIANT     106    106       G -> W (in RP4).
FT                                /FTId=VAR_004787.
FT   VARIANT     109    109       G -> R (in RP4).
FT                                /FTId=VAR_004788.
FT   VARIANT     110    110       C -> F (in RP4).
FT                                /FTId=VAR_004789.
FT   VARIANT     110    110       C -> Y (in RP4).
FT                                /FTId=VAR_004790.
FT   VARIANT     114    114       G -> D (in RP4).
FT                                /FTId=VAR_004791.
FT   VARIANT     125    125       L -> R (in RP4).
FT                                /FTId=VAR_004792.
FT   VARIANT     127    127       S -> F (in RP4).
FT                                /FTId=VAR_004793.
FT   VARIANT     131    131       L -> P (in RP4).
FT                                /FTId=VAR_004794.
FT   VARIANT     135    135       R -> G (in RP4).
FT                                /FTId=VAR_004795.
FT   VARIANT     135    135       R -> L (in RP4).
FT                                /FTId=VAR_004796.
FT   VARIANT     135    135       R -> W (in RP4).
FT                                /FTId=VAR_004797.
FT   VARIANT     140    140       C -> S (in RP4).
FT                                /FTId=VAR_004798.
FT   VARIANT     150    150       E -> K (in RP4; autosomal recessive).
FT                                /FTId=VAR_004799.
FT   VARIANT     164    164       A -> E (in RP4).
FT                                /FTId=VAR_004800.
FT   VARIANT     164    164       A -> V (in RP4).
FT                                /FTId=VAR_004801.
FT   VARIANT     167    167       C -> R (in RP4).
FT                                /FTId=VAR_004802.
FT   VARIANT     171    171       P -> L (in RP4).
FT                                /FTId=VAR_004803.
FT   VARIANT     171    171       P -> Q (in RP4).
FT                                /FTId=VAR_004804.
FT   VARIANT     171    171       P -> S (in RP4).
FT                                /FTId=VAR_004805.
FT   VARIANT     178    178       Y -> C (in RP4).
FT                                /FTId=VAR_004806.
FT   VARIANT     178    178       Y -> N (in RP4).
FT                                /FTId=VAR_004807.
FT   VARIANT     181    181       E -> K (in RP4).
FT                                /FTId=VAR_004808.
FT   VARIANT     182    182       G -> S (in RP4).
FT                                /FTId=VAR_004809.
FT   VARIANT     186    186       S -> P (in RP4).
FT                                /FTId=VAR_004810.
FT   VARIANT     188    188       G -> E (in RP4).
FT                                /FTId=VAR_004811.
FT   VARIANT     188    188       G -> R (in RP4).
FT                                /FTId=VAR_004812.
FT   VARIANT     190    190       D -> G (in RP4).
FT                                /FTId=VAR_004814.
FT   VARIANT     190    190       D -> N (in RP4; dbSNP:rs28933992).
FT                                /FTId=VAR_004813.
FT   VARIANT     190    190       D -> Y (in RP4).
FT                                /FTId=VAR_004815.
FT   VARIANT     207    207       M -> R (in RP4; dbSNP:rs28933995).
FT                                /FTId=VAR_004816.
FT   VARIANT     209    209       V -> M (effect not known).
FT                                /FTId=VAR_004817.
FT   VARIANT     211    211       H -> P (in RP4; dbSNP:rs28933993).
FT                                /FTId=VAR_004818.
FT   VARIANT     211    211       H -> R (in RP4).
FT                                /FTId=VAR_004819.
FT   VARIANT     216    216       M -> K (in RP4).
FT                                /FTId=VAR_004820.
FT   VARIANT     220    220       F -> C (in RP4).
FT                                /FTId=VAR_004821.
FT   VARIANT     222    222       C -> R (in RP4).
FT                                /FTId=VAR_004822.
FT   VARIANT     255    255       Missing (in RP4).
FT                                /FTId=VAR_004823.
FT   VARIANT     264    264       Missing (in RP4).
FT                                /FTId=VAR_004824.
FT   VARIANT     267    267       P -> L (in RP4).
FT                                /FTId=VAR_004825.
FT   VARIANT     267    267       P -> R (in RP4).
FT                                /FTId=VAR_004826.
FT   VARIANT     292    292       A -> E (in CSNBAD1).
FT                                /FTId=VAR_004827.
FT   VARIANT     296    296       K -> E (in RP4; dbSNP:rs29001653).
FT                                /FTId=VAR_004828.
FT   VARIANT     297    297       S -> R (in RP4).
FT                                /FTId=VAR_004829.
FT   VARIANT     342    342       T -> M (in RP4).
FT                                /FTId=VAR_004830.
FT   VARIANT     345    345       V -> L (in RP4).
FT                                /FTId=VAR_004831.
FT   VARIANT     345    345       V -> M (in RP4).
FT                                /FTId=VAR_004832.
FT   VARIANT     347    347       P -> A (in RP4).
FT                                /FTId=VAR_004833.
FT   VARIANT     347    347       P -> L (in RP4; common variant).
FT                                /FTId=VAR_004834.
FT   VARIANT     347    347       P -> Q (in RP4).
FT                                /FTId=VAR_004835.
FT   VARIANT     347    347       P -> R (in RP4; dbSNP:rs29001566).
FT                                /FTId=VAR_004836.
FT   VARIANT     347    347       P -> S (in RP4; dbSNP:rs29001637).
FT                                /FTId=VAR_004837.
SQ   SEQUENCE   348 AA;  38893 MW;  6F4F6FCBA34265B2 CRC64;
     MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
     VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG
     GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP
     EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES
     ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI
     YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA
//
ID   OPSD_XENLA              Reviewed;         354 AA.
AC   P29403;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   30-NOV-2010, entry version 75.
DE   RecName: Full=Rhodopsin;
GN   Name=rho;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93287804; PubMed=8510503; DOI=10.1016/0169-328X(93)90016-I;
RA   Saha M.S., Grainger R.M.;
RT   "Early opsin expression in Xenopus embryos precedes photoreceptor
RT   differentiation.";
RL   Brain Res. Mol. Brain Res. 17:307-318(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=96216396; PubMed=8621718; DOI=10.1074/jbc.271.6.3179;
RA   Batni S., Scalzetti L.C., Moody S.A., Knox B.E.;
RT   "Characterization of the Xenopus rhodopsin gene.";
RL   J. Biol. Chem. 271:3179-3186(1996).
CC   -!- FUNCTION: Visual pigments such as rhodopsin and porphyropsin are
CC       light-absorbing molecules that mediate vision. Rhodopsin consists
CC       of an apoprotein, opsin, covalently linked to 11-cis-retinal. This
CC       receptor is coupled to the activation of phospholipase C.
CC       Porphyropsin consists of opsin covalently linked to 11-cis 3,4-
CC       didehydroretinal.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates
CC       vision in dim light.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; S62229; AAB27128.2; -; mRNA.
DR   EMBL; L04692; AAB59950.1; -; mRNA.
DR   EMBL; L07770; AAC42232.1; -; mRNA.
DR   EMBL; U23808; AAC59901.1; -; Genomic_DNA.
DR   PIR; I51200; I51200.
DR   UniGene; Xl.326; -.
DR   ProteinModelPortal; P29403; -.
DR   SMR; P29403; 1-354.
DR   MINT; MINT-6824795; -.
DR   Xenbase; XB-GENE-966893; rho.
DR   HOVERGEN; HBG107442; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR000732; Rhodopsin.
DR   InterPro; IPR019477; Rhodopsin_N.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF10413; Rhodopsin_N; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00579; RHODOPSIN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Photoreceptor protein; Receptor; Retinal protein;
KW   Sensory transduction; Transducer; Transmembrane; Transmembrane helix;
KW   Vision.
FT   CHAIN         1    354       Rhodopsin.
FT                                /FTId=PRO_0000197727.
FT   TOPO_DOM      1     36       Extracellular.
FT   TRANSMEM     37     61       Helical; Name=1; (Potential).
FT   TOPO_DOM     62     73       Cytoplasmic.
FT   TRANSMEM     74     98       Helical; Name=2; (Potential).
FT   TOPO_DOM     99    113       Extracellular.
FT   TRANSMEM    114    133       Helical; Name=3; (Potential).
FT   TOPO_DOM    134    152       Cytoplasmic.
FT   TRANSMEM    153    176       Helical; Name=4; (Potential).
FT   TOPO_DOM    177    202       Extracellular.
FT   TRANSMEM    203    230       Helical; Name=5; (Potential).
FT   TOPO_DOM    231    252       Cytoplasmic.
FT   TRANSMEM    253    276       Helical; Name=6; (Potential).
FT   TOPO_DOM    277    284       Extracellular.
FT   TRANSMEM    285    309       Helical; Name=7; (Potential).
FT   TOPO_DOM    310    354       Cytoplasmic.
FT   MOD_RES     296    296       N6-(retinylidene)lysine.
FT   LIPID       322    322       S-palmitoyl cysteine (By similarity).
FT   LIPID       323    323       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD      2      2       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD     15     15       N-linked (GlcNAc...) (By similarity).
FT   DISULFID    110    187       By similarity.
FT   CONFLICT    107    107       P -> Q (in Ref. 2; AAC42232/AAC59901).
FT   CONFLICT    137    137       I -> M (in Ref. 2; AAC42232/AAC59901).
FT   CONFLICT    241    241       L -> A (in Ref. 2; AAC42232/AAC59901).
SQ   SEQUENCE   354 AA;  39787 MW;  CD18F49EC63D8FFE CRC64;
     MNGTEGPNFY VPMSNKTGVV RSPFDYPQYY LAEPWQYSAL AAYMFLLILL GLPINFMTLF
     VTIQHKKLRT PLNYILLNLV FANHFMVLCG FTVTMYTSMH GYFIFGPTGC YIEGFFATLG
     GEVALWSLVV LAVERYIVVC KPMANFRFGE NHAIMGVAFT WIMALSCAAP PLFGWSRYIP
     EGMQCSCGVD YYTLKPEVNN ESFVIYMFIV HFTIPLIVIF FCYGRLLCTV KEAAAQQQES
     LTTQKAEKEV TRMVVIMVVF FLICWVPYAY VAFYIFTHQG SNFGPVFMTV PAFFAKSSAI
     YNPVIYIVLN KQFRNCLITT LCCGKNPFGD EDGSSAATSK TEASSVSSSQ VSPA
//
ID   OPSO_LIMPO              Reviewed;         376 AA.
AC   P35361;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   21-SEP-2011, entry version 61.
DE   RecName: Full=Ocellar opsin;
OS   Limulus polyphemus (Atlantic horseshoe crab).
OC   Eukaryota; Metazoa; Arthropoda; Chelicerata; Merostomata; Xiphosura;
OC   Limulidae; Limulus.
OX   NCBI_TaxID=6850;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Median ocelli;
RX   MEDLINE=93317641; PubMed=8327495; DOI=10.1073/pnas.90.13.6150;
RA   Smith W.C., Price D.A., Greenberg R.M., Battelle B.-A.;
RT   "Opsins from the lateral eyes and ocelli of the horseshoe crab,
RT   Limulus polyphemus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6150-6154(1993).
CC   -!- FUNCTION: Visual pigments are the light-absorbing molecules that
CC       mediate vision. They consist of an apoprotein, opsin, covalently
CC       linked to cis-retinal.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Absorption:
CC         Abs(max)=530 nm;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Ocellar cells; median ocelli.
CC   -!- PTM: Phosphorylated on some or all of the serine and threonine
CC       residues present in the C-terminal region (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Opsin subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; L03792; AAA28274.1; -; mRNA.
DR   EMBL; L03782; AAA02499.1; -; mRNA.
DR   PIR; A48197; A48197.
DR   ProteinModelPortal; P35361; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007602; P:phototransduction; IEA:UniProtKB-KW.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001760; Opsin.
DR   InterPro; IPR001391; Opsin_lateye.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00238; OPSIN.
DR   PRINTS; PR00578; OPSINLTRLEYE.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   PROSITE; PS00238; OPSIN; 1.
PE   1: Evidence at protein level;
KW   Chromophore; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Photoreceptor protein; Receptor;
KW   Retinal protein; Sensory transduction; Transducer; Transmembrane;
KW   Transmembrane helix; Vision.
FT   CHAIN         1    376       Ocellar opsin.
FT                                /FTId=PRO_0000197752.
FT   TOPO_DOM      1     46       Extracellular.
FT   TRANSMEM     47     71       Helical; Name=1; (Potential).
FT   TOPO_DOM     72     83       Cytoplasmic.
FT   TRANSMEM     84    108       Helical; Name=2; (Potential).
FT   TOPO_DOM    109    123       Extracellular.
FT   TRANSMEM    124    143       Helical; Name=3; (Potential).
FT   TOPO_DOM    144    162       Cytoplasmic.
FT   TRANSMEM    163    186       Helical; Name=4; (Potential).
FT   TOPO_DOM    187    210       Extracellular.
FT   TRANSMEM    211    238       Helical; Name=5; (Potential).
FT   TOPO_DOM    239    274       Cytoplasmic.
FT   TRANSMEM    275    298       Helical; Name=6; (Potential).
FT   TOPO_DOM    299    306       Extracellular.
FT   TRANSMEM    307    331       Helical; Name=7; (Potential).
FT   TOPO_DOM    332    376       Cytoplasmic.
FT   MOD_RES     318    318       N6-(retinylidene)lysine (By similarity).
FT   CARBOHYD     17     17       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    193    193       N-linked (GlcNAc...) (Potential).
FT   DISULFID    120    197       By similarity.
SQ   SEQUENCE   376 AA;  42112 MW;  FA9647C40531CBF8 CRC64;
     MANQLSYSSL GWPYQPNASV VDTMPKEMLY MIHEHWYAFP PMNPLWYSIL GVAMIILGII
     CVLGNGMVIY LMMTTKSLRT PTNLLVVNLA FSDFCMMAFM MPTMASNCFA ETWILGPFMC
     EVYGMAGSLF GCASIWSMVM ITLDRYNVIV RGMAAAPLTH KKATLLLLFV WIWSGGWTIL
     PFFGWSRYVP EGNLTSCTVD YLTKDWSSAS YVIIYGLAVY FLPLITMIYC YFFIVHAVAE
     HEKQLREQAK KMNVASLRAN ADQQKQSAEC RLAKVAMMTV GLWFMAWTPY LIIAWAGVFS
     SGTRLTPLAT IWGSVFAKAN SCYNPIVYGI SHPRYKAALY QRFPSLACGS GESGSDVKSE
     ASATMTMEEK PKSPEA
//
ID   PAX1_HUMAN              Reviewed;         534 AA.
AC   P15863; B4E0D6; Q642X9; Q6NTC0; Q9Y558;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 4.
DT   13-JUN-2012, entry version 116.
DE   RecName: Full=Paired box protein Pax-1;
DE   AltName: Full=HuP48;
GN   Name=PAX1; Synonyms=HUP48;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3), AND VARIANTS ARG-439;
RP   LEU-453 AND LEU-504.
RG   NIEHS SNPs program;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-534 (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2/3).
RX   MEDLINE=89305521; PubMed=2501086;
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
RN   [6]
RP   VARIANT HIS-139.
RX   MEDLINE=97016531; PubMed=8863157;
RA   Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R.,
RA   Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "PAX genes and human neural tube defects: an amino acid substitution
RT   in PAX1 in a patient with spina bifida.";
RL   J. Med. Genet. 33:655-660(1996).
CC   -!- FUNCTION: This protein is a transcriptional activator. It may play
CC       a role in the formation of segmented structures of the embryo. May
CC       play an important role in the normal development of the vertebral
CC       column (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P15863-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15863-2; Sequence=VSP_039095, VSP_039096;
CC       Name=3;
CC         IsoId=P15863-3; Sequence=VSP_039095;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH69134.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAU21037.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/pax1/";
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK303335; BAG64398.1; -; mRNA.
DR   EMBL; AY740018; AAU21037.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL035562; CAX12115.1; -; Genomic_DNA.
DR   EMBL; AL035562; CAB46996.2; -; Genomic_DNA.
DR   EMBL; BC069134; AAH69134.1; ALT_INIT; mRNA.
DR   EMBL; X15044; CAA33146.1; -; Genomic_DNA.
DR   IPI; IPI00013473; -.
DR   IPI; IPI00419577; -.
DR   IPI; IPI00963849; -.
DR   PIR; S06961; S06961.
DR   RefSeq; NP_006183.2; NM_006192.4.
DR   UniGene; Hs.349082; -.
DR   ProteinModelPortal; P15863; -.
DR   SMR; P15863; 102-224.
DR   MINT; MINT-202824; -.
DR   STRING; P15863; -.
DR   DMDM; 296439493; -.
DR   PRIDE; P15863; -.
DR   Ensembl; ENST00000377123; ENSP00000366327; ENSG00000125813.
DR   Ensembl; ENST00000398485; ENSP00000381499; ENSG00000125813.
DR   Ensembl; ENST00000444366; ENSP00000410355; ENSG00000125813.
DR   GeneID; 5075; -.
DR   KEGG; hsa:5075; -.
DR   UCSC; uc002wsj.2; human.
DR   UCSC; uc010zsm.2; human.
DR   CTD; 5075; -.
DR   GeneCards; GC20P021634; -.
DR   H-InvDB; HIX0040597; -.
DR   HGNC; HGNC:8615; PAX1.
DR   MIM; 167411; gene.
DR   neXtProt; NX_P15863; -.
DR   PharmGKB; PA32955; -.
DR   eggNOG; NOG252808; -.
DR   GeneTree; ENSGT00650000093055; -.
DR   HOGENOM; HOG000230938; -.
DR   HOVERGEN; HBG009115; -.
DR   InParanoid; P15863; -.
DR   KO; K09382; -.
DR   OMA; AMAFKHP; -.
DR   OrthoDB; EOG4W6NW9; -.
DR   NextBio; 19556; -.
DR   ArrayExpress; P15863; -.
DR   Bgee; P15863; -.
DR   CleanEx; HS_PAX1; -.
DR   Genevestigator; P15863; -.
DR   GermOnline; ENSG00000125813; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; Complete proteome;
KW   Developmental protein; DNA-binding; Nucleus; Paired box; Polymorphism;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN         1    534       Paired box protein Pax-1.
FT                                /FTId=PRO_0000050172.
FT   DOMAIN       98    224       Paired.
FT   VAR_SEQ       1     95       MKFTLGLGSRAWRVSWEGAAAAAAGPGAGGSALRCRAQRVS
FT                                SPRLGRRGSRLSGALPLCLSRGGGGAQALPDCAGPSPGHPG
FT                                HPGARQLAGPLAM -> MRRAPLRGSSAPLPTPSQTQAVCP
FT                                WTPSCLGTHRSPLEVRLGAVPRSAWGPLANPPGVFSPSGSL
FT                                LSGASA (in isoform 2 and isoform 3).
FT                                /FTId=VSP_039095.
FT   VAR_SEQ     428    534       GSLPAPAARPRTPSVAYTDCPSRPRPPRGSSPRTRARRERQ
FT                                ADPGAQVCAAAPAIGTGRIGGLAEEEASAGPRGARPASPQA
FT                                QPCLWPDPPHFLYWSGFLGFSELGF -> VADRKPPSSGSK
FT                                APDALSSLHGLPIPASTS (in isoform 2).
FT                                /FTId=VSP_039096.
FT   VARIANT     139    139       Q -> H (in a patient with neural tube
FT                                defects, but not clearly linked to the
FT                                disease).
FT                                /FTId=VAR_003787.
FT   VARIANT     439    439       T -> R (in dbSNP:rs17861058).
FT                                /FTId=VAR_055369.
FT   VARIANT     453    453       P -> L (in dbSNP:rs17861059).
FT                                /FTId=VAR_055370.
FT   VARIANT     504    504       P -> L (in dbSNP:rs17861061).
FT                                /FTId=VAR_055371.
SQ   SEQUENCE   534 AA;  55499 MW;  6B06A2AD302FDEEA CRC64;
     MKFTLGLGSR AWRVSWEGAA AAAAGPGAGG SALRCRAQRV SSPRLGRRGS RLSGALPLCL
     SRGGGGAQAL PDCAGPSPGH PGHPGARQLA GPLAMEQTYG EVNQLGGVFV NGRPLPNAIR
     LRIVELAQLG IRPCDISRQL RVSHGCVSKI LARYNETGSI LPGAIGGSKP RVTTPNVVKH
     IRDYKQGDPG IFAWEIRDRL LADGVCDKYN VPSVSSISRI LRNKIGSLAQ PGPYEASKQP
     PSQPTLPYNH IYQYPYPSPV SPTGAKMGSH PGVPGTAGHV SIPRSWPSAH SVSNILGIRT
     FMEQTGALAG SEGTAYSPKM EDWAGVNRTA FPATPAVNGL EKPALEADIK YTQSASTLSA
     VGGFLPACAY PASNQHGVYS APGGGYLAPG PPWPPAQGPP LAPPGAGVAV HGGELAAAMT
     FKHPSREGSL PAPAARPRTP SVAYTDCPSR PRPPRGSSPR TRARRERQAD PGAQVCAAAP
     AIGTGRIGGL AEEEASAGPR GARPASPQAQ PCLWPDPPHF LYWSGFLGFS ELGF
//
ID   PAX2_HUMAN              Reviewed;         417 AA.
AC   Q02962; Q15105; Q15110; Q15837; Q5SZP2; Q5SZP3;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 4.
DT   13-JUN-2012, entry version 133.
DE   RecName: Full=Paired box protein Pax-2;
GN   Name=PAX2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Kidney;
RX   MEDLINE=92338102; PubMed=1378753;
RA   Eccles M.R., Wallis L.J., Fidler A.E., Spurr N.K., Goodfellow P.J.,
RA   Reeve A.E.;
RT   "Expression of the PAX2 gene in human fetal kidney and Wilms' tumor.";
RL   Cell Growth Differ. 3:279-289(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   TISSUE=Kidney cortex;
RX   PubMed=7819127;
RA   Ward T.A., Nebel A., Reeve A.E., Eccles M.R.;
RT   "Alternative messenger RNA forms and open reading frames within an
RT   additional conserved region of the human PAX-2 gene.";
RL   Cell Growth Differ. 5:1015-1021(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP   1).
RX   MEDLINE=96299768; PubMed=8661132; DOI=10.1006/geno.1996.0350;
RA   Sanyanusin P., Norrish J.H., Ward T.A., Nebel A., McNoe L.A.,
RA   Eccles M.R.;
RT   "Genomic structure of the human PAX2 gene.";
RL   Genomics 35:258-261(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
RX   MEDLINE=95072651; PubMed=7981748; DOI=10.1038/ng0493-292;
RA   Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.;
RT   "Chromosomal localization of seven PAX genes and cloning of a novel
RT   family member, PAX-9.";
RL   Nat. Genet. 3:292-298(1993).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   INTERACTION WITH EGLN3.
RX   PubMed=21575608; DOI=10.1016/j.bbrc.2011.05.012;
RA   Yan B., Jiao S., Zhang H.S., Lv D.D., Xue J., Fan L., Wu G.H.,
RA   Fang J.;
RT   "Prolyl hydroxylase domain protein 3 targets Pax2 for destruction.";
RL   Biochem. Biophys. Res. Commun. 409:315-320(2011).
RN   [9]
RP   VARIANTS RCS GLU-THR-75 INS AND SER-76.
RX   MEDLINE=98430997; PubMed=9760197; DOI=10.1007/s004390050798;
RA   Devriendt K., Matthijs G., van Damme B., van Caesbroeck D.,
RA   Eccles M.R., Vanrenterghem Y., Fryns J.-P., Leys A.;
RT   "Missense mutation and hexanucleotide duplication in the PAX2 gene in
RT   two unrelated families with renal-coloboma syndrome (MIM 120330).";
RL   Hum. Genet. 103:149-153(1998).
RN   [10]
RP   VARIANT VAL-334.
RX   MEDLINE=21113232; PubMed=11180607;
RX   DOI=10.1002/1098-1004(200102)17:2<155::AID-HUMU16>3.0.CO;2-9;
RA   Gelb A.C., Manligas G.S., Gharaybeh S., Schimmenti L.A.;
RT   "Identification of two novel polymorphisms (g.903C>T and g.1544C>T) in
RT   the PAX2 gene.";
RL   Hum. Mutat. 17:155-155(2001).
RN   [11]
RP   VARIANT OMN 39-GLN-ARG-40 DEL.
RX   MEDLINE=21105676; PubMed=11168927;
RX   DOI=10.1046/j.1523-1755.2001.059002457.x;
RA   Salomon R., Tellier A.-L., Attie-Bitach T., Amiel J., Vekemans M.,
RA   Lyonnet S., Dureau P., Niaudet P., Gubler M.-C., Broyer M.;
RT   "PAX2 mutations in oligomeganephronia.";
RL   Kidney Int. 59:457-462(2001).
CC   -!- FUNCTION: Probable transcription factor that may have a role in
CC       kidney cell differentiation. Has a critical role in the
CC       development of the urogenital tract, the eyes, and the CNS.
CC   -!- SUBUNIT: Interacts with ELGN3; the interaction targets PAX2 for
CC       destruction.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q02962-1; Sequence=Displayed;
CC       Name=2; Synonyms=Fetal kidney;
CC         IsoId=Q02962-2; Sequence=VSP_002346;
CC       Name=3;
CC         IsoId=Q02962-3; Sequence=VSP_002345;
CC       Name=4;
CC         IsoId=Q02962-4; Sequence=VSP_002345, VSP_002346;
CC   -!- TISSUE SPECIFICITY: Expressed in primitive cells of the kidney,
CC       ureter, eye, ear and central nervous system.
CC   -!- DEVELOPMENTAL STAGE: Mainly in fetal kidney and juvenile
CC       nephrogenic rests.
CC   -!- DISEASE: Defects in PAX2 are the cause of renal-coloboma syndrome
CC       (RCS) [MIM:120330]; also known as papillorenal syndrome or optic
CC       nerve coloboma with renal disease. RCS is an autosomal dominant
CC       disease characterized by the association of renal hypoplasia,
CC       vesicoureteral reflux and dysplasia of the retina and optic disk.
CC   -!- DISEASE: Note=Defects in PAX2 may be responsible for isolated
CC       renal hypoplasia as observed in oligomeganephronia, a rare
CC       congenital and usually sporadic anomaly characterized by bilateral
CC       renal hypoplasia, with a reduced number of enlarged nephrons and
CC       without urinary tract abnormalities.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: Name=PAX2 mutation db;
CC       URL="http://www.hgu.mrc.ac.uk/Softdata/PAX2/";
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PAX2ID41642ch10q24.html";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PAX2";
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DR   EMBL; M89470; AAA60024.1; -; mRNA.
DR   EMBL; L25597; AAA36417.1; -; mRNA.
DR   EMBL; U45255; AAC63385.1; -; Genomic_DNA.
DR   EMBL; U45245; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45246; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45247; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45248; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45249; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45250; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45251; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45253; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; U45254; AAC63385.1; JOINED; Genomic_DNA.
DR   EMBL; AL138762; CAH70951.1; -; Genomic_DNA.
DR   EMBL; AL589862; CAH70951.1; JOINED; Genomic_DNA.
DR   EMBL; AL138762; CAH70952.1; -; Genomic_DNA.
DR   EMBL; AL589862; CAH70952.1; JOINED; Genomic_DNA.
DR   EMBL; AL589862; CAI17855.1; -; Genomic_DNA.
DR   EMBL; AL138762; CAI17855.1; JOINED; Genomic_DNA.
DR   EMBL; AL589862; CAI17856.1; -; Genomic_DNA.
DR   EMBL; AL138762; CAI17856.1; JOINED; Genomic_DNA.
DR   EMBL; CH471066; EAW49812.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW49813.1; -; Genomic_DNA.
DR   EMBL; L09747; AAC41711.1; -; Genomic_DNA.
DR   EMBL; L09748; AAC41711.1; JOINED; Genomic_DNA.
DR   EMBL; L09746; AAC41711.1; JOINED; Genomic_DNA.
DR   IPI; IPI00179609; -.
DR   IPI; IPI00220545; -.
DR   IPI; IPI00375134; -.
DR   IPI; IPI00395548; -.
DR   PIR; A49008; A49008.
DR   RefSeq; NP_000269.2; NM_000278.3.
DR   RefSeq; NP_003978.2; NM_003987.3.
DR   RefSeq; NP_003979.2; NM_003988.3.
DR   RefSeq; NP_003980.2; NM_003989.3.
DR   RefSeq; NP_003981.2; NM_003990.3.
DR   UniGene; Hs.155644; -.
DR   ProteinModelPortal; Q02962; -.
DR   SMR; Q02962; 19-142, 250-311.
DR   IntAct; Q02962; 4.
DR   STRING; Q02962; -.
DR   PhosphoSite; Q02962; -.
DR   DMDM; 223590261; -.
DR   PRIDE; Q02962; -.
DR   DNASU; 5076; -.
DR   Ensembl; ENST00000355243; ENSP00000347385; ENSG00000075891.
DR   Ensembl; ENST00000361791; ENSP00000355069; ENSG00000075891.
DR   Ensembl; ENST00000370294; ENSP00000359317; ENSG00000075891.
DR   Ensembl; ENST00000370296; ENSP00000359319; ENSG00000075891.
DR   Ensembl; ENST00000428433; ENSP00000396259; ENSG00000075891.
DR   GeneID; 5076; -.
DR   KEGG; hsa:5076; -.
DR   UCSC; uc001krk.4; human.
DR   UCSC; uc001krl.4; human.
DR   UCSC; uc001krm.4; human.
DR   UCSC; uc001krn.4; human.
DR   CTD; 5076; -.
DR   GeneCards; GC10P102495; -.
DR   HGNC; HGNC:8616; PAX2.
DR   HPA; CAB013024; -.
DR   MIM; 120330; phenotype.
DR   MIM; 167409; gene.
DR   neXtProt; NX_Q02962; -.
DR   Orphanet; 2260; Oligomeganephronia.
DR   Orphanet; 1475; Papillo-renal syndrome.
DR   PharmGKB; PA32956; -.
DR   eggNOG; NOG326044; -.
DR   GeneTree; ENSGT00650000093055; -.
DR   HOGENOM; HOG000230938; -.
DR   HOVERGEN; HBG009115; -.
DR   KO; K15608; -.
DR   OMA; FSAMHRH; -.
DR   OrthoDB; EOG49S66H; -.
DR   PhylomeDB; Q02962; -.
DR   NextBio; 19560; -.
DR   ArrayExpress; Q02962; -.
DR   Bgee; Q02962; -.
DR   CleanEx; HS_PAX2; -.
DR   Genevestigator; Q02962; -.
DR   GermOnline; ENSG00000075891; Homo sapiens.
DR   GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0043234; C:protein complex; ISS:UniProtKB.
DR   GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR   GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0016175; F:superoxide-generating NADPH oxidase activity; ISS:UniProtKB.
DR   GO; GO:0006916; P:anti-apoptosis; IMP:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; TAS:ProtInc.
DR   GO; GO:0048854; P:brain morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEP:UniProtKB.
DR   GO; GO:0001709; P:cell fate determination; ISS:UniProtKB.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR   GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR   GO; GO:0090103; P:cochlea morphogenesis; ISS:UniProtKB.
DR   GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; ISS:UniProtKB.
DR   GO; GO:0007501; P:mesodermal cell fate specification; ISS:UniProtKB.
DR   GO; GO:0001823; P:mesonephros development; ISS:UniProtKB.
DR   GO; GO:0072205; P:metanephric collecting duct development; ISS:UniProtKB.
DR   GO; GO:0072221; P:metanephric distal convoluted tubule development; ISS:UniProtKB.
DR   GO; GO:0072162; P:metanephric mesenchymal cell differentiation; ISS:UniProtKB.
DR   GO; GO:0072289; P:metanephric nephron tubule formation; ISS:UniProtKB.
DR   GO; GO:1900215; P:negative regulation of apoptotic process involved in metanephric collecting duct development; ISS:UniProtKB.
DR   GO; GO:1900218; P:negative regulation of apoptotic process involved in metanephric nephron tubule development; ISS:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR   GO; GO:0045918; P:negative regulation of cytolysis; IMP:UniProtKB.
DR   GO; GO:1900212; P:negative regulation of mesenchymal cell apoptotic process involved in metanephros development; ISS:UniProtKB.
DR   GO; GO:0072305; P:negative regulation of mesenchymal stem cell apoptotic process involved in metanephric nephron morphogenesis; ISS:UniProtKB.
DR   GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
DR   GO; GO:0072179; P:nephric duct formation; ISS:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; ISS:UniProtKB.
DR   GO; GO:0061360; P:optic chiasma development; ISS:UniProtKB.
DR   GO; GO:0002072; P:optic cup morphogenesis involved in camera-type eye development; ISS:UniProtKB.
DR   GO; GO:0021633; P:optic nerve structural organization; ISS:UniProtKB.
DR   GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
DR   GO; GO:0072108; P:positive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis; ISS:UniProtKB.
DR   GO; GO:2000594; P:positive regulation of metanephric DCT cell differentiation; ISS:UniProtKB.
DR   GO; GO:0072300; P:positive regulation of metanephric glomerulus development; ISS:UniProtKB.
DR   GO; GO:2000597; P:positive regulation of optic nerve formation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0039003; P:pronephric field specification; ISS:UniProtKB.
DR   GO; GO:0043491; P:protein kinase B signaling cascade; ISS:UniProtKB.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; ISS:UniProtKB.
DR   GO; GO:0072307; P:regulation of metanephric nephron tubule epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0035566; P:regulation of metanephros size; IMP:UniProtKB.
DR   GO; GO:0003406; P:retinal pigment epithelium development; ISS:UniProtKB.
DR   GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0035799; P:ureter maturation; ISS:UniProtKB.
DR   GO; GO:0021650; P:vestibulocochlear nerve formation; ISS:UniProtKB.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR022130; Pax2_C.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF00292; PAX; 1.
DR   Pfam; PF12403; Pax2_C; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Developmental protein;
KW   Differentiation; Disease mutation; DNA-binding; Nucleus; Paired box;
KW   Phosphoprotein; Polymorphism; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    417       Paired box protein Pax-2.
FT                                /FTId=PRO_0000050175.
FT   DOMAIN       16    142       Paired.
FT   MOD_RES     226    226       Phosphothreonine.
FT   VAR_SEQ     206    228       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_002345.
FT   VAR_SEQ     364    417       GSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRG
FT                                SAPAAAAAAYDRH -> EAAVGPSSSLMSKPGRKLAEVPPC
FT                                VQPTGASSPATRTATPSTRPTTRLGDSATPPY (in
FT                                isoform 2 and isoform 4).
FT                                /FTId=VSP_002346.
FT   VARIANT      39     40       Missing (in OMN; with bilateral
FT                                coloboma).
FT                                /FTId=VAR_012442.
FT   VARIANT      75     75       T -> TET (in RCS).
FT                                /FTId=VAR_003788.
FT   VARIANT      76     76       G -> S (in RCS).
FT                                /FTId=VAR_003789.
FT   VARIANT     334    334       A -> V.
FT                                /FTId=VAR_012443.
FT   CONFLICT     15     16       PG -> R (in Ref. 6; AAC41711).
FT   CONFLICT    404    404       Missing (in Ref. 1; AAA60024 and 3;
FT                                AAC63385).
FT   CONFLICT    410    410       A -> R (in Ref. 1; AAA60024 and 3;
FT                                AAC63385).
SQ   SEQUENCE   417 AA;  44706 MW;  7EA24F9EB8C843F8 CRC64;
     MDMHCKADPF SAMHPGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV
     SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVDKIA EYKRQNPTMF AWEIRDRLLA
     EGICDNDTVP SVSSINRIIR TKVQQPFHPT PDGAGTGVTA PGHTIVPSTA SPPVSSASND
     PVGSYSINGI LGIPRSNGEK RKRDEVEVYT DPAHIRGGGG LHLVWTLRDV SEGSVPNGDS
     QSGVDSLRKH LRADTFTQQQ LEALDRVFER PSYPDVFQAS EHIKSEQGNE YSLPALTPGL
     DEVKSSLSAS TNPELGSNVS GTQTYPVVTG RDMASTTLPG YPPHVPPTGQ GSYPTSTLAG
     MVPGSEFSGN PYSHPQYTAY NEAWRFSNPA LLSSPYYYSA APRGSAPAAA AAAYDRH
//
ID   PAX3_HUMAN              Reviewed;         479 AA.
AC   P23760; Q16448; Q494Z3; Q494Z4; Q53T90; Q6GSJ9; Q86UQ2; Q86UQ3;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   13-JUN-2012, entry version 145.
DE   RecName: Full=Paired box protein Pax-3;
DE   AltName: Full=HuP2;
GN   Name=PAX3; Synonyms=HUP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PAX3G AND PAX3H), AND ALTERNATIVE
RP   SPLICING.
RX   MEDLINE=22999378; PubMed=14639621; DOI=10.1002/ijc.11527;
RA   Parker C.J., Shawcross S.G., Li H., Wang Q.-Y., Herrington C.S.,
RA   Kumar S., MacKie R.M., Prime W., Renne I.G., Sisley K., Kumar P.;
RT   "Expression of PAX 3 alternatively spliced transcripts and
RT   identification of two new isoforms in human tumors of neural crest
RT   origin.";
RL   Int. J. Cancer 108:314-320(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS PAX3B; 6 AND 7).
RC   TISSUE=Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 AND 197-479.
RX   MEDLINE=95301273; PubMed=7782066; DOI=10.1016/0888-7543(95)80076-X;
RA   Macina R.A., Barr F.G., Galili N., Riethman H.C.;
RT   "Genomic organization of the human PAX3 gene: DNA sequence analysis of
RT   the region disrupted in alveolar rhabdomyosarcoma.";
RL   Genomics 26:1-8(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-195.
RX   MEDLINE=89305521; PubMed=2501086;
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-392, AND VARIANTS WS1 LEU-45
RP   AND ASP-99.
RX   MEDLINE=95072569; PubMed=7981674; DOI=10.1093/hmg/3.7.1069;
RA   Tassabehji M., Newton V.E., Leverton K., Turnbull K., Seemanova E.,
RA   Kunze J., Sperling K., Strachan T., Read A.P.;
RT   "PAX3 gene structure and mutations: close analogies between
RT   Waardenburg syndrome and the Splotch mouse.";
RL   Hum. Mol. Genet. 3:1069-1074(1994).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] (PAX3A AND PAX3B).
RX   MEDLINE=94171226; PubMed=7545913; DOI=10.1007/BF00212021;
RA   Tsukamoto K., Nakamura Y., Niikawa N.;
RT   "Isolation of two isoforms of the PAX3 gene transcripts and their
RT   tissue-specific alternative expression in human adult tissues.";
RL   Hum. Genet. 93:270-274(1994).
RN   [10]
RP   NUCLEOTIDE SEQUENCE OF 1-319 (ISOFORM 6/7), AND CHROMOSOMAL
RP   TRANSLOCATION WITH NCOA1.
RX   PubMed=15313887; DOI=10.1158/0008-5472.CAN-04-0844;
RA   Wachtel M., Dettling M., Koscielniak E., Stegmaier S., Treuner J.,
RA   Simon-Klingenstein K., Buehlmann P., Niggli F.K., Schaefer B.W.;
RT   "Gene expression signatures identify rhabdomyosarcoma subtypes and
RT   detect a novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1.";
RL   Cancer Res. 64:5539-5545(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-74, AND VARIANT WS1
RP   63-ALA--ILE-67 DEL.
RX   MEDLINE=92168113; PubMed=1347148; DOI=10.1038/355635a0;
RA   Tassabehji M., Read A.P., Newton V.E., Harris R., Balling R.,
RA   Gruss P., Strachan T.;
RT   "Waardenburg's syndrome patients have mutations in the human homologue
RT   of the Pax-3 paired box gene.";
RL   Nature 355:635-636(1992).
RN   [12]
RP   NUCLEOTIDE SEQUENCE OF 265-319.
RA   Lalwani A.K., Ploplis B., Fex J., Grundfast K.M., San Agustin T.B.,
RA   Wilcox E.R.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   CHROMOSOMAL TRANSLOCATION WITH FOXO1.
RX   MEDLINE=94100975; PubMed=8275086; DOI=10.1038/ng1193-230;
RA   Galili N., Davis R.J., Fredericks W.J., Mukhopadhyay S.,
RA   Rauscher F.J. III, Emanuel B.S., Rovera G., Barr F.G.;
RT   "Fusion of a fork head domain gene to PAX3 in the solid tumour
RT   alveolar rhabdomyosarcoma.";
RL   Nat. Genet. 5:230-235(1993).
RN   [14]
RP   INTERACTION WITH DAXX.
RX   MEDLINE=99321757; PubMed=10393185; DOI=10.1093/emboj/18.13.3702;
RA   Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.;
RT   "The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated
RT   repressor hDaxx.";
RL   EMBO J. 18:3702-3711(1999).
RN   [15]
RP   INVOLVEMENT IN WS1.
RX   PubMed=1303193; DOI=10.1093/hmg/1.4.243;
RA   Morell R., Friedman T.B., Moeljopawiro S., Hartono S., Asher J.H. Jr.;
RT   "A frameshift mutation in the HuP2 paired domain of the probable human
RT   homolog of murine Pax-3 is responsible for Waardenburg syndrome type 1
RT   in an Indonesian family.";
RL   Hum. Mol. Genet. 1:243-247(1992).
RN   [16]
RP   PHOSPHORYLATION AT SER-201; SER-205 AND SER-209.
RX   PubMed=21440083; DOI=10.1016/j.biocel.2011.03.010;
RA   Dietz K.N., Miller P.J., Iyengar A.S., Loupe J.M., Hollenbach A.D.;
RT   "Identification of serines 201 and 209 as sites of Pax3
RT   phosphorylation and the altered phosphorylation status of Pax3-FOXO1
RT   during early myogenic differentiation.";
RL   Int. J. Biochem. Cell Biol. 43:936-945(2011).
RN   [17]
RP   VARIANT WS1 LEU-50.
RX   MEDLINE=92168114; PubMed=1347149; DOI=10.1038/355637a0;
RA   Baldwin C.T., Hoth C.F., Amos J.A., Da-Silva E.O., Milunsky A.;
RT   "An exonic mutation in the HuP2 paired domain gene causes
RT   Waardenburg's syndrome.";
RL   Nature 355:637-638(1992).
RN   [18]
RP   VARIANT WS1 ALA-81.
RX   MEDLINE=93258399; PubMed=8490648; DOI=10.1038/ng0193-26;
RA   Tassabehji M., Read A.P., Newton V.E., Patton M., Gruss P., Harris R.,
RA   Strachan T.;
RT   "Mutations in the PAX3 gene causing Waardenburg syndrome type 1 and
RT   type 2.";
RL   Nat. Genet. 3:26-30(1993).
RN   [19]
RP   VARIANTS WS3 HIS-47 AND WS1 LEU-56.
RX   MEDLINE=93190976; PubMed=8447316;
RA   Hoth C.F., Milunsky A., Lipsky N., Sheffer R., Clarren S.K.,
RA   Baldwin C.T.;
RT   "Mutations in the paired domain of the human PAX3 gene cause Klein-
RT   Waardenburg syndrome (WS-III) as well as Waardenburg syndrome type I
RT   (WS-I).";
RL   Am. J. Hum. Genet. 52:455-462(1993).
RN   [20]
RP   VARIANT WS1 VAL-62.
RX   MEDLINE=95135456; PubMed=7833953; DOI=10.1002/humu.1380040310;
RA   Pierpont J.W., Doolan L.D., Amann K., Snead G.R., Erickson R.P.;
RT   "A single base pair substitution within the paired box of PAX3 in an
RT   individual with Waardenburg syndrome type 1 (WS1).";
RL   Hum. Mutat. 4:227-228(1994).
RN   [21]
RP   VARIANTS WS1 PHE-265 AND GLY-271.
RX   MEDLINE=95126143; PubMed=7825605;
RA   Lalwani A.K., Brister J.R., Fex J., Grundfast K.M., Ploplis B.,
RA   San Agustin T.B., Wilcox E.R.;
RT   "Further elucidation of the genomic structure of PAX3, and
RT   identification of two different point mutations within the PAX3
RT   homeobox that cause Waardenburg syndrome type 1 in two families.";
RL   Am. J. Hum. Genet. 56:75-83(1995).
RN   [22]
RP   VARIANT WS3 PHE-84.
RX   MEDLINE=95243235; PubMed=7726174;
RA   Zlotogora J., Lerer I., Bar-David S., Ergaz Z., Abeliovich D.;
RT   "Homozygosity for Waardenburg syndrome.";
RL   Am. J. Hum. Genet. 56:1173-1178(1995).
RN   [23]
RP   VARIANTS WS1 MET-60; GLU-85 AND SER-238.
RX   MEDLINE=96042708; PubMed=8533800; DOI=10.1002/ajmg.1320580205;
RA   Baldwin C.T., Hoth C.F., Macina R.A., Milunsky A.;
RT   "Mutations in PAX3 that cause Waardenburg syndrome type I: ten new
RT   mutations and review of the literature.";
RL   Am. J. Med. Genet. 58:115-122(1995).
RN   [24]
RP   VARIANTS WS1 MET-78; ALA-81; ASP-99; CYS-266; CYS-270; CYS-271 AND
RP   HIS-271, AND VARIANT LYS-315.
RX   MEDLINE=96154685; PubMed=8589691; DOI=10.1093/hmg/4.11.2131;
RA   Tassabehji M., Newton V.E., Liu X.-Z., Brady A., Donnai D.,
RA   Krajewska-Walasek M., Murday V., Norman A., Obersztyn E., Reardon W.,
RA   Rice J.C., Trembath R., Wieacker P., Whiteford M., Winter R.,
RA   Read A.P.;
RT   "The mutational spectrum in Waardenburg syndrome.";
RL   Hum. Mol. Genet. 4:2131-2137(1995).
RN   [25]
RP   VARIANTS WS1 ARG-48; CYS-270 AND HIS-271, AND VARIANTS LYS-273 AND
RP   LYS-315.
RX   PubMed=8845842; DOI=10.1093/hmg/5.4.497;
RA   Pandya A., Xia X.-J., Landa B.L., Arnos K.S., Israel J., Lloyd J.,
RA   James A.L., Diehl S.R., Blanton S.H., Nance W.E.;
RT   "Phenotypic variation in Waardenburg syndrome: mutational
RT   heterogeneity, modifier genes or polygenic background?";
RL   Hum. Mol. Genet. 5:497-502(1996).
RN   [26]
RP   VARIANT CDHS LYS-47.
RX   MEDLINE=96263735; PubMed=8664898;
RX   DOI=10.1002/(SICI)1098-1004(1996)7:1<30::AID-HUMU4>3.3.CO;2-H;
RA   Asher J.H. Jr., Sommer A., Morell R., Friedman T.B.;
RT   "Missense mutation in the paired domain of PAX3 causes craniofacial-
RT   deafness-hand syndrome.";
RL   Hum. Mutat. 7:30-35(1996).
RN   [27]
RP   VARIANT LYS-315.
RX   MEDLINE=97016531; PubMed=8863157;
RA   Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R.,
RA   Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "PAX genes and human neural tube defects: an amino acid substitution
RT   in PAX1 in a patient with spina bifida.";
RL   J. Med. Genet. 33:655-660(1996).
RN   [28]
RP   VARIANT WS1 PHE-59.
RX   MEDLINE=97220597; PubMed=9067759;
RX   DOI=10.1002/(SICI)1098-1004(1997)9:2<177::AID-HUMU11>3.3.CO;2-Z;
RA   Soejima H., Fujimoto M., Tsukamoto K., Matsumoto N., Yoshiura K.,
RA   Fukushima Y., Jinno Y., Niikawa N.;
RT   "Three novel PAX3 mutations observed in patients with Waardenburg
RT   syndrome type 1.";
RL   Hum. Mutat. 9:177-180(1997).
RN   [29]
RP   VARIANT WS1 VAL-62.
RX   MEDLINE=98112449; PubMed=9452070;
RA   Hol F.A., Geurds M.P.A., Cremers C.W.R.J., Hamel B.C.J.,
RA   Mariman E.C.M.;
RT   "Identification of two PAX3 mutations causing Waardenburg syndrome,
RT   one within the paired domain (M62V) and the other downstream of the
RT   homeodomain (Q282X).";
RL   Hum. Mutat. Suppl. 1:S145-S147(1998).
RN   [30]
RP   VARIANT WS1 HIS-391.
RX   MEDLINE=98200183; PubMed=9541113;
RA   Carey M.L., Friedman T.B., Asher J.H. Jr., Innis J.W.;
RT   "Septo-optic dysplasia and WS1 in the proband of a WS1 family
RT   segregating for a novel mutation in PAX3 exon 7.";
RL   J. Med. Genet. 35:248-250(1998).
RN   [31]
RP   VARIANT LYS-315.
RX   MEDLINE=98250826; PubMed=9584079; DOI=10.1006/mcpr.1997.0149;
RA   Wang C., Kim E., Attaie A., Smith T.N., Wilcox E.R., Lalwani A.K.;
RT   "A PAX3 polymorphism (T315K) in a family exhibiting Waardenburg
RT   syndrome type 2.";
RL   Mol. Cell. Probes 12:55-57(1998).
RN   [32]
RP   VARIANT WS1 ASN-59.
RA   Markova T.G., Shevtsov S.P., Moskolenko L.N., Lantsov A.A.,
RA   Schwartz E.I.;
RT   "A novel missense mutation Ile59Asn in the PAX3 gene in a family with
RT   Waardenburg syndrome type I.";
RL   Hum. Mutat. 13:85-85(1999).
RN   [33]
RP   VARIANT WS3 CYS-270.
RA   Bottani A., Antonarakis S.E., Blouin J.-L.;
RL   Submitted (MAY-1999) to UniProtKB.
RN   [34]
RP   VARIANT WS1 LEU-73.
RX   MEDLINE=20243823; PubMed=10779847;
RX   DOI=10.1076/1381-6810(200003)21:1;1-I;FT025;
RA   Sotirova V.N., Rezaie T.M., Khoshsorour M.M., Sarfarazi M.;
RT   "Identification of a novel mutation in the paired domain of PAX3 in an
RT   Iranian family with waardenburg syndrome type I.";
RL   Ophthalmic Genet. 21:25-28(2000).
RN   [35]
RP   VARIANT WS1 MET-60, AND VARIANT WS3 HIS-90.
RX   MEDLINE=22829208; PubMed=12949970; DOI=10.1002/ajmg.a.20260;
RA   Wollnik B., Tukel T., Uyguner O., Ghanbari A., Kayserili H.,
RA   Emiroglu M., Yuksel-Apak M.;
RT   "Homozygous and heterozygous inheritance of PAX3 mutations causes
RT   different types of Waardenburg syndrome.";
RL   Am. J. Med. Genet. A 122:42-45(2003).
CC   -!- FUNCTION: Probable transcription factor associated with
CC       development of alveolar rhabdomyosarcoma.
CC   -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX7. Interacts
CC       with DAXX.
CC   -!- INTERACTION:
CC       P20265:POU3F2; NbExp=2; IntAct=EBI-1167564, EBI-1167176;
CC       P56693:SOX10; NbExp=2; IntAct=EBI-1167564, EBI-1167533;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=Pax3;
CC         IsoId=P23760-1; Sequence=Displayed;
CC       Name=Pax3A;
CC         IsoId=P23760-2; Sequence=VSP_002355, VSP_002356;
CC       Name=Pax3B;
CC         IsoId=P23760-3; Sequence=VSP_002357, VSP_002358;
CC       Name=Pax3G;
CC         IsoId=P23760-4; Sequence=VSP_042004;
CC       Name=Pax3H;
CC         IsoId=P23760-5; Sequence=VSP_042005;
CC       Name=6;
CC         IsoId=P23760-6; Sequence=VSP_043634, VSP_043635;
CC         Note=No experimental confirmation available;
CC       Name=7;
CC         IsoId=P23760-7; Sequence=VSP_043635;
CC   -!- DISEASE: Defects in PAX3 are the cause of Waardenburg syndrome
CC       type 1 (WS1) [MIM:193500]. WS1 is an autosomal dominant disorder
CC       characterized by wide bridge of nose owing to lateral displacement
CC       of the inner canthus of each eye (dystopia canthorum), pigmentary
CC       disturbances such as frontal white blaze of hair, heterochromia of
CC       irides, white eyelashes, leukoderma and sensorineural deafness.
CC       The syndrome shows variable clinical expression and some affected
CC       individuals do not manifest hearing impairment.
CC   -!- DISEASE: Defects in PAX3 are the cause of Waardenburg syndrome
CC       type 3 (WS3) [MIM:148820]; also known as Klein-Waardenburg
CC       syndrome or Waardenburg syndrome with upper limb anomalies or
CC       white forelock with malformations. WS3 is a very rare autosomal
CC       dominant disorder, which shares many of the characteristics of
CC       WS1. Patients additionally present with musculoskeletal
CC       abnormalities.
CC   -!- DISEASE: Defects in PAX3 are the cause of craniofacial-deafness-
CC       hand syndrome (CDHS) [MIM:122880]. CDHS is thought to be an
CC       autosomal dominant disease which comprises absence or hypoplasia
CC       of the nasal bones, hypoplastic maxilla, small and short nose with
CC       thin nares, limited movement of the wrist, short palpebral
CC       fissures, ulnar deviation of the fingers, hypertelorism and
CC       profound sensory-neural deafness.
CC   -!- DISEASE: Defects in PAX3 are a cause of rhabdomyosarcoma type 2
CC       (RMS2) [MIM:268220]. It is a form of rhabdomyosarcoma, a highly
CC       malignant tumor of striated muscle derived from primitive
CC       mesenchimal cells and exhibiting differentiation along
CC       rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most
CC       frequently occurring soft tissue sarcomas and the most common in
CC       children. It occurs in four forms: alveolar, pleomorphic,
CC       embryonal and botryoidal rhabdomyosarcomas. Note=A chromosomal
CC       aberration involving PAX3 is found in rhabdomyosarcoma.
CC       Translocation (2;13)(q35;q14) with FOXO1. The resulting protein is
CC       a transcriptional activator.
CC   -!- DISEASE: Note=A chromosomal aberration involving PAX3 is a cause
CC       of rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with NCOA1
CC       generates the NCOA1-PAX3 oncogene consisting of the N-terminus
CC       part of PAX3 and the C-terminus part of NCOA1. The fusion protein
CC       acts as a transcriptional activator. Rhabdomyosarcoma is the most
CC       common soft tissue carcinoma in childhood, representing 5-8% of
CC       all malignancies in children.
CC   -!- SIMILARITY: Belongs to the paired homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PAX3ID70ch2q35.html";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PAX3";
CC   -----------------------------------------------------------------------
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DR   EMBL; AY251279; AAP13872.1; -; mRNA.
DR   EMBL; AY251280; AAP13873.1; -; mRNA.
DR   EMBL; AK291278; BAF83967.1; -; mRNA.
DR   EMBL; AC010980; AAY14900.1; -; Genomic_DNA.
DR   EMBL; AC012591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471063; EAW70789.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70791.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70794.1; -; Genomic_DNA.
DR   EMBL; BC063547; AAH63547.1; -; mRNA.
DR   EMBL; BC101299; AAI01300.1; -; mRNA.
DR   EMBL; BC101300; AAI01301.1; -; mRNA.
DR   EMBL; BC101301; AAI01302.1; -; mRNA.
DR   EMBL; BC101302; AAI01303.1; -; mRNA.
DR   EMBL; BC114363; AAI14364.1; -; mRNA.
DR   EMBL; U12263; AAA80573.1; -; Genomic_DNA.
DR   EMBL; U12259; AAA80574.1; -; Genomic_DNA.
DR   EMBL; U12258; AAA80574.1; JOINED; Genomic_DNA.
DR   EMBL; U12260; AAA80574.1; JOINED; Genomic_DNA.
DR   EMBL; U12262; AAA80574.1; JOINED; Genomic_DNA.
DR   EMBL; X15043; CAA33145.1; -; Genomic_DNA.
DR   EMBL; X15252; CAA33145.1; JOINED; Genomic_DNA.
DR   EMBL; X15253; CAA33145.1; JOINED; Genomic_DNA.
DR   EMBL; Z29972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z29973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z29974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S69369; AAB30167.1; -; mRNA.
DR   EMBL; S69370; AAB30168.1; -; mRNA.
DR   EMBL; AY633656; AAT47737.1; -; mRNA.
DR   EMBL; S83614; AAB21476.1; -; Genomic_DNA.
DR   EMBL; L10614; AAA91849.1; -; Genomic_DNA.
DR   IPI; IPI00012896; -.
DR   IPI; IPI00219092; -.
DR   IPI; IPI00219093; -.
DR   IPI; IPI00375387; -.
DR   IPI; IPI00895878; -.
DR   PIR; I54276; I54276.
DR   PIR; I68547; I68547.
DR   PIR; S06960; S06960.
DR   RefSeq; NP_000429.2; NM_000438.5.
DR   RefSeq; NP_001120838.1; NM_001127366.2.
DR   RefSeq; NP_039230.1; NM_013942.4.
DR   RefSeq; NP_852122.1; NM_181457.3.
DR   RefSeq; NP_852123.1; NM_181458.3.
DR   RefSeq; NP_852124.1; NM_181459.3.
DR   RefSeq; NP_852125.1; NM_181460.3.
DR   RefSeq; NP_852126.1; NM_181461.3.
DR   UniGene; Hs.42146; -.
DR   PDB; 3CMY; X-ray; 1.95 A; A=219-278.
DR   PDBsum; 3CMY; -.
DR   ProteinModelPortal; P23760; -.
DR   SMR; P23760; 35-158, 219-277.
DR   IntAct; P23760; 7.
DR   MINT; MINT-202884; -.
DR   STRING; P23760; -.
DR   PhosphoSite; P23760; -.
DR   DMDM; 1172022; -.
DR   PRIDE; P23760; -.
DR   DNASU; 5077; -.
DR   Ensembl; ENST00000258387; ENSP00000258387; ENSG00000135903.
DR   Ensembl; ENST00000336840; ENSP00000338767; ENSG00000135903.
DR   Ensembl; ENST00000344493; ENSP00000342092; ENSG00000135903.
DR   Ensembl; ENST00000350526; ENSP00000343052; ENSG00000135903.
DR   Ensembl; ENST00000392070; ENSP00000375922; ENSG00000135903.
DR   Ensembl; ENST00000409551; ENSP00000386750; ENSG00000135903.
DR   Ensembl; ENST00000409828; ENSP00000386817; ENSG00000135903.
DR   GeneID; 5077; -.
DR   KEGG; hsa:5077; -.
DR   UCSC; uc002vmw.2; human.
DR   UCSC; uc002vmz.2; human.
DR   UCSC; uc002vna.2; human.
DR   CTD; 5077; -.
DR   GeneCards; GC02M223029; -.
DR   HGNC; HGNC:8617; PAX3.
DR   HPA; CAB013466; -.
DR   MIM; 122880; phenotype.
DR   MIM; 148820; phenotype.
DR   MIM; 193500; phenotype.
DR   MIM; 268220; phenotype.
DR   MIM; 606597; gene.
DR   neXtProt; NX_P23760; -.
DR   Orphanet; 99756; Alveolar rhabdomyosarcoma.
DR   Orphanet; 1529; Craniofacial-deafness-hand syndrome.
DR   Orphanet; 894; Waardenburg syndrome type 1.
DR   Orphanet; 896; Waardenburg syndrome type 3.
DR   PharmGKB; PA32957; -.
DR   eggNOG; NOG326044; -.
DR   GeneTree; ENSGT00650000093130; -.
DR   HOGENOM; HOG000230939; -.
DR   HOVERGEN; HBG009115; -.
DR   KO; K09381; -.
DR   EvolutionaryTrace; P23760; -.
DR   NextBio; 19572; -.
DR   ArrayExpress; P23760; -.
DR   Bgee; P23760; -.
DR   CleanEx; HS_PAX3; -.
DR   Genevestigator; P23760; -.
DR   GermOnline; ENSG00000135903; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeodomain.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR022106; Pax7.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00292; PAX; 1.
DR   Pfam; PF12360; Pax7; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromosomal rearrangement;
KW   Complete proteome; Deafness; Developmental protein; Disease mutation;
KW   DNA-binding; Homeobox; Nucleus; Paired box; Phosphoprotein;
KW   Polymorphism; Proto-oncogene; Reference proteome; Transcription;
KW   Transcription regulation; Waardenburg syndrome.
FT   CHAIN         1    479       Paired box protein Pax-3.
FT                                /FTId=PRO_0000050178.
FT   DOMAIN       34    161       Paired.
FT   DNA_BIND    219    278       Homeobox.
FT   SITE        319    320       Breakpoint for translocation to form
FT                                PAX3-NCOA1 oncogene.
FT   MOD_RES     201    201       Phosphoserine.
FT   MOD_RES     205    205       Phosphoserine.
FT   MOD_RES     209    209       Phosphoserine.
FT   VAR_SEQ     108    108       Missing (in isoform 6).
FT                                /FTId=VSP_043634.
FT   VAR_SEQ     196    215       ASAPQSDEGSDIDSEPDLPL -> GKRWRLGRRTCWVTWRA
FT                                SAS (in isoform Pax3A).
FT                                /FTId=VSP_002355.
FT   VAR_SEQ     196    206       ASAPQSDEGSD -> GKALVSGVSSH (in isoform
FT                                Pax3B).
FT                                /FTId=VSP_002357.
FT   VAR_SEQ     207    479       Missing (in isoform Pax3B).
FT                                /FTId=VSP_002358.
FT   VAR_SEQ     216    479       Missing (in isoform Pax3A).
FT                                /FTId=VSP_002356.
FT   VAR_SEQ     393    479       MGLLTNHGGVPHQPQTDYALSPLTGGLEPTTTVSASCSQRL
FT                                DHMKSLDSLPTSQSYCPPTYSTTGYSMDPVTGYQYGQYGQS
FT                                KPWTF -> PFIISSQISRK (in isoform Pax3G).
FT                                /FTId=VSP_042004.
FT   VAR_SEQ     393    479       MGLLTNHGGVPHQPQTDYALSPLTGGLEPTTTVSASCSQRL
FT                                DHMKSLDSLPTSQSYCPPTYSTTGYSMDPVTGYQYGQYGQS
FT                                KPWTF -> PFIISSQISLGFKSF (in isoform
FT                                Pax3H).
FT                                /FTId=VSP_042005.
FT   VAR_SEQ     475    479       KPWTF -> AFHYLKPDIA (in isoform 6 and
FT                                isoform 7).
FT                                /FTId=VSP_043635.
FT   VARIANT      45     45       F -> L (in WS1).
FT                                /FTId=VAR_003790.
FT   VARIANT      47     47       N -> H (in WS3).
FT                                /FTId=VAR_003791.
FT   VARIANT      47     47       N -> K (in CDHS).
FT                                /FTId=VAR_003792.
FT   VARIANT      48     48       G -> R (in WS1).
FT                                /FTId=VAR_017533.
FT   VARIANT      50     50       P -> L (in WS1; important hearing loss).
FT                                /FTId=VAR_003793.
FT   VARIANT      56     56       R -> L (in WS1; associated with
FT                                meningomyelocele).
FT                                /FTId=VAR_003794.
FT   VARIANT      59     59       I -> F (in WS1).
FT                                /FTId=VAR_003795.
FT   VARIANT      59     59       I -> N (in WS1).
FT                                /FTId=VAR_003796.
FT   VARIANT      60     60       V -> M (in WS1).
FT                                /FTId=VAR_003797.
FT   VARIANT      62     62       M -> V (in WS1).
FT                                /FTId=VAR_003798.
FT   VARIANT      63     67       Missing (in WS1).
FT                                /FTId=VAR_003799.
FT   VARIANT      73     73       S -> L (in WS1).
FT                                /FTId=VAR_013640.
FT   VARIANT      78     78       V -> M (in WS1).
FT                                /FTId=VAR_017534.
FT   VARIANT      81     81       G -> A (in WS1; originally classified as
FT                                Waardenburg syndrome type 2).
FT                                /FTId=VAR_003800.
FT   VARIANT      84     84       S -> F (in WS3).
FT                                /FTId=VAR_003801.
FT   VARIANT      85     85       K -> E (in WS1).
FT                                /FTId=VAR_003802.
FT   VARIANT      90     90       Y -> H (in WS3; dbSNP:rs28939096).
FT                                /FTId=VAR_017535.
FT   VARIANT      99     99       G -> D (in WS1).
FT                                /FTId=VAR_003803.
FT   VARIANT     238    238       F -> S (in WS1).
FT                                /FTId=VAR_003804.
FT   VARIANT     265    265       V -> F (in WS1).
FT                                /FTId=VAR_003805.
FT   VARIANT     266    266       W -> C (in WS1).
FT                                /FTId=VAR_017536.
FT   VARIANT     270    270       R -> C (in WS1 and WS3).
FT                                /FTId=VAR_013619.
FT   VARIANT     271    271       R -> C (in WS1).
FT                                /FTId=VAR_017537.
FT   VARIANT     271    271       R -> G (in WS1).
FT                                /FTId=VAR_003806.
FT   VARIANT     271    271       R -> H (in WS1; associated with Lys-273
FT                                in one family).
FT                                /FTId=VAR_017538.
FT   VARIANT     273    273       R -> K (associated with His-271 in one
FT                                Waardenburg syndrome type I family).
FT                                /FTId=VAR_017539.
FT   VARIANT     315    315       T -> K (in dbSNP:rs2234675).
FT                                /FTId=VAR_003807.
FT   VARIANT     391    391       Q -> H (in WS1).
FT                                /FTId=VAR_013641.
FT   CONFLICT    358    358       S -> R (in Ref. 1; AAP13872/AAP13873).
FT   HELIX       228    240
FT   HELIX       246    256
FT   HELIX       260    276
SQ   SEQUENCE   479 AA;  52968 MW;  8AFCA674E3ACB4FE CRC64;
     MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV
     EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE
     YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES
     EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER
     THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP
     TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR
     HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE
     PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF
//
ID   PAX4_HUMAN              Reviewed;         350 AA.
AC   O43316; O95161; Q6B0H0;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   13-JUN-2012, entry version 118.
DE   RecName: Full=Paired box protein Pax-4;
GN   Name=PAX4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=98102804; PubMed=9439631; DOI=10.1006/bbrc.1997.7935;
RA   Matsushita T., Yamaoka T., Otsuka S., Moritani M., Matsumoto T.,
RA   Itakura M.;
RT   "Molecular cloning of mouse paired-box-containing gene (Pax-4) from an
RT   islet beta cell line and deduced sequence of human Pax-4.";
RL   Biochem. Biophys. Res. Commun. 242:176-180(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Placenta;
RX   MEDLINE=98424228; PubMed=9753306;
RA   Tao T., Wasson J., Bernal-Mizrachi E., Behn P.S., Chayen S.,
RA   Duprat L., Meyer J., Glaser B., Permutt M.A.;
RT   "Isolation and characterization of the human PAX4 gene.";
RL   Diabetes 47:1650-1653(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORM 2).
RC   TISSUE=Insulinoma;
RX   MEDLINE=21164695; PubMed=11263967; DOI=10.1006/bbrc.2001.4552;
RA   Miyamoto T., Kakizawa T., Ichikawa K., Nishio S., Kajikawa S.,
RA   Hashizume K.;
RT   "Expression of dominant negative form of PAX4 in human insulinoma.";
RL   Biochem. Biophys. Res. Commun. 282:34-40(2001).
RN   [6]
RP   VARIANT DIABETES MELLITUS TYPE 2 TRP-129.
RX   PubMed=11723072;
RA   Shimajiri Y., Sanke T., Furuta H., Hanabusa T., Nakagawa T.,
RA   Fujitani Y., Kajimoto Y., Takasu N., Nanjo K.;
RT   "A missense mutation of Pax4 gene (R121W) is associated with type 2
RT   diabetes in Japanese.";
RL   Diabetes 50:2864-2869(2001).
RN   [7]
RP   VARIANTS TRP-45 AND TRP-141, AND ASSOCIATION WITH SUSCEPTIBILITY TO
RP   KETOSIS-PRONE DIABETES.
RX   PubMed=15509590; DOI=10.1093/hmg/ddh341;
RA   Mauvais-Jarvis F., Smith S.B., Le May C., Leal S.M., Gautier J.-F.,
RA   Molokhia M., Riveline J.-P., Rajan A.S., Kevorkian J.-P., Zhang S.,
RA   Vexiau P., German M.S., Vaisse C.;
RT   "PAX4 gene variations predispose to ketosis-prone diabetes.";
RL   Hum. Mol. Genet. 13:3151-3159(2004).
RN   [8]
RP   VARIANT PRO-321 (ISOFORM 3), AND ASSOCIATION WITH SUSCEPTIBILITY TO
RP   IDDM.
RX   PubMed=15834548; DOI=10.1007/s00125-005-1723-5;
RA   Biason-Lauber A., Boehm B., Lang-Muritano M., Gauthier B.R., Brun T.,
RA   Wollheim C.B., Schoenle E.J.;
RT   "Association of childhood type 1 diabetes mellitus with a variant of
RT   PAX4: possible link to beta cell regenerative capacity.";
RL   Diabetologia 48:900-905(2005).
RN   [9]
RP   VARIANT MODY9 TRP-172, VARIANTS GLN-39; CYS-191; HIS-200 AND SER-200,
RP   VARIANT PRO-321 (ISOFORM 3), AND CHARACTERIZATION OF VARIANT MODY9
RP   TRP-172.
RX   PubMed=17426099; DOI=10.1210/jc.2006-1927;
RA   Plengvidhya N., Kooptiwut S., Songtawee N., Doi A., Furuta H.,
RA   Nishi M., Nanjo K., Tantibhedhyangkul W., Boonyasrisawat W.,
RA   Yenchitsomanus P.-T., Doria A., Banchuin N.;
RT   "PAX4 mutations in Thais with maturity onset diabetes of the young.";
RL   J. Clin. Endocrinol. Metab. 92:2821-2826(2007).
CC   -!- FUNCTION: Plays an important role in the differentiation and
CC       development of pancreatic islet beta cells. Transcriptional
CC       repressor that binds to a common element in the glucagon, insulin
CC       and somatostatin promoters. Competes with PAX6 for this same
CC       promoter binding site. Isoform 2 appears to be a dominant negative
CC       form antagonizing PAX4 transcriptional activity.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Pax4;
CC         IsoId=O43316-1; Sequence=Displayed;
CC       Name=2; Synonyms=Pax4V;
CC         IsoId=O43316-2; Sequence=VSP_002359, VSP_002360;
CC       Name=3;
CC         IsoId=O43316-4; Sequence=VSP_036448, VSP_036449;
CC         Note=Variant in position: 321:H->P (associated with
CC         susceptibility to IDDM, dbSNP:rs712701);
CC   -!- DISEASE: Defects in PAX4 are a cause of noninsulin-dependent
CC       diabetes mellitus (NIDDM) [MIM:125853]; also known as diabetes
CC       mellitus type 2 or maturity-onset diabetes. NIDDM is characterized
CC       by an autosomal dominant mode of inheritance, onset during
CC       adulthood and insulin resistance.
CC   -!- DISEASE: Genetic variations in PAX4 are associated with
CC       susceptibility to insulin-dependent diabetes mellitus (IDDM)
CC       [MIM:222100]. IDDM normally starts in childhood or adolescence and
CC       is caused by the body's own immune system which destroys the
CC       insulin-producing beta cells in the pancreas. Classical features
CC       are polydipsia, polyphagia and polyuria, due to hyperglycemia-
CC       induced osmotic diuresis.
CC   -!- DISEASE: Defects in PAX4 are a cause of susceptibility to diabetes
CC       mellitus ketosis-prone (KPD) [MIM:612227]. KPD is an atypical form
CC       of diabetes mellitus characterized by an acute initial
CC       presentation with severe hyperglycemia and ketosis, as seen in
CC       classic type 1 diabetes, but after initiation of insulin therapy,
CC       prolonged remission is often possible with cessation of insulin
CC       therapy and maintenance of appropriate metabolic control.
CC       Metabolic studies show a markedly blunted insulin secretory
CC       response to glucose, partially reversible with the improvement of
CC       blood glucose control. Variable levels of insulin resistance are
CC       observed, especially in obese patients. Pancreatic beta-cell
CC       autoimmunity is a rare finding.
CC   -!- DISEASE: Defects in PAX4 are the cause of maturity-onset diabetes
CC       of the young type 9 (MODY9) [MIM:612225]. MODY is a form of
CC       diabetes that is characterized by an autosomal dominant mode of
CC       inheritance, onset in childhood or early adulthood (usually before
CC       25 years of age), a primary defect in insulin secretion and
CC       frequent insulin-independence at the beginning of the disease.
CC   -!- SIMILARITY: Belongs to the paired homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AC073934; Type=Miscellaneous discrepancy; Note=According to the human genome assembly there is a stop codon in position 349;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB008913; BAA24506.1; -; mRNA.
DR   EMBL; AF043978; AAD02289.1; -; mRNA.
DR   EMBL; AC073934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC074761; AAH74761.1; -; mRNA.
DR   IPI; IPI00011955; -.
DR   IPI; IPI00218426; -.
DR   IPI; IPI00844339; -.
DR   RefSeq; NP_006184.2; NM_006193.2.
DR   UniGene; Hs.129706; -.
DR   ProteinModelPortal; O43316; -.
DR   SMR; O43316; 7-135, 164-233.
DR   STRING; O43316; -.
DR   PRIDE; O43316; -.
DR   DNASU; 5078; -.
DR   Ensembl; ENST00000338516; ENSP00000344297; ENSG00000106331.
DR   Ensembl; ENST00000341640; ENSP00000339906; ENSG00000106331.
DR   Ensembl; ENST00000378740; ENSP00000368014; ENSG00000106331.
DR   GeneID; 5078; -.
DR   KEGG; hsa:5078; -.
DR   UCSC; uc003vmg.1; human.
DR   UCSC; uc010lld.1; human.
DR   CTD; 5078; -.
DR   GeneCards; GC07M127250; -.
DR   H-InvDB; HIX0033508; -.
DR   HGNC; HGNC:8618; PAX4.
DR   HPA; HPA006806; -.
DR   HPA; HPA007182; -.
DR   MIM; 125853; phenotype.
DR   MIM; 167413; gene.
DR   MIM; 222100; phenotype.
DR   MIM; 612225; phenotype.
DR   MIM; 612227; phenotype.
DR   neXtProt; NX_O43316; -.
DR   Orphanet; 552; MODY syndrome.
DR   PharmGKB; PA32958; -.
DR   eggNOG; NOG309473; -.
DR   GeneTree; ENSGT00650000093130; -.
DR   HOGENOM; HOG000230939; -.
DR   HOVERGEN; HBG009115; -.
DR   KO; K08032; -.
DR   Reactome; REACT_111045; Developmental Biology.
DR   NextBio; 19588; -.
DR   ArrayExpress; O43316; -.
DR   Bgee; O43316; -.
DR   CleanEx; HS_PAX4; -.
DR   Genevestigator; O43316; -.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeodomain.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Developmental protein;
KW   Diabetes mellitus; Differentiation; Disease mutation; DNA-binding;
KW   Homeobox; Nucleus; Paired box; Polymorphism; Reference proteome;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    350       Paired box protein Pax-4.
FT                                /FTId=PRO_0000050180.
FT   DOMAIN        5    131       Paired.
FT   DNA_BIND    170    229       Homeobox.
FT   REGION      278    350       Transcription repression.
FT   VAR_SEQ       1      8       Missing (in isoform 3).
FT                                /FTId=VSP_036448.
FT   VAR_SEQ     239    257       Missing (in isoform 2).
FT                                /FTId=VSP_002359.
FT   VAR_SEQ     258    350       QSPGSVPTAALPALEPLGPSCYQLCWATAPERCLSDTPPKA
FT                                CLKPCWDCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAG
FT                                KATPTHFSHWP -> AVPWQCAHSSPACPGTTGSLLLSAVL
FT                                GNSTRKVSE (in isoform 2).
FT                                /FTId=VSP_002360.
FT   VAR_SEQ     305    350       DCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAGKATPTH
FT                                FSHWP -> GHLPPQPNSLDSGLLCLPCPSSHCHLASLSGS
FT                                QALLWPGCPLLYGLE (in isoform 3).
FT                                /FTId=VSP_036449.
FT   VARIANT      39     39       R -> Q.
FT                                /FTId=VAR_054879.
FT   VARIANT      45     45       R -> W (associated with PKD
FT                                susceptbility).
FT                                /FTId=VAR_054880.
FT   VARIANT     129    129       R -> W (in diabetes mellitus type 2).
FT                                /FTId=VAR_054881.
FT   VARIANT     141    141       R -> W (confers susceptibility to
FT                                ketosis-prone diabetes mellitus).
FT                                /FTId=VAR_054882.
FT   VARIANT     172    172       R -> W (in MODY9; the mutant sequence
FT                                represses the activity of the insulin and
FT                                glucagon promoters by only 35% compared
FT                                to 50% and 57% respectively with wild-
FT                                type sequence).
FT                                /FTId=VAR_054883.
FT   VARIANT     191    191       R -> C.
FT                                /FTId=VAR_054884.
FT   VARIANT     200    200       R -> H.
FT                                /FTId=VAR_054885.
FT   VARIANT     200    200       R -> S.
FT                                /FTId=VAR_054886.
SQ   SEQUENCE   350 AA;  37833 MW;  2C2343AF16AEAAAC CRC64;
     MHQDGISSMN QLGGLFVNGR PLPLDTRQQI VRLAVSGMRP CDISRILKVS NGCVSKILGR
     YYRTGVLEPK GIGGSKPRLA TPPVVARIAQ LKGECPALFA WEIQRQLCAE GLCTQDKTPS
     VSSINRVLRA LQEDQGLPCT RLRSPAVLAP AVLTPHSGSE TPRGTHPGTG HRNRTIFSPS
     QAEALEKEFQ RGQYPDSVAR GKLATATSLP EDTVRVWFSN RRAKWRRQEK LKWEMQLPGA
     SQGLTVPRVA PGIISAQQSP GSVPTAALPA LEPLGPSCYQ LCWATAPERC LSDTPPKACL
     KPCWDCGSFL LPVIAPSCVD VAWPCLDASL AHHLIGGAGK ATPTHFSHWP
//
ID   PAX5_HUMAN              Reviewed;         391 AA.
AC   Q02548; A3QVP6; A3QVP7; A3QVP8; O75933;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   13-JUN-2012, entry version 114.
DE   RecName: Full=Paired box protein Pax-5;
DE   AltName: Full=B-cell-specific transcription factor;
DE            Short=BSAP;
GN   Name=PAX5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92387536; PubMed=1516825;
RA   Adams B., Doerfler P., Aguzzi A., Kozmik Z., Urbanek P.,
RA   Maurer-Fogy I., Busslinger M.;
RT   "Pax-5 encodes the transcription factor BSAP and is expressed in B
RT   lymphocytes, the developing CNS, and adult testis.";
RL   Genes Dev. 6:1589-1607(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-333, CHROMOSOMAL TRANSLOCATION WITH
RP   ZNF521, CHROMOSOMAL TRANSLOCATION WITH FOXP1, AND CHROMOSOMAL
RP   TRANSLOCATION WITH ETV6.
RX   PubMed=17344859; DOI=10.1038/nature05690;
RA   Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E.,
RA   Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X.,
RA   Pui C.-H., Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R.;
RT   "Genome-wide analysis of genetic alterations in acute lymphoblastic
RT   leukaemia.";
RL   Nature 446:758-764(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 62-197.
RX   MEDLINE=98416211; PubMed=9742255; DOI=10.1093/nar/26.19.4497;
RA   Verkoczy L.K., Berinstein N.L.;
RT   "Isolation of genes negatively or positively co-expressed with human
RT   recombination activating gene 1 (RAG1) by differential display PCR (DD
RT   RT-PCR).";
RL   Nucleic Acids Res. 26:4497-4507(1998).
RN   [4]
RP   INTERACTION WITH TLE4.
RX   MEDLINE=20271869; PubMed=10811620; DOI=10.1093/emboj/19.10.2292;
RA   Eberhard D., Jimenez G., Heavey B., Busslinger M.;
RT   "Transcriptional repression by Pax5 (BSAP) through interaction with
RT   corepressors of the Groucho family.";
RL   EMBO J. 19:2292-2303(2000).
CC   -!- FUNCTION: May play an important role in B-cell differentiation as
CC       well as neural development and spermatogenesis. Involved in the
CC       regulation of the CD19 gene, a B-lymphoid-specific target gene.
CC   -!- SUBUNIT: Interacts with DAXX (By similarity). Binds DNA as a
CC       monomer. Binds TLE4.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Expressed at early B-cell differentiation, in
CC       the developing CNS and in adult testis.
CC   -!- PTM: O-glycosylated (Probable).
CC   -!- DISEASE: Note=A chromosomal aberration involving PAX5 is a cause
CC       of acute lymphoblastic leukemia. Translocation t(9;18)(p13;q11.2)
CC       with ZNF521. Translocation t(9;3)(p13;p14.1) with FOXP1.
CC       Translocation t(9;12)(p13;p13) with ETV6.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PAX5ID62.html";
CC   -----------------------------------------------------------------------
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DR   EMBL; M96944; AAA58397.1; -; mRNA.
DR   EMBL; DQ841178; ABI30005.1; ALT_TERM; mRNA.
DR   EMBL; DQ845345; ABI33104.1; ALT_TERM; mRNA.
DR   EMBL; DQ845346; ABI33105.1; ALT_TERM; mRNA.
DR   EMBL; AF080573; AAC35286.1; -; mRNA.
DR   IPI; IPI00026209; -.
DR   PIR; A44063; A44063.
DR   RefSeq; NP_057953.1; NM_016734.1.
DR   UniGene; Hs.654464; -.
DR   PDB; 1K78; X-ray; 2.25 A; A/E/I=1-149.
DR   PDB; 1MDM; X-ray; 2.80 A; A=1-149.
DR   PDBsum; 1K78; -.
DR   PDBsum; 1MDM; -.
DR   ProteinModelPortal; Q02548; -.
DR   SMR; Q02548; 19-142, 222-281.
DR   IntAct; Q02548; 2.
DR   STRING; Q02548; -.
DR   PhosphoSite; Q02548; -.
DR   DMDM; 417449; -.
DR   PRIDE; Q02548; -.
DR   DNASU; 5079; -.
DR   Ensembl; ENST00000358127; ENSP00000350844; ENSG00000196092.
DR   GeneID; 5079; -.
DR   KEGG; hsa:5079; -.
DR   UCSC; uc003zzo.1; human.
DR   CTD; 5079; -.
DR   GeneCards; GC09M036828; -.
DR   HGNC; HGNC:8619; PAX5.
DR   HPA; CAB026269; -.
DR   HPA; CAB026869; -.
DR   MIM; 167414; gene.
DR   neXtProt; NX_Q02548; -.
DR   PharmGKB; PA32959; -.
DR   eggNOG; NOG326044; -.
DR   HOGENOM; HOG000230938; -.
DR   HOVERGEN; HBG009115; -.
DR   InParanoid; Q02548; -.
DR   KO; K09383; -.
DR   OMA; HSIASTG; -.
DR   OrthoDB; EOG4DZ1VJ; -.
DR   EvolutionaryTrace; Q02548; -.
DR   NextBio; 19592; -.
DR   ArrayExpress; Q02548; -.
DR   Bgee; Q02548; -.
DR   CleanEx; HS_PAX5; -.
DR   Genevestigator; Q02548; -.
DR   GermOnline; ENSG00000196092; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006959; P:humoral immune response; TAS:ProtInc.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR022130; Pax2_C.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF00292; PAX; 1.
DR   Pfam; PF12403; Pax2_C; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromosomal rearrangement; Complete proteome;
KW   Developmental protein; Differentiation; DNA-binding; Glycoprotein;
KW   Neurogenesis; Nucleus; Paired box; Polymorphism; Proto-oncogene;
KW   Reference proteome; Spermatogenesis; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    391       Paired box protein Pax-5.
FT                                /FTId=PRO_0000050183.
FT   DOMAIN       16    142       Paired.
FT   SITE        158    159       Breakpoint for translocation to form
FT                                PAX5-ETV6.
FT   SITE        260    261       Breakpoint for translocation to form
FT                                PAX5-FOXP1.
FT   SITE        303    304       Breakpoint for translocation to form
FT                                PAX5-ZNF521.
FT   VARIANT     322    322       A -> T (in dbSNP:rs34810717).
FT                                /FTId=VAR_034370.
FT   CONFLICT     99     99       I -> F (in Ref. 3; AAC35286).
FT   CONFLICT    141    143       TKV -> PKL (in Ref. 3; AAC35286).
FT   HELIX        35     46
FT   HELIX        51     58
FT   HELIX        62     75
FT   STRAND       89     91
FT   HELIX        93    105
FT   HELIX       111    120
FT   TURN        126    128
FT   HELIX       132    140
SQ   SEQUENCE   391 AA;  42149 MW;  DB37E6EACD9F993A CRC64;
     MDLEKNYPTP RTSRTGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV
     SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVEKIA EYKRQNPTMF AWEIRDRLLA
     ERVCDNDTVP SVSSINRIIR TKVQQPPNQP VPASSHSIVS TGSVTQVSSV STDSAGSSYS
     ISGILGITSP SADTNKRKRD EGIQESPVPN GHSLPGRDFL RKQMRGDLFT QQQLEVLDRV
     FERQHYSDIF TTTEPIKPEQ TTEYSAMASL AGGLDDMKAN LASPTPADIG SSVPGPQSYP
     IVTGRDLAST TLPGYPPHVP PAGQGSYSAP TLTGMVPGSE FSGSPYSHPQ YSSYNDSWRF
     PNPGLLGSPY YYSAAARGAA PPAAATAYDR H
//
ID   PAX6_HUMAN              Reviewed;         422 AA.
AC   P26367; Q6N006; Q99413;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   13-JUN-2012, entry version 151.
DE   RecName: Full=Paired box protein Pax-6;
DE   AltName: Full=Aniridia type II protein;
DE   AltName: Full=Oculorhombin;
GN   Name=PAX6; Synonyms=AN2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal eye;
RX   MEDLINE=92103673; PubMed=1684738; DOI=10.1016/0092-8674(91)90284-6;
RA   Ton C.C.T., Hirvonen H., Miwa H., Weil M.M., Monaghan P., Jordan T.,
RA   van Heyningen V., Hastie N.D., Meijers-Heijboer H., Drechsler M.,
RA   Royer-Pokora B., Collins F.S., Swaroop A., Strong L.C., Saunders G.F.;
RT   "Positional cloning and characterization of a paired box- and
RT   homeobox-containing gene from the aniridia region.";
RL   Cell 67:1059-1074(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=94258210; PubMed=1345175; DOI=10.1038/ng1192-232;
RA   Glaser T., Walton D.S., Maas R.L.;
RT   "Genomic structure, evolutionary conservation and aniridia mutations
RT   in the human PAX6 gene.";
RL   Nat. Genet. 2:232-239(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Liu J., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5A).
RC   TISSUE=Cerebellum;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   ALTERNATIVE SPLICING, AND DNA-BINDING.
RX   MEDLINE=95047352; PubMed=7958875;
RA   Epstein J.A., Glaser T., Cai J., Jepeal L., Walton D.S., Maas R.L.;
RT   "Two independent and interactive DNA-binding subdomains of the Pax6
RT   paired domain are regulated by alternative splicing.";
RL   Genes Dev. 8:2022-2034(1994).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-136.
RX   PubMed=10346815;
RA   Xu H.E., Rould M.A., Xu W., Epstein J.A., Maas R.L., Pabo C.O.;
RT   "Crystal structure of the human Pax-6 paired domain-DNA complex
RT   reveals specific roles for the linker region and carboxyl-terminal
RT   subdomain in DNA binding.";
RL   Genes Dev. 13:1263-1275(1999).
RN   [9]
RP   REVIEW ON VARIANTS.
RX   MEDLINE=98141676; PubMed=9482572;
RX   DOI=10.1002/(SICI)1098-1004(1998)11:2<93::AID-HUMU1>3.3.CO;2-J;
RA   Prosser J., van Heyningen V.;
RT   "PAX6 mutations reviewed.";
RL   Hum. Mutat. 11:93-108(1998).
RN   [10]
RP   STRUCTURE BY NMR OF 211-277.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the homeobox domain of the human paired box
RT   protein PAX-6.";
RL   Submitted (NOV-2005) to the PDB data bank.
RN   [11]
RP   VARIANT AN TRP-208.
RX   MEDLINE=93372853; PubMed=8364574; DOI=10.1093/hmg/2.7.915;
RA   Hanson I.M., Seawright A., Hardman K., Hodgson S., Zaletayev D.,
RA   Fekete G., van Heyningen V.;
RT   "PAX6 mutations in aniridia.";
RL   Hum. Mol. Genet. 2:915-920(1993).
RN   [12]
RP   VARIANT PAN GLY-26.
RX   MEDLINE=94214497; PubMed=8162071; DOI=10.1038/ng0294-168;
RA   Hanson I.M., Fletcher J.M., Jordan T., Brown A., Taylor D.,
RA   Adams R.J., Punnet H.H., van Heyningen V.;
RT   "Mutations at the PAX6 locus are found in heterogeneous anterior
RT   segment malformations including Peters' anomaly.";
RL   Nat. Genet. 6:168-173(1994).
RN   [13]
RP   VARIANTS FOVHYP CYS-125 AND CYS-128.
RX   MEDLINE=96225435; PubMed=8640214; DOI=10.1038/ng0696-141;
RA   Azuma N., Nishina S., Yanagisawa H., Okuyama T., Yamada M.;
RT   "PAX6 missense mutation in isolated foveal hypoplasia.";
RL   Nat. Genet. 13:141-142(1996).
RN   [14]
RP   VARIANT AN ARG-87, AND VARIANT GLY-26.
RX   MEDLINE=97227282; PubMed=9147640; DOI=10.1093/hmg/6.3.381;
RA   Tang H.K., Chao L.-Y., Saunders G.F.;
RT   "Functional analysis of paired box missense mutations in the PAX6
RT   gene.";
RL   Hum. Mol. Genet. 6:381-386(1997).
RN   [15]
RP   VARIANT AN 22-PRO--ARG-26 DEL.
RX   MEDLINE=97428347; PubMed=9281415; DOI=10.1006/mcpr.1997.0117;
RA   Axton R., Hanson I.M., Love J., Seawright A., Prosser J.,
RA   van Heyningen V.;
RT   "Combined SSCP/heteroduplex analysis in the screening for PAX6
RT   mutations.";
RL   Mol. Cell. Probes 11:287-292(1997).
RN   [16]
RP   VARIANT AN TRP-18.
RX   MEDLINE=99006892; PubMed=9792406;
RX   DOI=10.1002/(SICI)1098-1004(1998)12:5<304::AID-HUMU3>3.3.CO;2-Y;
RA   Wolf M.T.F., Lorenz B., Winterpacht A., Drechsler M., Schumacher V.,
RA   Royer-Pokora B., Blankenagel A., Zabel B., Wildhardt G.;
RT   "Ten novel mutations found in Aniridia.";
RL   Hum. Mutat. 12:304-313(1998).
RN   [17]
RP   VARIANT EYE MALFORMATIONS ARG-422.
RX   MEDLINE=98199717; PubMed=9538891;
RA   Azuma N., Yamada M.;
RT   "Missense mutation at the C-terminus of the PAX6 gene in ocular
RT   anterior segment anomalies.";
RL   Invest. Ophthalmol. Vis. Sci. 39:828-830(1998).
RN   [18]
RP   VARIANTS AN SER-17; VAL-29; GLN-44 AND HIS-178.
RX   MEDLINE=99072581; PubMed=9856761;
RA   Azuma N., Hotta Y., Tanaka H., Yamada M.;
RT   "Missense mutations in the PAX6 gene in aniridia.";
RL   Invest. Ophthalmol. Vis. Sci. 39:2524-2528(1998).
RN   [19]
RP   VARIANT PAN ASP-53.
RX   MEDLINE=99375017; PubMed=10441571; DOI=10.1086/302529;
RA   Azuma N., Yamaguchi Y., Handa H., Hayakawa M., Kanai A., Yamada M.;
RT   "Missense mutation in the alternative splice region of the PAX6 gene
RT   in eye anomalies.";
RL   Am. J. Hum. Genet. 65:656-663(1999).
RN   [20]
RP   ALTERNATIVE SPLICING, AND VARIANTS AN SER-42; LEU-53; PRO-63; GLU-79
RP   AND GLN-208.
RX   MEDLINE=99250762; PubMed=10234503; DOI=10.1038/sj.ejhg.5200308;
RA   Groenskov K., Rosenberg T., Sand A., Broendum-Nielsen K.;
RT   "Mutational analysis of PAX6: 16 novel mutations including 5 missense
RT   mutations with a mild aniridia phenotype.";
RL   Eur. J. Hum. Genet. 7:274-286(1999).
RN   [21]
RP   VARIANTS AN PRO-33; PRO-43 AND ASP-126, AND VARIANT FOVHYP VAL-64.
RX   MEDLINE=99135896; PubMed=9931324; DOI=10.1093/hmg/8.2.165;
RA   Hanson I.M., Churchill A., Love J., Axton R., Moore T., Clarke M.,
RA   Meire F., van Heyningen V.;
RT   "Missense mutations in the most ancient residues of the PAX6 paired
RT   domain underlie a spectrum of human congenital eye malformations.";
RL   Hum. Mol. Genet. 8:165-172(1999).
RN   [22]
RP   VARIANTS AN SER-29; ARG-119 AND ALA-353.
RA   Wildhardt G.;
RL   Unpublished observations (APR-1999).
RN   [23]
RP   VARIANT AN 37-ALA--PRO-39 DEL.
RA   Saunders G.F.;
RL   Unpublished observations (AUG-1999).
RN   [24]
RP   VARIANT NYSTAGMUS ARG-118.
RX   MEDLINE=20410622; PubMed=10955655; DOI=10.1007/s004170000124;
RA   Sonoda S., Isashiki Y., Tabata Y., Kimura K., Kakiuchi T., Ohba N.;
RT   "A novel PAX6 gene mutation (P118R) in a family with congenital
RT   nystagmus associated with a variant form of aniridia.";
RL   Graefes Arch. Clin. Exp. Ophthalmol. 238:552-558(2000).
RN   [25]
RP   VARIANT AN 37-ARG--PRO-39 DEL, AND VARIANT ASP-387.
RX   PubMed=10737978;
RX   DOI=10.1002/(SICI)1098-1004(200004)15:4<332::AID-HUMU5>3.0.CO;2-1;
RA   Chao L.-Y., Huff V., Strong L.C., Saunders G.F.;
RT   "Mutation in the PAX6 gene in twenty patients with aniridia.";
RL   Hum. Mutat. 15:332-339(2000).
RN   [26]
RP   VARIANT AN ARG-119.
RX   PubMed=11553050; DOI=10.1034/j.1399-0004.2001.600210.x;
RA   Malandrini A., Mari F., Palmeri S., Gambelli S., Berti G.,
RA   Bruttini M., Bardelli A.M., Williamson K., van Heyningen V.,
RA   Renieri A.;
RT   "PAX6 mutation in a family with aniridia, congenital ptosis, and
RT   mental retardation.";
RL   Clin. Genet. 60:151-154(2001).
RN   [27]
RP   VARIANTS AN GLN-375 AND ARG-422.
RX   MEDLINE=21205761; PubMed=11309364; DOI=10.1093/hmg/10.9.911;
RA   Singh S., Chao L.-Y., Mishra R., Davies J., Saunders G.F.;
RT   "Missense mutation at the C-terminus of PAX6 negatively modulates
RT   homeodomain function.";
RL   Hum. Mol. Genet. 10:911-918(2001).
RN   [28]
RP   VARIANT AN THR-242.
RX   PubMed=11826019; DOI=10.1136/jmg.39.1.16;
RA   Morrison D., FitzPatrick D., Hanson I., Williamson K.,
RA   van Heyningen V., Fleck B., Jones I., Chalmers J., Campbell H.;
RT   "National study of microphthalmia, anophthalmia, and coloboma (MAC) in
RT   Scotland: investigation of genetic aetiology.";
RL   J. Med. Genet. 39:16-22(2002).
RN   [29]
RP   VARIANT MORNING GLORY DISK ANOMALY SER-68, VARIANT COI SER-258,
RP   VARIANT PAN PRO-363, AND VARIANTS BONH ILE-292; ARG-378; VAL-381 AND
RP   ALA-391.
RX   MEDLINE=22633032; PubMed=12721955; DOI=10.1086/375555;
RA   Azuma N., Yamaguchi Y., Handa H., Tadokoro K., Asaka A., Kawase E.,
RA   Yamada M.;
RT   "Mutations of the PAX6 gene detected in patients with a variety of
RT   optic-nerve malformations.";
RL   Am. J. Hum. Genet. 72:1565-1570(2003).
RN   [30]
RP   VARIANTS AN PRO-19 AND 22-PRO--ARG-26 DEL.
RX   PubMed=12634864; DOI=10.1038/sj.ejhg.5200940;
RA   Vincent M.-C., Pujo A.-L., Olivier D., Calvas P.;
RT   "Screening for PAX6 gene mutations is consistent with
RT   haploinsufficiency as the main mechanism leading to various ocular
RT   defects.";
RL   Eur. J. Hum. Genet. 11:163-169(2003).
RN   [31]
RP   VARIANTS AN ARG-46; ARG-52; THR-56; ASP-73 AND LYS-87, VARIANT
RP   THR-321, CHARACTERIZATION OF VARIANTS AN ARG-46; ARG-52; LEU-53;
RP   THR-56 AND ASP-73, AND CHARACTERIZATION OF VARIANT THR-321.
RX   PubMed=12552561; DOI=10.1002/humu.10163;
RA   Chao L.-Y., Mishra R., Strong L.C., Saunders G.F.;
RT   "Missense mutations in the DNA-binding region and termination codon in
RT   PAX6.";
RL   Hum. Mutat. 21:138-145(2003).
RN   [32]
RP   CHARACTERIZATION OF VARIANT AN THR-242.
RX   PubMed=16493447; DOI=10.1038/sj.ejhg.5201579;
RA   D'Elia A.V., Puppin C., Pellizzari L., Pianta A., Bregant E.,
RA   Lonigro R., Tell G., Fogolari F., van Heyningen V., Damante G.;
RT   "Molecular analysis of a human PAX6 homeobox mutant.";
RL   Eur. J. Hum. Genet. 14:744-751(2006).
RN   [33]
RP   INVOLVEMENT IN ACAMD.
RX   PubMed=17595013; DOI=10.1002/ajmg.a.31808;
RA   Graziano C., D'Elia A.V., Mazzanti L., Moscano F., Guidelli Guidi S.,
RA   Scarano E., Turchetti D., Franzoni E., Romeo G., Damante G., Seri M.;
RT   "A de novo nonsense mutation of PAX6 gene in a patient with aniridia,
RT   ataxia, and mental retardation.";
RL   Am. J. Med. Genet. A 143:1802-1805(2007).
RN   [34]
RP   VARIANT AN ARG-395.
RX   PubMed=21850189;
RA   Zhang X., Wang P., Li S., Xiao X., Guo X., Zhang Q.;
RT   "Mutation spectrum of PAX6 in Chinese patients with aniridia.";
RL   Mol. Vis. 17:2139-2147(2011).
CC   -!- FUNCTION: Transcription factor with important functions in the
CC       development of the eye, nose, central nervous system and pancreas.
CC       Required for the differentiation of pancreatic islet alpha cells
CC       (By similarity). Competes with PAX4 in binding to a common element
CC       in the glucagon, insulin and somatostatin promoters. Regulates
CC       specification of the ventral neuron subtypes by establishing the
CC       correct progenitor domains (By similarity). Isoform 5a appears to
CC       function as a molecular switch that specifies target genes.
CC   -!- SUBUNIT: Interacts with MAF and MAFB (By similarity). Interacts
CC       with TRIM11; this interaction leads to ubiquitination and
CC       proteasomal degradation, as well as inhibition of transactivation,
CC       possibly in part by preventing PAX6 binding to consensus DNA
CC       sequences (By similarity).
CC   -!- INTERACTION:
CC       P63168:Dynll1 (xeno); NbExp=3; IntAct=EBI-747278, EBI-349121;
CC       Q9NSC5:HOMER3; NbExp=3; IntAct=EBI-747278, EBI-748420;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P26367-1; Sequence=Displayed;
CC       Name=5a; Synonyms=Pax6-5a;
CC         IsoId=P26367-2; Sequence=VSP_002366;
CC       Name=3; Synonyms=Pax6-5A,6*;
CC         IsoId=P26367-3; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Fetal eye, brain, spinal cord and olfactory
CC       epithelium. Isoform 5a is less abundant than the PAX6 shorter
CC       form.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing eye and brain.
CC   -!- PTM: Ubiquitinated by TRIM11, leading to ubiquitination and
CC       proteasomal degradation (By similarity).
CC   -!- DISEASE: Defects in PAX6 are the cause of aniridia (AN)
CC       [MIM:106210]. A congenital, bilateral, panocular disorder
CC       characterized by complete absence of the iris or extreme iris
CC       hypoplasia. Aniridia is not just an isolated defect in iris
CC       development but it is associated with macular and optic nerve
CC       hypoplasia, cataract, corneal changes, nystagmus. Visual acuity is
CC       generally low but is unrelated to the degree of iris hypoplasia.
CC       Glaucoma is a secondary problem causing additional visual loss
CC       over time.
CC   -!- DISEASE: Defects in PAX6 are a cause of Peters anomaly (PAN)
CC       [MIM:604229]. Peters anomaly consists of a central corneal
CC       leukoma, absence of the posterior corneal stroma and Descemet
CC       membrane, and a variable degree of iris and lenticular attachments
CC       to the central aspect of the posterior cornea.
CC   -!- DISEASE: Defects in PAX6 are a cause of foveal hypoplasia (FOVHYP)
CC       [MIM:136520]. Foveal hypoplasia can be isolated or associated with
CC       presenile cataract. Inheritance is autosomal dominant.
CC   -!- DISEASE: Defects in PAX6 are a cause of keratitis hereditary
CC       (KERH) [MIM:148190]. An ocular disorder characterized by corneal
CC       opacification, recurrent stromal keratitis and vascularization.
CC   -!- DISEASE: Defects in PAX6 are a cause of coloboma of iris choroid
CC       and retina (COI) [MIM:120200]; also known as uveoretinal coloboma.
CC       Ocular colobomas are a set of malformations resulting from
CC       abnormal morphogenesis of the optic cup and stalk, and the fusion
CC       of the fetal fissure (optic fissure). Severe colobomatous
CC       malformations may cause as much as 10% of the childhood blindness.
CC       The clinical presentation of ocular coloboma is variable. Some
CC       individuals may present with minimal defects in the anterior iris
CC       leaf without other ocular defects. More complex malformations
CC       create a combination of iris, uveoretinal and/or optic nerve
CC       defects without or with microphthalmia or even anophthalmia.
CC   -!- DISEASE: Defects in PAX6 are a cause of coloboma of optic nerve
CC       (COLON) [MIM:120430].
CC   -!- DISEASE: Defects in PAX6 are a cause of bilateral optic nerve
CC       hypoplasia (BONH) [MIM:165550]; also known as bilateral optic
CC       nerve aplasia. A congenital anomaly in which the optic disc
CC       appears abnormally small. It may be an isolated finding or part of
CC       a spectrum of anatomic and functional abnormalities that includes
CC       partial or complete agenesis of the septum pellucidum, other
CC       midline brain defects, cerebral anomalies, pituitary dysfunction,
CC       and structural abnormalities of the pituitary.
CC   -!- DISEASE: Defects in PAX6 are a cause of aniridia cerebellar ataxia
CC       and mental deficiency (ACAMD) [MIM:206700]; also known as
CC       Gillespie syndrome. A rare condition consisting of partial
CC       rudimentary iris, cerebellar impairment of the ability to perform
CC       coordinated voluntary movements, and mental retardation.
CC   -!- SIMILARITY: Belongs to the paired homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: Name=Human PAX6 allelic variant database web site;
CC       URL="http://pax6.hgu.mrc.ac.uk/";
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PAX6";
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DR   EMBL; M77844; AAA59962.1; -; mRNA.
DR   EMBL; M93650; AAA36416.1; -; mRNA.
DR   EMBL; AY047583; AAK95849.1; -; mRNA.
DR   EMBL; BX640762; CAE45868.1; -; mRNA.
DR   EMBL; Z95332; CAG38363.1; -; Genomic_DNA.
DR   EMBL; Z83307; CAG38363.1; JOINED; Genomic_DNA.
DR   EMBL; Z83307; CAG38087.1; -; Genomic_DNA.
DR   EMBL; Z95332; CAG38087.1; JOINED; Genomic_DNA.
DR   EMBL; BC011953; AAH11953.1; -; mRNA.
DR   IPI; IPI00218800; -.
DR   IPI; IPI00449071; -.
DR   PIR; A56674; A56674.
DR   RefSeq; NP_000271.1; NM_000280.3.
DR   RefSeq; NP_001121084.1; NM_001127612.1.
DR   RefSeq; NP_001595.2; NM_001604.4.
DR   UniGene; Hs.270303; -.
DR   UniGene; Hs.611376; -.
DR   PDB; 2CUE; NMR; -; A=211-277.
DR   PDB; 6PAX; X-ray; 2.50 A; A=4-136.
DR   PDBsum; 2CUE; -.
DR   PDBsum; 6PAX; -.
DR   ProteinModelPortal; P26367; -.
DR   SMR; P26367; 4-136, 211-278.
DR   IntAct; P26367; 5.
DR   MINT; MINT-1465118; -.
DR   STRING; P26367; -.
DR   PhosphoSite; P26367; -.
DR   DMDM; 6174889; -.
DR   PRIDE; P26367; -.
DR   DNASU; 5080; -.
DR   Ensembl; ENST00000241001; ENSP00000241001; ENSG00000007372.
DR   Ensembl; ENST00000379107; ENSP00000368401; ENSG00000007372.
DR   Ensembl; ENST00000379109; ENSP00000368403; ENSG00000007372.
DR   Ensembl; ENST00000379111; ENSP00000368406; ENSG00000007372.
DR   Ensembl; ENST00000379115; ENSP00000368410; ENSG00000007372.
DR   Ensembl; ENST00000379123; ENSP00000368418; ENSG00000007372.
DR   Ensembl; ENST00000379129; ENSP00000368424; ENSG00000007372.
DR   Ensembl; ENST00000379132; ENSP00000368427; ENSG00000007372.
DR   Ensembl; ENST00000419022; ENSP00000404100; ENSG00000007372.
DR   Ensembl; ENST00000439164; ENSP00000407893; ENSG00000007372.
DR   GeneID; 5080; -.
DR   KEGG; hsa:5080; -.
DR   UCSC; uc001mtd.4; human.
DR   CTD; 5080; -.
DR   GeneCards; GC11M031768; -.
DR   HGNC; HGNC:8620; PAX6.
DR   HPA; CAB034143; -.
DR   HPA; HPA030775; -.
DR   MIM; 106210; phenotype.
DR   MIM; 120200; phenotype.
DR   MIM; 120430; phenotype.
DR   MIM; 136520; phenotype.
DR   MIM; 148190; phenotype.
DR   MIM; 165550; phenotype.
DR   MIM; 206700; phenotype.
DR   MIM; 604229; phenotype.
DR   MIM; 607108; gene.
DR   neXtProt; NX_P26367; -.
DR   Orphanet; 1065; Aniridia - cerebellar ataxia - intellectual deficit.
DR   Orphanet; 2253; Foveal hypoplasia - presenile cataract.
DR   Orphanet; 2334; Hereditary keratitis.
DR   Orphanet; 250923; Isolated aniridia.
DR   Orphanet; 137902; Isolated optic nerve hypoplasia.
DR   Orphanet; 194; Ocular coloboma.
DR   Orphanet; 708; Peters anomaly.
DR   Orphanet; 893; WAGR syndrome.
DR   PharmGKB; PA32960; -.
DR   eggNOG; NOG326044; -.
DR   GeneTree; ENSGT00650000093130; -.
DR   HOVERGEN; HBG009115; -.
DR   KO; K08031; -.
DR   OMA; AGENTNS; -.
DR   OrthoDB; EOG47PX63; -.
DR   EvolutionaryTrace; P26367; -.
DR   NextBio; 19596; -.
DR   ArrayExpress; P26367; -.
DR   Bgee; P26367; -.
DR   CleanEx; HS_PAX6; -.
DR   Genevestigator; P26367; -.
DR   GermOnline; ENSG00000007372; Homo sapiens.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO:0035035; F:histone acetyltransferase binding; ISS:BHF-UCL.
DR   GO; GO:0019901; F:protein kinase binding; ISS:BHF-UCL.
DR   GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
DR   GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:BHF-UCL.
DR   GO; GO:0000981; F:sequence-specific DNA binding RNA polymerase II transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0008134; F:transcription factor binding; ISS:BHF-UCL.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0001568; P:blood vessel development; IMP:DFLAT.
DR   GO; GO:0061303; P:cornea development in camera-type eye; IMP:DFLAT.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:DFLAT.
DR   GO; GO:0061072; P:iris morphogenesis; IMP:DFLAT.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
DR   GO; GO:0003322; P:pancreatic A cell development; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
DR   GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeodomain.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome;
KW   Developmental protein; Differentiation; Disease mutation; DNA-binding;
KW   Homeobox; Mental retardation; Nucleus; Paired box; Peters anomaly;
KW   Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    422       Paired box protein Pax-6.
FT                                /FTId=PRO_0000050185.
FT   DOMAIN        4    130       Paired.
FT   DNA_BIND    210    269       Homeobox.
FT   COMPBIAS    131    209       Gln/Gly-rich.
FT   COMPBIAS    279    422       Pro/Ser/Thr-rich.
FT   VAR_SEQ      47     47       Q -> QTHADAKVQVLDNQN (in isoform 5a).
FT                                /FTId=VSP_002366.
FT   VARIANT      17     17       N -> S (in AN).
FT                                /FTId=VAR_003808.
FT   VARIANT      18     18       G -> W (in AN).
FT                                /FTId=VAR_003809.
FT   VARIANT      19     19       R -> P (in AN).
FT                                /FTId=VAR_047860.
FT   VARIANT      22     26       Missing (in AN).
FT                                /FTId=VAR_008693.
FT   VARIANT      26     26       R -> G (in PAN).
FT                                /FTId=VAR_003810.
FT   VARIANT      29     29       I -> S (in AN).
FT                                /FTId=VAR_008694.
FT   VARIANT      29     29       I -> V (in AN).
FT                                /FTId=VAR_003811.
FT   VARIANT      33     33       A -> P (in AN).
FT                                /FTId=VAR_008695.
FT   VARIANT      37     39       Missing (in AN).
FT                                /FTId=VAR_008696.
FT   VARIANT      42     42       I -> S (in AN; mild).
FT                                /FTId=VAR_008697.
FT   VARIANT      43     43       S -> P (in AN).
FT                                /FTId=VAR_008698.
FT   VARIANT      44     44       R -> Q (in AN).
FT                                /FTId=VAR_003812.
FT   VARIANT      46     46       L -> R (in AN; shows almost no binding
FT                                efficiency; transcriptional activation
FT                                ability is about 50% lower than that of
FT                                the wild-type protein).
FT                                /FTId=VAR_047861.
FT   VARIANT      52     52       C -> R (in AN; shows almost no binding
FT                                efficiency; transcriptional activation
FT                                ability is about 50% lower than that of
FT                                the wild-type protein).
FT                                /FTId=VAR_047862.
FT   VARIANT      53     53       V -> D (in PAN; also found in patients
FT                                with congenital cataract and foveal
FT                                hypoplasia).
FT                                /FTId=VAR_008700.
FT   VARIANT      53     53       V -> L (in AN; mild; shows 50% lower DNA-
FT                                binding and transactivation ability than
FT                                the wild-type protein).
FT                                /FTId=VAR_008699.
FT   VARIANT      56     56       I -> T (in AN; shows only one-quarter to
FT                                one-third the binding ability of the
FT                                normal wild-type protein; exhibits normal
FT                                transactivation).
FT                                /FTId=VAR_047863.
FT   VARIANT      63     63       T -> P (in AN; mild).
FT                                /FTId=VAR_008701.
FT   VARIANT      64     64       G -> V (in foveal hypoplasia; associated
FT                                with presenile cataract syndrome).
FT                                /FTId=VAR_008702.
FT   VARIANT      68     68       P -> S (in morning glory disk anomaly;
FT                                significant impairment of transcriptional
FT                                activation ability).
FT                                /FTId=VAR_017540.
FT   VARIANT      73     73       G -> D (in AN; shows almost no binding
FT                                efficiency; transcriptional activation
FT                                ability is about 80% of that of the wild-
FT                                type protein).
FT                                /FTId=VAR_047864.
FT   VARIANT      79     79       A -> E (in AN; mild).
FT                                /FTId=VAR_008703.
FT   VARIANT      87     87       I -> K (in AN).
FT                                /FTId=VAR_047865.
FT   VARIANT      87     87       I -> R (in AN; loss of activity).
FT                                /FTId=VAR_003813.
FT   VARIANT     118    118       P -> R (in a family with nystagmus
FT                                associated with a variant form of
FT                                aniridia).
FT                                /FTId=VAR_015065.
FT   VARIANT     119    119       S -> R (in AN).
FT                                /FTId=VAR_008704.
FT   VARIANT     125    125       R -> C (in FOVHYP; isolated).
FT                                /FTId=VAR_017541.
FT   VARIANT     126    126       V -> D (in AN; atypical form).
FT                                /FTId=VAR_008705.
FT   VARIANT     128    128       R -> C (in FOVHYP; isolated).
FT                                /FTId=VAR_003814.
FT   VARIANT     178    178       Q -> H (in AN).
FT                                /FTId=VAR_003815.
FT   VARIANT     208    208       R -> Q (in AN; mild).
FT                                /FTId=VAR_008706.
FT   VARIANT     208    208       R -> W (in AN).
FT                                /FTId=VAR_003816.
FT   VARIANT     242    242       R -> T (in AN; the mutant homeodomain
FT                                binds DNA as well as the wild-type
FT                                homeodomain; the mutant does not modify
FT                                the DNA-binding properties of the paired
FT                                domain; the steady-state levels of the
FT                                full length mutant protein are higher
FT                                than those of the wild-type one; a
FT                                responsive promoter is activated to a
FT                                higher extend by the mutant protein than
FT                                by the wild-type protein; the presence of
FT                                the mutation reduces sensitivity to
FT                                trypsin digestion).
FT                                /FTId=VAR_047866.
FT   VARIANT     258    258       F -> S (in COI; significant impairment of
FT                                transcriptional activation ability).
FT                                /FTId=VAR_017542.
FT   VARIANT     292    292       S -> I (in BONH; significant impairment
FT                                of ability to activate transcription).
FT                                /FTId=VAR_017543.
FT   VARIANT     321    321       A -> T (shows about two-fold higher
FT                                binding efficiency than the normal wild-
FT                                type protein; transcriptional activation
FT                                ability is about 89% of that of the wild-
FT                                type protein).
FT                                /FTId=VAR_047867.
FT   VARIANT     353    353       S -> A (in AN).
FT                                /FTId=VAR_008707.
FT   VARIANT     363    363       S -> P (in PAN).
FT                                /FTId=VAR_017544.
FT   VARIANT     375    375       P -> Q (in AN; reduced DNA binding
FT                                ability).
FT                                /FTId=VAR_015066.
FT   VARIANT     378    378       Q -> R (in optic nerve aplasia).
FT                                /FTId=VAR_017545.
FT   VARIANT     381    381       M -> V (in BONH).
FT                                /FTId=VAR_017546.
FT   VARIANT     387    387       G -> D.
FT                                /FTId=VAR_047868.
FT   VARIANT     391    391       T -> A (in BONH).
FT                                /FTId=VAR_017547.
FT   VARIANT     395    395       G -> R (in AN).
FT                                /FTId=VAR_067698.
FT   VARIANT     422    422       Q -> R (in AN and ocular anterior segment
FT                                anomalies; loss of DNA binding ability).
FT                                /FTId=VAR_008708.
FT   CONFLICT    317    317       R -> L (in Ref. 1; AAA59962).
FT   CONFLICT    369    369       Y -> C (in Ref. 4; CAE45868).
FT   STRAND        6      8
FT   STRAND       14     16
FT   HELIX        23     34
FT   HELIX        39     46
FT   HELIX        50     63
FT   STRAND       77     79
FT   HELIX        81     93
FT   HELIX        99    108
FT   TURN        114    116
FT   HELIX       120    133
FT   HELIX       219    229
FT   HELIX       237    246
FT   HELIX       251    275
SQ   SEQUENCE   422 AA;  46683 MW;  C33CDD2C1B13C397 CRC64;
     MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY
     YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV
     SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ
     EGGGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR
     ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP
     QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT
     SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG TTSTGLISPG VSVPVQVPGS EPDMSQYWPR
     LQ
//
ID   PAX7_HUMAN              Reviewed;         520 AA.
AC   P23759; Q0VA99;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   13-JUN-2012, entry version 132.
DE   RecName: Full=Paired box protein Pax-7;
DE   AltName: Full=HuP1;
GN   Name=PAX7; Synonyms=HUP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX   MEDLINE=97480728; PubMed=9339373; DOI=10.1006/geno.1997.4915;
RA   Vorobyov E., Mertsalov I., Dockhorn-Dworniczak B., Dworniczak B.,
RA   Horst J.;
RT   "The genomic organization and the full coding region of the human PAX7
RT   gene.";
RL   Genomics 45:168-174(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-467 (ISOFORM LONG).
RX   MEDLINE=95075634; PubMed=7527137; DOI=10.1093/nar/22.22.4574;
RA   Schaefer B.W., Czerny T., Bernasconi M., Genini M., Busslinger M.;
RT   "Molecular cloning and characterization of a human PAX-7 cDNA
RT   expressed in normal and neoplastic myocytes.";
RL   Nucleic Acids Res. 22:4574-4582(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE OF 30-195 (ISOFORM SHORT).
RX   MEDLINE=89305521; PubMed=2501086;
RA   Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.;
RT   "Conservation of the paired domain in metazoans and its structure in
RT   three isolated human genes.";
RL   EMBO J. 8:1183-1190(1989).
CC   -!- FUNCTION: Probable transcription factor. May have a role in
CC       myogenesis.
CC   -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX3. Interacts
CC       with DAXX.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P23759-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P23759-2; Sequence=VSP_002370;
CC   -!- DISEASE: Defects in PAX7 are a cause of rhabdomyosarcoma type 2
CC       (RMS2) [MIM:268220]. It is a form of rhabdomyosarcoma, a highly
CC       malignant tumor of striated muscle derived from primitive
CC       mesenchimal cells and exhibiting differentiation along
CC       rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most
CC       frequently occurring soft tissue sarcomas and the most common in
CC       children. It occurs in four forms: alveolar, pleomorphic,
CC       embryonal and botryoidal rhabdomyosarcomas. Note=A chromosomal
CC       aberration involving PAX7 is found in rhabdomyosarcoma.
CC       Translocation t(1;13)(p36;q14) with FOXO1. The resulting protein
CC       is a transcriptional activator.
CC   -!- SIMILARITY: Belongs to the paired homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; X96743; CAA65520.1; -; mRNA.
DR   EMBL; X96744; CAA65521.1; -; Genomic_DNA.
DR   EMBL; X15042; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X15250; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X15251; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96745; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96746; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96747; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96748; CAA65521.1; JOINED; Genomic_DNA.
DR   EMBL; X96744; CAA65522.1; -; Genomic_DNA.
DR   EMBL; X15042; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X15250; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X15251; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X96745; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X96746; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X96747; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; X96748; CAA65522.1; JOINED; Genomic_DNA.
DR   EMBL; AL021528; CAA16432.1; -; Genomic_DNA.
DR   EMBL; CH471134; EAW94853.1; -; Genomic_DNA.
DR   EMBL; BC121165; AAI21166.1; -; mRNA.
DR   EMBL; BC121166; AAI21167.1; -; mRNA.
DR   EMBL; Z35141; CAA84513.1; -; mRNA.
DR   IPI; IPI00004431; -.
DR   IPI; IPI00012894; -.
DR   PIR; S78502; S78502.
DR   RefSeq; NP_001128726.1; NM_001135254.1.
DR   RefSeq; NP_002575.1; NM_002584.2.
DR   RefSeq; NP_039236.1; NM_013945.2.
DR   UniGene; Hs.113253; -.
DR   ProteinModelPortal; P23759; -.
DR   SMR; P23759; 35-160, 217-275.
DR   IntAct; P23759; 4.
DR   MINT; MINT-7241806; -.
DR   STRING; P23759; -.
DR   DMDM; 8247951; -.
DR   PRIDE; P23759; -.
DR   Ensembl; ENST00000375375; ENSP00000364524; ENSG00000009709.
DR   Ensembl; ENST00000400661; ENSP00000383502; ENSG00000009709.
DR   GeneID; 5081; -.
DR   KEGG; hsa:5081; -.
DR   UCSC; uc001bay.3; human.
DR   UCSC; uc001baz.3; human.
DR   CTD; 5081; -.
DR   GeneCards; GC01P018957; -.
DR   HGNC; HGNC:8621; PAX7.
DR   MIM; 167410; gene.
DR   MIM; 268220; phenotype.
DR   neXtProt; NX_P23759; -.
DR   Orphanet; 99756; Alveolar rhabdomyosarcoma.
DR   PharmGKB; PA32961; -.
DR   eggNOG; NOG326044; -.
DR   GeneTree; ENSGT00650000093130; -.
DR   HOGENOM; HOG000230939; -.
DR   HOVERGEN; HBG009115; -.
DR   InParanoid; P23759; -.
DR   KO; K09381; -.
DR   OMA; MSILGNP; -.
DR   OrthoDB; EOG4JM7PH; -.
DR   PhylomeDB; P23759; -.
DR   NextBio; 19602; -.
DR   ArrayExpress; P23759; -.
DR   Bgee; P23759; -.
DR   CleanEx; HS_PAX7; -.
DR   Genevestigator; P23759; -.
DR   GermOnline; ENSG00000009709; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR   GO; GO:0006916; P:anti-apoptosis; TAS:ProtInc.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeodomain.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR022106; Pax7.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00292; PAX; 1.
DR   Pfam; PF12360; Pax7; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chromosomal rearrangement; Complete proteome;
KW   Developmental protein; DNA-binding; Homeobox; Nucleus; Paired box;
KW   Proto-oncogene; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    520       Paired box protein Pax-7.
FT                                /FTId=PRO_0000050194.
FT   DOMAIN       34    163       Paired.
FT   DNA_BIND    217    276       Homeobox.
FT   COMPBIAS    340    346       Poly-Ala.
FT   VAR_SEQ     151    152       Missing (in isoform Short).
FT                                /FTId=VSP_002370.
SQ   SEQUENCE   520 AA;  56896 MW;  3B0F8CC99D65699C CRC64;
     MAALPGTVPR MMRPAPGQNY PRTGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV
     EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPRQVA TPDVEKKIEE
     YKRENPGMFS WEIRDRLLKD GHCDRSTVPS GLVSSISRVL RIKFGKKEEE DEADKKEDDG
     EKKAKHSIDG ILGDKGNRLD EGSDVESEPD LPLKRKQRRS RTTFTAEQLE ELEKAFERTH
     YPDIYTREEL AQRTKLTEAR VQVWFSNRRA RWRKQAGANQ LAAFNHLLPG GFPPTGMPTL
     PPYQLPDSTY PTTTISQDGG STVHRPQPLP PSTMHQGGLA AAAAAADTSS AYGARHSFSS
     YSDSFMNPAA PSNHMNPVSN GLSPQVMSIL GNPSAVPPQP QADFSISPLH GGLDSATSIS
     ASCSQRADSI KPGDSLPTSQ AYCPPTYSTT GYSVDPVAGY QYGQYGQSEC LVPWASPVPI
     PSPTPRASCL FMESYKVVSG WGMSISQMEK LKSSQMEQFT
//
ID   PAX9_HUMAN              Reviewed;         341 AA.
AC   P55771; Q99582; Q9UQR4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   13-JUN-2012, entry version 116.
DE   RecName: Full=Paired box protein Pax-9;
GN   Name=PAX9;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20461864; PubMed=10899593; DOI=10.1016/S0167-4781(00)00130-5;
RA   Hetzer-Egger C., Schorpp M., Boehm T.;
RT   "Evolutionary conservation of gene structures of the Pax1/9 gene
RT   family.";
RL   Biochim. Biophys. Acta 1492:517-521(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-211.
RX   MEDLINE=95072651; PubMed=7981748; DOI=10.1038/ng0493-292;
RA   Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.;
RT   "Chromosomal localization of seven PAX genes and cloning of a novel
RT   family member, PAX-9.";
RL   Nat. Genet. 3:292-298(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-339.
RC   TISSUE=Esophagus;
RX   MEDLINE=97179475; PubMed=9021154; DOI=10.1007/s003359900351;
RA   Peters H., Schuster G., Neubueser A., Richter T., Hoefler H.;
RT   "Isolation of the Pax9 cDNA from adult human esophagus.";
RL   Mamm. Genome 8:62-64(1997).
RN   [5]
RP   INTERACTION WITH KDM5B, MUTAGENESIS OF 173-VAL-PRO-174;
RP   179-VAL-PRO-180 AND PRO-189, AND FUNCTION.
RX   PubMed=12657635; DOI=10.1074/jbc.M301994200;
RA   Tan K., Shaw A.L., Madsen B., Jensen K., Taylor-Papadimitriou J.,
RA   Freemont P.S.;
RT   "Human PLU-1 has transcriptional repression properties and interacts
RT   with the developmental transcription factors BF-1 and PAX9.";
RL   J. Biol. Chem. 278:20507-20513(2003).
RN   [6]
RP   VARIANT STHAG3 SER-51.
RX   MEDLINE=22671556; PubMed=12786960;
RX   DOI=10.1034/j.1600-0722.2003.00036.x;
RA   Mostowska A., Kobielak A., Biedziak B., Trzeciak W.H.;
RT   "Novel mutation in the paired box sequence of PAX9 gene in a sporadic
RT   form of oligodontia.";
RL   Eur. J. Oral Sci. 111:272-276(2003).
CC   -!- FUNCTION: Transcription factor required for normal development of
CC       thymus, parathyroid glands, ultimobranchial bodies, teeth,
CC       skeletal elements of skull and larynx as well as distal limbs (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with KDM5B.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DISEASE: Defects in PAX9 are the cause of tooth agenesis selective
CC       type 3 (STHAG3) [MIM:604625]. A form of selective tooth agenesis,
CC       a common anomaly characterized by the congenital absence of one or
CC       more teeth. Selective tooth agenesis without associated systemic
CC       disorders has sometimes been divided into 2 types: oligodontia,
CC       defined as agenesis of 6 or more permanent teeth, and hypodontia,
CC       defined as agenesis of less than 6 teeth. The number in both cases
CC       does not include absence of third molars (wisdom teeth).
CC   -!- SIMILARITY: Contains 1 paired domain.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/PAX9ID41644ch14q12.html";
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DR   EMBL; AJ238381; CAB41533.1; -; Genomic_DNA.
DR   EMBL; AJ238382; CAB41533.1; JOINED; Genomic_DNA.
DR   EMBL; AJ238383; CAB41533.1; JOINED; Genomic_DNA.
DR   EMBL; BC001159; AAH01159.1; -; mRNA.
DR   EMBL; L09745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X92850; CAA63436.1; -; mRNA.
DR   IPI; IPI00413469; -.
DR   PIR; S36155; S36155.
DR   RefSeq; NP_006185.1; NM_006194.3.
DR   UniGene; Hs.132576; -.
DR   UniGene; Hs.609574; -.
DR   ProteinModelPortal; P55771; -.
DR   SMR; P55771; 8-130.
DR   STRING; P55771; -.
DR   DMDM; 8247954; -.
DR   PRIDE; P55771; -.
DR   DNASU; 5083; -.
DR   Ensembl; ENST00000361487; ENSP00000355245; ENSG00000198807.
DR   Ensembl; ENST00000402703; ENSP00000384817; ENSG00000198807.
DR   GeneID; 5083; -.
DR   KEGG; hsa:5083; -.
DR   UCSC; uc001wty.4; human.
DR   CTD; 5083; -.
DR   GeneCards; GC14P037126; -.
DR   HGNC; HGNC:8623; PAX9.
DR   HPA; HPA038462; -.
DR   MIM; 167416; gene.
DR   MIM; 604625; phenotype.
DR   neXtProt; NX_P55771; -.
DR   Orphanet; 2227; Hypodontia.
DR   PharmGKB; PA32963; -.
DR   eggNOG; NOG252808; -.
DR   HOGENOM; HOG000230938; -.
DR   HOVERGEN; HBG009115; -.
DR   InParanoid; P55771; -.
DR   KO; K09382; -.
DR   OMA; HGWQHAG; -.
DR   OrthoDB; EOG4RBQJV; -.
DR   PhylomeDB; P55771; -.
DR   NextBio; 19612; -.
DR   ArrayExpress; P55771; -.
DR   Bgee; P55771; -.
DR   CleanEx; HS_PAX9; -.
DR   Genevestigator; P55771; -.
DR   GermOnline; ENSG00000198807; Homo sapiens.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001523; Paired_box_N.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Pfam; PF00292; PAX; 1.
DR   PRINTS; PR00027; PAIREDBOX.
DR   SMART; SM00351; PAX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS00034; PAIRED_1; 1.
DR   PROSITE; PS51057; PAIRED_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Developmental protein; Disease mutation;
KW   DNA-binding; Nucleus; Paired box; Polymorphism; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    341       Paired box protein Pax-9.
FT                                /FTId=PRO_0000050203.
FT   DOMAIN        4    130       Paired.
FT   REGION      168    189       Interaction with KDM5B.
FT   VARIANT      51     51       G -> S (in STHAG3).
FT                                /FTId=VAR_015698.
FT   VARIANT     240    240       A -> P (in dbSNP:rs4904210).
FT                                /FTId=VAR_034371.
FT   MUTAGEN     173    174       VP->AA: Abolishes interaction with KDM5B.
FT   MUTAGEN     179    180       VP->AA: Abolishes interaction with KDM5B.
FT   MUTAGEN     189    189       P->A: Abolishes interaction with KDM5B.
FT   CONFLICT    211    211       V -> G (in Ref. 3; L09745).
SQ   SEQUENCE   341 AA;  36310 MW;  F5E6B0BC991E7C1D CRC64;
     MEPAFGEVNQ LGGVFVNGRP LPNAIRLRIV ELAQLGIRPC DISRQLRVSH GCVSKILARY
     NETGSILPGA IGGSKPRVTT PTVVKHIRTY KQRDPGIFAW EIRDRLLADG VCDKYNVPSV
     SSISRILRNK IGNLAQQGHY DSYKQHQPTP QPALPYNHIY SYPSPITAAA AKVPTPPGVP
     AIPGSVAMPR TWPSSHSVTD ILGIRSITDQ VSDSSPYHSP KVEEWSSLGR NNFPAAAPHA
     VNGLEKGALE QEAKYGQAPN GLPAVGSFVS ASSMAPYPTP AQVSPYMTYS AAPSGYVAGH
     GWQHAGGTSL SPHNCDIPAS LAFKGMQAAR EGSHSVTASA L
//
ID   PAXI_HUMAN              Reviewed;         591 AA.
AC   P49023; B2RAI3; B7ZMB4; O14970; O14971; O60360; Q5HYA4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   13-JUN-2012, entry version 135.
DE   RecName: Full=Paxillin;
GN   Name=PXN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND VARIANT GLY-73.
RX   MEDLINE=95197488; PubMed=7534286; DOI=10.1074/jbc.270.10.5039;
RA   Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S.,
RA   Sobhany E.S., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R.,
RA   Chen L.B., Griffin J.D.;
RT   "Molecular cloning of human paxillin, a focal adhesion protein
RT   phosphorylated by P210BCR/ABL.";
RL   J. Biol. Chem. 270:5039-5047(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-73.
RA   Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V.,
RA   Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M.,
RA   Lathrop M., Cox R.D., Bell G.I.;
RT   "Transcription map of the 5cM region surrounding the hepatocyte
RT   nuclear factor-1a/MODY3 gene on chromosome 12.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA), AND VARIANT
RP   GLY-73.
RC   TISSUE=Placenta;
RX   MEDLINE=97207310; PubMed=9054445; DOI=10.1074/jbc.272.11.7437;
RA   Mazaki Y., Hashimoto S., Sabe H.;
RT   "Monocyte cells and cancer cells express novel paxillin isoforms with
RT   different binding properties to focal adhesion proteins.";
RL   J. Biol. Chem. 272:7437-7444(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
RP   GLY-73.
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Fetal kidney;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT
RP   GLY-73.
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   INTERACTION WITH ITGA4.
RX   PubMed=10604475; DOI=10.1038/45264;
RA   Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M.,
RA   Ginsberg M.H.;
RT   "Binding of paxillin to alpha4 integrins modifies integrin-dependent
RT   biological responses.";
RL   Nature 402:676-681(1999).
RN   [9]
RP   INTERACTION WITH GIT1.
RX   PubMed=10938112; DOI=10.1128/MCB.20.17.6354-6363.2000;
RA   Zhao Z.-S., Manser E., Loo T.-H., Lim L.;
RT   "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes
RT   focal complex disassembly.";
RL   Mol. Cell. Biol. 20:6354-6363(2000).
RN   [10]
RP   INTERACTION WITH ASAP2.
RX   MEDLINE=20214823; PubMed=10749932;
RA   Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.;
RT   "A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an
RT   ADP-ribosylation factor GTPase-activating protein activity, is
RT   involved in paxillin recruitment to focal adhesions and cell
RT   migration.";
RL   Mol. Biol. Cell 11:1315-1327(2000).
RN   [11]
RP   PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181.
RX   MEDLINE=21634701; PubMed=11774284; DOI=10.1002/ijc.1609;
RA   Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H.,
RA   Schaefer E., Tatsuta M., Tsujimura T., Terada N., Kakishita E.,
RA   Akedo H.;
RT   "Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in
RT   MM1 cancer cell migration.";
RL   Int. J. Cancer 97:330-335(2002).
RN   [12]
RP   INTERACTION WITH RNF5.
RX   PubMed=12861019; DOI=10.1128/MCB.23.15.5331-5345.2003;
RA   Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S.,
RA   Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H.,
RA   Ronai Z.;
RT   "RNF5, a RING finger protein that regulates cell motility by targeting
RT   paxillin ubiquitination and altered localization.";
RL   Mol. Cell. Biol. 23:5331-5345(2003).
RN   [13]
RP   PHOSPHORYLATION AT TYR-31 AND TYR-118, AND INTERACTION WITH PTK6.
RX   PubMed=15572663; DOI=10.1128/MCB.24.24.10558-10572.2004;
RA   Chen H.Y., Shen C.H., Tsai Y.T., Lin F.C., Huang Y.P., Chen R.H.;
RT   "Brk activates rac1 and promotes cell migration and invasion by
RT   phosphorylating paxillin.";
RL   Mol. Cell. Biol. 24:10558-10572(2004).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16212419; DOI=10.1021/pr050134h;
RA   Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.;
RT   "Phosphoproteome analysis of HeLa cells using stable isotope labeling
RT   with amino acids in cell culture (SILAC).";
RL   J. Proteome Res. 4:1661-1671(2005).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mammary epithelium;
RX   PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200;
RA   Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,
RA   Lauffenburger D.A., White F.M.;
RT   "Time-resolved mass spectrometry of tyrosine phosphorylation sites in
RT   the epidermal growth factor receptor signaling network reveals dynamic
RT   modules.";
RL   Mol. Cell. Proteomics 4:1240-1250(2005).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=16094384; DOI=10.1038/nmeth776;
RA   Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,
RA   Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
RT   "Quantitative phosphoproteome analysis using a dendrimer conjugation
RT   chemistry and tandem mass spectrometry.";
RL   Nat. Methods 2:591-598(2005).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118 AND SER-303, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Lung carcinoma;
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [21]
RP   PHOSPHORYLATION AT SER-244.
RX   PubMed=18042622; DOI=10.1242/jcs.018218;
RA   Miyamoto Y., Yamauchi J., Chan J.R., Okada A., Tomooka Y.,
RA   Hisanaga S., Tanoue A.;
RT   "Cdk5 regulates differentiation of oligodendrocyte precursor cells
RT   through the direct phosphorylation of paxillin.";
RL   J. Cell Sci. 120:4355-4366(2007).
RN   [22]
RP   INTERACTION WITH NEK3.
RX   PubMed=17297458; DOI=10.1038/sj.onc.1210264;
RA   Miller S.L., Antico G., Raghunath P.N., Tomaszewski J.E.,
RA   Clevenger C.V.;
RT   "Nek3 kinase regulates prolactin-mediated cytoskeletal reorganization
RT   and motility of breast cancer cells.";
RL   Oncogene 26:4668-4678(2007).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; TYR-88 AND TYR-118,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Mammary epithelium;
RX   PubMed=17389395; DOI=10.1073/pnas.0608638104;
RA   Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
RT   "Multiple reaction monitoring for robust quantitative proteomic
RT   analysis of cellular signaling networks.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-106; SER-126;
RP   SER-130 AND SER-137, AND MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [27]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-106, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31; TYR-88 AND TYR-118,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Mammary epithelium;
RX   PubMed=19534553; DOI=10.1021/pr900044c;
RA   Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,
RA   Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,
RA   Wiley H.S., Qian W.-J.;
RT   "An extensive survey of tyrosine phosphorylation revealing new sites
RT   in human mammary epithelial cells.";
RL   J. Proteome Res. 8:3852-3861(2009).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND THR-318,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [30]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-126, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [31]
RP   INTERACTION WITH PDCD10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   7-LEU-LEU-8.
RX   PubMed=20489202; DOI=10.1074/jbc.M110.128470;
RA   Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J.;
RT   "Crystal structure of CCM3, a cerebral cavernous malformation protein
RT   critical for vascular integrity.";
RL   J. Biol. Chem. 285:24099-24107(2010).
RN   [32]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 262-274 IN COMPLEX WITH
RP   PTK2/FAK1, AND INTERACTION WITH PTK2/FAK1.
RX   PubMed=14527389; DOI=10.1016/j.str.2003.08.010;
RA   Hoellerer M.K., Noble M.E., Labesse G., Campbell I.D., Werner J.M.,
RA   Arold S.T.;
RT   "Molecular recognition of paxillin LD motifs by the focal adhesion
RT   targeting domain.";
RL   Structure 11:1207-1217(2003).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 262-274 IN COMPLEX WITH
RP   PTK2B/PYK2, AND INTERACTION WITH PTK2B/PYK2.
RX   PubMed=19358827; DOI=10.1016/j.bbrc.2009.04.011;
RA   Lulo J., Yuzawa S., Schlessinger J.;
RT   "Crystal structures of free and ligand-bound focal adhesion targeting
RT   domain of Pyk2.";
RL   Biochem. Biophys. Res. Commun. 383:347-352(2009).
CC   -!- FUNCTION: Cytoskeletal protein involved in actin-membrane
CC       attachment at sites of cell adhesion to the extracellular matrix
CC       (focal adhesion).
CC   -!- SUBUNIT: Binds in vitro to vinculin as well as to the SH3 domain
CC       of SRC and, when tyrosine phosphorylated, to the SH2 domain of V-
CC       CRK. Isoform beta binds to PTK2/FAK1 but weakly to vinculin.
CC       Isoform gamma binds to vinculin but only weakly to PTK2/FAK1.
CC       Interacts with GIT1, NUDT16L1/SDOS, PARVA and TGFB1I1. Component
CC       of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and
CC       PAK1 (By similarity). Interacts with PTK2/FAK1 and PTK2B/PYK2.
CC       Binds ASAP2. Interacts with unphosphorylated ITGA4. Interacts with
CC       RNF5 and PDCD10. Interacts with NEK3 and this interaction is
CC       prolactin-dependent. Interacts with PTK6.
CC   -!- INTERACTION:
CC       Q05397:PTK2; NbExp=7; IntAct=EBI-702209, EBI-702142;
CC       Q09463:rnf-5 (xeno); NbExp=2; IntAct=EBI-702209, EBI-963421;
CC       Q99942:RNF5; NbExp=6; IntAct=EBI-702209, EBI-348482;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
CC       focal adhesion. Cytoplasm, cell cortex (By similarity).
CC       Note=Colocalizes with integrins at the cell periphery (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Beta;
CC         IsoId=P49023-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=P49023-2; Sequence=VSP_003114;
CC       Name=Gamma;
CC         IsoId=P49023-3; Sequence=VSP_003115;
CC       Name=4;
CC         IsoId=P49023-4; Sequence=VSP_040483, VSP_003114;
CC   -!- PTM: Phosphorylated by MAPK1/ERK2 (By similarity). Phosphorylated
CC       on tyrosine residues during integrin-mediated cell adhesion,
CC       embryonic development, fibroblast transformation and following
CC       stimulation of cells by mitogens. Phosphorylation at Ser-244 by
CC       CDK5 reduces its interaction with PTK2/FAK1 in matrix-cell focal
CC       adhesions (MCFA) during oligodendrocytes (OLs) differentiation.
CC       Phosphorylation at Tyr-31 and Tyr-118 by PTK6 promote the
CC       activation of RAC1 via CRK/CrKII, thereby promoting migration and
CC       invasion.
CC   -!- SIMILARITY: Belongs to the paxillin family.
CC   -!- SIMILARITY: Contains 4 LIM zinc-binding domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U14588; AAC50104.1; -; mRNA.
DR   EMBL; U87946; AAD00648.1; -; Genomic_DNA.
DR   EMBL; U87941; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; U87942; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; U87943; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; U87944; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; U87945; AAD00648.1; JOINED; Genomic_DNA.
DR   EMBL; D86862; BAA18997.1; -; mRNA.
DR   EMBL; D86863; BAA18998.1; -; mRNA.
DR   EMBL; AK314204; BAG36880.1; -; mRNA.
DR   EMBL; BX648777; CAI46024.1; -; mRNA.
DR   EMBL; AC004263; AAC05175.1; -; Genomic_DNA.
DR   EMBL; BC136787; AAI36788.1; -; mRNA.
DR   EMBL; BC136794; AAI36795.1; -; mRNA.
DR   EMBL; BC144410; AAI44411.1; -; mRNA.
DR   IPI; IPI00220030; -.
DR   IPI; IPI00220031; -.
DR   IPI; IPI00335634; -.
DR   IPI; IPI00890738; -.
DR   PIR; A55933; A55933.
DR   RefSeq; NP_001074324.1; NM_001080855.2.
DR   RefSeq; NP_001230685.1; NM_001243756.1.
DR   RefSeq; NP_002850.2; NM_002859.3.
DR   RefSeq; NP_079433.3; NM_025157.4.
DR   UniGene; Hs.446336; -.
DR   PDB; 1KKY; Model; -; A=142-157.
DR   PDB; 1KL0; Model; -; B=142-157.
DR   PDB; 1OW6; X-ray; 2.35 A; D/F=262-274.
DR   PDB; 1OW7; X-ray; 2.60 A; D/E/F=262-274.
DR   PDB; 1OW8; X-ray; 2.85 A; D/F=141-153.
DR   PDB; 2O9V; X-ray; 1.63 A; B=45-54.
DR   PDB; 2VZD; X-ray; 2.10 A; C/D=1-20.
DR   PDB; 2VZG; X-ray; 1.80 A; A=141-160.
DR   PDB; 2VZI; X-ray; 2.20 A; A=262-315.
DR   PDB; 3GM1; X-ray; 2.95 A; C/D/E/F=262-274.
DR   PDB; 3PY7; X-ray; 2.29 A; A=1-10.
DR   PDB; 3RQE; X-ray; 2.80 A; E=2-15.
DR   PDB; 3RQF; X-ray; 2.70 A; E=141-153.
DR   PDB; 3RQG; X-ray; 2.50 A; E=262-274.
DR   PDBsum; 1KKY; -.
DR   PDBsum; 1KL0; -.
DR   PDBsum; 1OW6; -.
DR   PDBsum; 1OW7; -.
DR   PDBsum; 1OW8; -.
DR   PDBsum; 2O9V; -.
DR   PDBsum; 2VZD; -.
DR   PDBsum; 2VZG; -.
DR   PDBsum; 2VZI; -.
DR   PDBsum; 3GM1; -.
DR   PDBsum; 3PY7; -.
DR   PDBsum; 3RQE; -.
DR   PDBsum; 3RQF; -.
DR   PDBsum; 3RQG; -.
DR   ProteinModelPortal; P49023; -.
DR   SMR; P49023; 357-590.
DR   DIP; DIP-33851N; -.
DR   IntAct; P49023; 20.
DR   MINT; MINT-92615; -.
DR   STRING; P49023; -.
DR   DMDM; 27735219; -.
DR   PRIDE; P49023; -.
DR   Ensembl; ENST00000228307; ENSP00000228307; ENSG00000089159.
DR   Ensembl; ENST00000267257; ENSP00000267257; ENSG00000089159.
DR   Ensembl; ENST00000424649; ENSP00000391283; ENSG00000089159.
DR   Ensembl; ENST00000458477; ENSP00000395536; ENSG00000089159.
DR   GeneID; 5829; -.
DR   KEGG; hsa:5829; -.
DR   UCSC; uc001txt.3; human.
DR   UCSC; uc001txv.3; human.
DR   UCSC; uc001txx.3; human.
DR   UCSC; uc001txy.3; human.
DR   CTD; 5829; -.
DR   GeneCards; GC12M120648; -.
DR   HGNC; HGNC:9718; PXN.
DR   HPA; CAB003841; -.
DR   MIM; 602505; gene.
DR   neXtProt; NX_P49023; -.
DR   PharmGKB; PA34062; -.
DR   eggNOG; NOG267887; -.
DR   GeneTree; ENSGT00640000091240; -.
DR   HOVERGEN; HBG001512; -.
DR   KO; K05760; -.
DR   Pathway_Interaction_DB; angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
DR   Pathway_Interaction_DB; arf6cyclingpathway; Arf6 signaling events.
DR   Pathway_Interaction_DB; ephbfwdpathway; EPHB forward signaling.
DR   Pathway_Interaction_DB; fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
DR   Pathway_Interaction_DB; igf1_pathway; IGF1 pathway.
DR   Pathway_Interaction_DB; avb3_integrin_pathway; Integrins in angiogenesis.
DR   Pathway_Interaction_DB; lysophospholipid_pathway; LPA receptor mediated events.
DR   Pathway_Interaction_DB; a4b1_paxdep_pathway; Paxillin-dependent events mediated by a4b1.
DR   Pathway_Interaction_DB; a4b1_paxindep_pathway; Paxillin-independent events mediated by a4b1 and a4b7.
DR   Pathway_Interaction_DB; met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).
DR   Pathway_Interaction_DB; vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
DR   Pathway_Interaction_DB; ret_pathway; Signaling events regulated by Ret tyrosine kinase.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_111155; Cell-Cell communication.
DR   Reactome; REACT_116125; Disease.
DR   Reactome; REACT_17044; Muscle contraction.
DR   EvolutionaryTrace; P49023; -.
DR   NextBio; 22710; -.
DR   PMAP-CutDB; P49023; -.
DR   ArrayExpress; P49023; -.
DR   Bgee; P49023; -.
DR   CleanEx; HS_PXN; -.
DR   Genevestigator; P49023; -.
DR   GermOnline; ENSG00000089159; Homo sapiens.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL.
DR   GO; GO:0030027; C:lamellipodium; IDA:BHF-UCL.
DR   GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR   GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0034614; P:cellular response to reactive oxygen species; IEP:BHF-UCL.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0060396; P:growth hormone receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0006936; P:muscle contraction; TAS:Reactome.
DR   GO; GO:0007172; P:signal complex assembly; TAS:ProtInc.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 4.
DR   InterPro; IPR001904; Paxillin.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00412; LIM; 4.
DR   PRINTS; PR00832; PAXILLIN.
DR   SMART; SM00132; LIM; 4.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW   Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; LIM domain;
KW   Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; Zinc.
FT   CHAIN         1    591       Paxillin.
FT                                /FTId=PRO_0000075853.
FT   DOMAIN      356    415       LIM zinc-binding 1.
FT   DOMAIN      416    473       LIM zinc-binding 2.
FT   DOMAIN      474    533       LIM zinc-binding 3.
FT   DOMAIN      534    591       LIM zinc-binding 4.
FT   MOTIF         3     15       LD motif 1.
FT   MOTIF       144    156       LD motif 2.
FT   MOTIF       216    228       LD motif 3.
FT   MOTIF       265    276       LD motif 4.
FT   MOTIF       333    345       LD motif 5.
FT   COMPBIAS     46     53       Pro-rich.
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES      31     31       Phosphotyrosine; by PTK6.
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES      84     84       Phosphoserine.
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES      88     88       Phosphotyrosine.
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     109    109       Phosphoserine (By similarity).
FT   MOD_RES     118    118       Phosphotyrosine; by PTK6.
FT   MOD_RES     126    126       Phosphoserine.
FT   MOD_RES     130    130       Phosphoserine.
FT   MOD_RES     137    137       Phosphoserine.
FT   MOD_RES     181    181       Phosphotyrosine.
FT   MOD_RES     244    244       Phosphoserine; by CDK5.
FT   MOD_RES     303    303       Phosphoserine.
FT   MOD_RES     318    318       Phosphothreonine.
FT   VAR_SEQ       1    133       Missing (in isoform 4).
FT                                /FTId=VSP_040483.
FT   VAR_SEQ     278    311       Missing (in isoform Alpha and isoform 4).
FT                                /FTId=VSP_003114.
FT   VAR_SEQ     278    311       IQGLEQRADGERCWAAGWPRDGGRSSPGGQDEGG -> GSW
FT                                PLEEVVLLVSISSSVQEGEKYPHPCAARHRTPSLRSPDQPP
FT                                PCPQ (in isoform Gamma).
FT                                /FTId=VSP_003115.
FT   VARIANT      73     73       S -> G (in dbSNP:rs4767884).
FT                                /FTId=VAR_065099.
FT   MUTAGEN       7      8       LL->RR: Loss of interaction with PDCD10.
FT   CONFLICT    280    280       G -> D (in Ref. 3; BAA18997).
FT   CONFLICT    327    327       P -> L (in Ref. 5; CAI46024).
FT   CONFLICT    413    413       F -> S (in Ref. 5; CAI46024).
FT   HELIX       143    155
SQ   SEQUENCE   591 AA;  64505 MW;  ABF6C0BE5939623F CRC64;
     MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG
     TILDPLDQWQ PSSSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDSVGSPCSR VGEEEHVYSF
     PNKQKSAEPS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSS PPLPGALSPL
     YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG
     EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFKIQG LEQRADGERC WAAGWPRDGG
     RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA
     CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH NLFSPRCYYC
     NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA
     RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK
     PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C
//
ID   RS24_TAKRU              Reviewed;         132 AA.
AC   O42387;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-MAY-2012, entry version 54.
DE   RecName: Full=40S ribosomal protein S24;
GN   Name=rps24;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Crosio C., Cecconi F., Giorgi M., Amaldi F., Mariottini P.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ribosomal protein S24e family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ001398; CAA04728.1; -; Genomic_DNA.
DR   ProteinModelPortal; O42387; -.
DR   STRING; O42387; -.
DR   PRIDE; O42387; -.
DR   eggNOG; COG2004; -.
DR   InParanoid; O42387; -.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR012678; Ribosomal_L23/L15e_core_dom.
DR   InterPro; IPR001976; Ribosomal_S24e.
DR   InterPro; IPR018098; Ribosomal_S24e_CS.
DR   PANTHER; PTHR10496; Ribosomal_S24E; 1.
DR   Pfam; PF01282; Ribosomal_S24e; 1.
DR   ProDom; PD006052; Ribosomal_S24e; 1.
DR   SUPFAM; SSF54189; L23_L15e_core; 1.
DR   PROSITE; PS00529; RIBOSOMAL_S24E; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN         1    132       40S ribosomal protein S24.
FT                                /FTId=PRO_0000137627.
SQ   SEQUENCE   132 AA;  15305 MW;  DC437F60F20C14F5 CRC64;
     MNDTVTVRTR KFMTNRLLQR KQMVVDVLHP GKATVPKTEI REKLAKMYKT TPDVVFVFGF
     RTQFGGGKTT GFAMVYDSLD YAKKNEPKHR LARHGLFEKK KTSRKQRKER KNRMKKVRGT
     KKASVGASKK KD
//
ID   RS7_TAKRU               Reviewed;         194 AA.
AC   P50894; P53548;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 53.
DE   RecName: Full=40S ribosomal protein S7;
GN   Name=rps7;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96371061; PubMed=8774896; DOI=10.1093/nar/24.16.3167;
RA   Cecconi F., Crosio C., Mariottini P., Cesareni G., Giorgi M.,
RA   Brenner S., Amaldi F.;
RT   "A functional role for some Fugu introns larger than the typical short
RT   ones: the example of the gene coding for ribosomal protein S7 and
RT   snoRNA U17.";
RL   Nucleic Acids Res. 24:3167-3172(1996).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S7e family.
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DR   EMBL; X94942; CAA64412.1; -; Genomic_DNA.
DR   STRING; P50894; -.
DR   PRIDE; P50894; -.
DR   Ensembl; ENSTRUT00000040395; ENSTRUP00000040253; ENSTRUG00000015750.
DR   eggNOG; NOG280542; -.
DR   GeneTree; ENSGT00390000014122; -.
DR   InParanoid; P50894; -.
DR   OMA; KFSDRHV; -.
DR   OrthoDB; EOG4GQQ61; -.
DR   GO; GO:0030686; C:90S preribosome; ISS:RefGenome.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; ISS:RefGenome.
DR   GO; GO:0032040; C:small-subunit processome; ISS:RefGenome.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; ISS:RefGenome.
DR   GO; GO:0006364; P:rRNA processing; ISS:RefGenome.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR000554; Ribosomal_S7e.
DR   PANTHER; PTHR11278; Ribosomal_S7E; 1.
DR   Pfam; PF01251; Ribosomal_S7e; 1.
DR   PROSITE; PS00948; RIBOSOMAL_S7E; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Reference proteome; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN         1    194       40S ribosomal protein S7.
FT                                /FTId=PRO_0000174194.
FT   COMPBIAS     98    120       Arg/Lys-rich (basic).
SQ   SEQUENCE   194 AA;  22206 MW;  D202501948D47E86 CRC64;
     MFSTSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGSRKAI
     IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRS KNKQKRPRSR
     TLTSVHDAIL EDLVFPSEIV GKRIRVKMDS SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL
     TGKDVVFEFP EFQL
//
ID   SSRL_TAKRU              Reviewed;         289 AA.
AC   O42179;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-MAY-2012, entry version 60.
DE   RecName: Full=Somatostatin-like receptor F_48D10.1;
GN   ORFNames=F_48D10.1;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hawkins J., Gillam B.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -!- CAUTION: Seems to lack the C-terminal part (TM6 and TM7).
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DR   EMBL; AF013613; AAB86684.1; -; Genomic_DNA.
DR   ProteinModelPortal; O42179; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    289       Somatostatin-like receptor F_48D10.1.
FT                                /FTId=PRO_0000070133.
FT   TOPO_DOM      1     57       Extracellular (Potential).
FT   TRANSMEM     58     79       Helical; Name=1; (Potential).
FT   TOPO_DOM     80     89       Cytoplasmic (Potential).
FT   TRANSMEM     90    110       Helical; Name=2; (Potential).
FT   TOPO_DOM    111    126       Extracellular (Potential).
FT   TRANSMEM    127    148       Helical; Name=3; (Potential).
FT   TOPO_DOM    149    170       Cytoplasmic (Potential).
FT   TRANSMEM    171    191       Helical; Name=4; (Potential).
FT   TOPO_DOM    192    240       Extracellular (Potential).
FT   TRANSMEM    241    261       Helical; Name=5; (Potential).
FT   TOPO_DOM    262    289       Cytoplasmic (Potential).
FT   CARBOHYD     40     40       N-linked (GlcNAc...) (Potential).
FT   DISULFID    125    221       By similarity.
SQ   SEQUENCE   289 AA;  32172 MW;  4F5A1776911D0ADA CRC64;
     MEPLDQTPGF PLSPEPNYWY ETTPSLLLVS YPHLLDISSN QSTQSVPFQG SSALLTAVIY
     ITVFVVGLTG NTLAIYVVLR YAGMKTVTNI YILNLAVADE LYIVGLPFLA TQNVLSYWPF
     GSFLCRVVMT ADSMNQFTSI FCLTVMSIDR YLAVVHPIRS TKWRHPRVAK VVSAAVWAVS
     FVVVLPVVIF SDVQVRPSRP LQVGTSSKCL VKRVQETFNS CNMIWPEPKN VWSTAFILYT
     AMVGFFGPLL IICLCYLLIV IKVRHRMSAA QVGAVVSTCP LNICCLSRR
//
ID   SYHC_TAKRU              Reviewed;         519 AA.
AC   P70076;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-MAY-2012, entry version 76.
DE   RecName: Full=Histidine--tRNA ligase, cytoplasmic;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hars; Synonyms=hiss;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=96323249; PubMed=8710896; DOI=10.1073/pnas.93.16.8485;
RA   Brenner S., Corrochano L.M.;
RT   "Translocation events in the evolution of aminoacyl-tRNA
RT   synthetases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8485-8489(1996).
CC   -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP +
CC       diphosphate + L-histidyl-tRNA(His).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; Z54243; CAA91012.1; -; Genomic_DNA.
DR   ProteinModelPortal; P70076; -.
DR   SMR; P70076; 32-66.
DR   STRING; P70076; -.
DR   Ensembl; ENSTRUT00000023098; ENSTRUP00000023002; ENSTRUG00000009144.
DR   eggNOG; COG0124; -.
DR   GeneTree; ENSGT00390000005922; -.
DR   OMA; LVSELWD; -.
DR   BRENDA; 6.1.1.21; 7222.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR015807; His-tRNA-synth_IIa_subgr.
DR   InterPro; IPR004516; His-tRNA_synth_IIA.
DR   PANTHER; PTHR11476; His-tRNA_synth; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF52954; Anticodon_bd; 1.
DR   TIGRFAMs; TIGR00442; HisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    519       Histidine--tRNA ligase, cytoplasmic.
FT                                /FTId=PRO_0000136337.
SQ   SEQUENCE   519 AA;  57913 MW;  A1CBF5752070759E CRC64;
     MLAMHCARVC SVLMGCRTTT RALSIRSFPG VTLAQIDEEV AKLLELKAHL GGDDGKHQFV
     LKTAKGTRDY NPKQMAIREK VFNTIVSCFK RHGAETIDTP VFELKETLTG KYGEDSKLIY
     DLKDQGGELL SLRYDLTVPF ARYLAMNKIT NIKRYHIAKV YRRDNPAMTR GRYREFYQCD
     FDIAGQYDAM IPDAECLKIV HEILSELDLG DFRIKVNDRR ILDGMFAVCG VPDNMFRTIC
     STVDKLDKLP WEAVKNEMVN EKGLSEEAAD QIGVYVGMQG GMDLAERLLQ DQKMCQSTQA
     CAGLTDIKLL FSYLQLFQVT DKVVFDLSLA RGLDYYTGII YEAILTQAGV APVAPETSNE
     APTEECVTVG SVAGGGRYDG LVGMFDPKGR KVPCVGVSIG IERIFSIMEQ KAEASTEKIR
     TTEVQVMVAA AQKNLLEERL RLITELWNAG IKAELMYKKS PKLLSQLQHC EESGIPLVAI
     LGEQELKNGV VKLRNVATRD EVDISRADLI AEIKKRTSA
//
ID   SYVC_TAKRU              Reviewed;        1217 AA.
AC   P49696;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   16-MAY-2012, entry version 77.
DE   RecName: Full=Valine--tRNA ligase;
DE            EC=6.1.1.9;
DE   AltName: Full=Valyl-tRNA synthetase;
DE            Short=ValRS;
GN   Name=vars; Synonyms=vars1;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97396021; PubMed=9254008;
RA   Lim E.H., Corrochano L.M., Elgar G., Brenner S.;
RT   "Genomic structure and sequence analysis of the valyl-tRNA synthetase
RT   gene of the Japanese pufferfish, Fugu rubripes.";
RL   DNA Seq. 7:141-151(1997).
CC   -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate
CC       + L-valyl-tRNA(Val).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
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DR   EMBL; X91856; CAA62967.1; -; Genomic_DNA.
DR   ProteinModelPortal; P49696; -.
DR   STRING; P49696; -.
DR   PRIDE; P49696; -.
DR   eggNOG; COG0525; -.
DR   OrthoDB; EOG4QZ7K3; -.
DR   BRENDA; 6.1.1.9; 7222.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; G3DSA:3.90.740.10; G3DSA:3.90.740.10; 1.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 3.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   InterPro; IPR013155; V/L/I-tRNA-synth_anticodon-bd.
DR   InterPro; IPR019499; Val-tRNA_synth_Ia_tRNA-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_synthetase.
DR   PANTHER; PTHR11946:SF5; tRNA-synt_val; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
DR   Pfam; PF10458; Val_tRNA-synt_C; 1.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF47616; GST_C_like; 1.
DR   SUPFAM; SSF46589; tRNA_binding_arm; 1.
DR   SUPFAM; SSF47323; tRNAsyn_1a_bind; 1.
DR   SUPFAM; SSF50677; ValRS_IleRS_edit; 1.
DR   TIGRFAMs; TIGR00422; ValS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1   1217       Valine--tRNA ligase.
FT                                /FTId=PRO_0000106256.
FT   DOMAIN       27    155       GST C-terminal.
FT   MOTIF       293    303       "HIGH" region.
FT   MOTIF       809    813       "KMSKS" region.
FT   BINDING     812    812       ATP (By similarity).
SQ   SEQUENCE   1217 AA;  138218 MW;  5E08AF24B5C8A7A1 CRC64;
     MATLYVSPHL DDFRSLLALV AAEYCGNAKQ QSQVWQWLSF ADNELTPVSC AVVFPLMGMT
     GLDKKIQQNS RVELMRVLKV LDQALEPRTF LVGESITLAD MAVAMAVLLP FKYVLEPSDR
     NVLMNVTRWF TTCINQPEFL KVLGKISLCE KMVPVTAKTS TEEAAAVHPD AAALNGPPKT
     EAQLKKEAKK REKLEKFQQK KEMEAKKKMQ PVAEKKAKPE KRELGVITYD IPTPSGEKKD
     VVSPLPDSYS PQYVEAAWYP WWEKQGFFKP EFGRKSIGEQ NPRGIFMMCI PPPNVTGSLH
     LGHALTNAIQ DTLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLMREKG TSRHDLGREK
     FIEEVWKWKN EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SYAVQEAFIR MHDEGVIYRS
     KRLVNWSCSL NSAISDIEVD KNELSGRTLL PVPGYKEKVE FGVLVSFAYK VDGSDEEVVV
     ATTRIETMLG DTAVAVHPSD SRYQHLKGKT VLHPFCDRKI PVVFDDFVDM SFGTGAVKIT
     PAHDHNDYEV GVRHNLAFIN ILDENGFVIN VPPPFLGMKR FDARKAVLQA LKDRDQFKEI
     KDNPMVVPVC SRSKDIVEPL MKPQWYVSCS DMGKQAADAV REGRLKIIPD HHSQTWFNWM
     DNIRDWCISR QLWWGHRIPA YFITVSDPSV KPGEDMDGHY RVSGRTPEEA REKAAKRFNV
     SPDKIALRQD EDVLDTWFSS GINPFSILGW PNETEDLNVF YPGTLLETGH DILFFWVARM
     VMMGLKLTGK LPFKEVYHCA VVRDAHGRKM SKSLGNVIDP LDDHIGIALE GLHAQLMDTN
     LDPLEVEKPK KVQKADYPNC IPECGTDALR FALCAYTSQG RDINLDVNRI LGYRHFCNKL
     WNAVKFAMRT LGDQFVPADT SPAEREESVS DRWILSRLST AVAQCDAAFR TYDFPAITTA
     IYNFWLYELC DVYLESVKPV FIKAKEDGSC ERPAAVCRQT LYTCLEVGLR LLAPLMPFVT
     EELYQRLPRR RPQSDPPSIC VTPYPDAAEF CWQCEDVDRD IDFIMGVVRT IRSLRSDYKL
     TKTAADCYLQ CTDAATVSLV QKYSLQIQTL SYSQAIVPLM APQPAPEGCA VAIASDRCTV
     NMMLKGLIDV EKEVPKLMGK KTDLEKQIEK LSEKISKGDY KEKVPVKVQE QDTEKLRQSQ
     TELEKVKEAM DNFQKMM
//
ID   TCPD_TAKRU              Reviewed;         536 AA.
AC   P53451;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2012, entry version 76.
DE   RecName: Full=T-complex protein 1 subunit delta;
DE            Short=TCP-1-delta;
DE   AltName: Full=CCT-delta;
GN   Name=cct4; Synonyms=cctd;
OS   Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes;
OC   Tetradontoidea; Tetraodontidae; Takifugu.
OX   NCBI_TaxID=31033;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=96125198; PubMed=8543170; DOI=10.1016/0378-1119(95)00604-4;
RA   Yoda T., Morita T., Kawatsu K., Sueki K., Shibata T., Hamano Y.;
RT   "Cloning and sequencing of the chaperonin-encoding Cctd gene from Fugu
RT   rubripes rubripes.";
RL   Gene 166:249-253(1995).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC       upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC       role in the assembly of BBSome, a complex involved in ciliogenesis
CC       regulating transports vesicles to the cilia. Known to play a role,
CC       in vitro, in the folding of actin and tubulin (By similarity).
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC       forms two stacked rings, 12 to 16 nm in diameter. Component of the
CC       BBS/CCT complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
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DR   EMBL; D49483; BAA08447.1; -; mRNA.
DR   EMBL; D49484; BAA18913.1; -; Genomic_DNA.
DR   PIR; JC4521; JC4521.
DR   RefSeq; NP_001027851.1; NM_001032679.1.
DR   UniGene; Tru.1843; -.
DR   ProteinModelPortal; P53451; -.
DR   STRING; P53451; -.
DR   Ensembl; ENSTRUT00000004220; ENSTRUP00000004197; ENSTRUG00000001819.
DR   GeneID; 446052; -.
DR   CTD; 10575; -.
DR   eggNOG; COG0459; -.
DR   GeneTree; ENSGT00550000074956; -.
DR   InParanoid; P53451; -.
DR   OMA; CNVLLVQ; -.
DR   OrthoDB; EOG4RJG1B; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR012717; Chap_CCT_delta.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   PANTHER; PTHR11353:SF26; Chap_CCT_delta; 1.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; GroEL-ATPase; 1.
DR   TIGRFAMs; TIGR02342; Chap_CCT_delta; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN         1    536       T-complex protein 1 subunit delta.
FT                                /FTId=PRO_0000128336.
SQ   SEQUENCE   536 AA;  57716 MW;  B3ED3285FAC18D07 CRC64;
     MPEGKATSSA SNTGKNKGGA YQDRDKPAQI RYSNISAAKA VADAVRTSLG PKGMDKMIQD
     EKGDVTITND GATILKQMQV LHPSAKMLVE LSKAQDIEAG DGTTSVVVIA GALLDSCNRL
     LQRGIHPTII SESFQKAVDK GVEVLTAMSQ PVQLGDRETL LNSATTSLCS KVVSQYSSLL
     APMSVDAVMR VIDPATATSV DLHDIKIIKK LGGTIDDCEL VEGLVLTQRV ANSSVSRVEK
     AKIGLIQFCL SPPKTDMDNQ IVVSDYTQMD RVLREERAYI LNMVKQIKKA GCNVLFIQKS
     ILRDALSDLA LHFLNKMKIM VVKDIEREDI EFICKTIGTK PIAHIDHFTP EMLGTAELAE
     EVSLDGSGKL VKITGCASPG KTVSIVVRGS NKLVIEEAER SIHDALCVIR CLVKKRALIA
     GGGAPEIELA VRLAEYSRTL GGMEAYCVRA YSDALEVIPS TLAENAGLNP ISTVTELRNR
     HAQGDKMAGI NVRKGGISNI MEELVVQPLL VSISALTLAT ETVRSILKID DVVNAR
//
ID   THGA_ECOLI              Reviewed;         203 AA.
AC   P07464; P77862; Q2MC82;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   16-MAY-2012, entry version 112.
DE   RecName: Full=Galactoside O-acetyltransferase;
DE            Short=GAT;
DE            EC=2.3.1.18;
DE   AltName: Full=Thiogalactoside acetyltransferase;
GN   Name=lacA; OrderedLocusNames=b0342, JW0333;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=85200082; PubMed=3922433; DOI=10.1016/S0300-9084(85)80235-2;
RA   Fowler A.V., Hediger M.A., Musso R.E., Zabin I.;
RT   "The amino acid sequence of thiogalactoside transacetylase of
RT   Escherichia coli.";
RL   Biochimie 67:101-108(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86016712; PubMed=3901000; DOI=10.1073/pnas.82.19.6414;
RA   Hediger M.A., Johnson D.F., Nierlich D.P., Zabin I.;
RT   "DNA sequence of the lactose operon: the lacA gene and the
RT   transcriptional termination region.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:6414-6418(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX   MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0;
RA   Buechel D.E., Gronenborn B., Mueller-Hill B.;
RT   "Sequence of the lactose permease gene.";
RL   Nature 283:541-545(1980).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX   MEDLINE=21936195; PubMed=11937062; DOI=10.1016/S0969-2126(02)00741-4;
RA   Wang X.G., Olsen L.R., Roderick S.L.;
RT   "Structure of the lac operon galactoside acetyltransferase.";
RL   Structure 10:581-588(2002).
CC   -!- FUNCTION: May assist cellular detoxification by acetylating non-
CC       metabolizable pyranosides, thereby preventing their reentry into
CC       the cell.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + a beta-D-galactoside = CoA + a 6-
CC       acetyl-beta-D-galactoside.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: The N-terminus of this protein is heterogeneous because the
CC       initiator methionine is only partially cleaved.
CC   -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family.
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DR   EMBL; J01636; AAA24055.1; -; Genomic_DNA.
DR   EMBL; X51872; CAA36162.1; -; Genomic_DNA.
DR   EMBL; U73857; AAB18066.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73445.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76124.1; -; Genomic_DNA.
DR   EMBL; V00295; CAA23572.1; -; Genomic_DNA.
DR   PIR; A94061; XXECTG.
DR   RefSeq; NP_414876.1; NC_000913.2.
DR   PDB; 1KQA; X-ray; 3.20 A; A/B/C=1-203.
DR   PDB; 1KRR; X-ray; 2.50 A; A/B/C=1-203.
DR   PDB; 1KRU; X-ray; 2.80 A; A/B/C=1-203.
DR   PDB; 1KRV; X-ray; 2.80 A; A/B/C=1-203.
DR   PDBsum; 1KQA; -.
DR   PDBsum; 1KRR; -.
DR   PDBsum; 1KRU; -.
DR   PDBsum; 1KRV; -.
DR   ProteinModelPortal; P07464; -.
DR   SMR; P07464; 2-202.
DR   DIP; DIP-10078N; -.
DR   IntAct; P07464; 4.
DR   EnsemblBacteria; EBESCT00000004023; EBESCP00000004023; EBESCG00000003288.
DR   EnsemblBacteria; EBESCT00000004024; EBESCP00000004024; EBESCG00000003288.
DR   EnsemblBacteria; EBESCT00000004025; EBESCP00000004025; EBESCG00000003288.
DR   EnsemblBacteria; EBESCT00000004026; EBESCP00000004026; EBESCG00000003288.
DR   EnsemblBacteria; EBESCT00000017191; EBESCP00000016482; EBESCG00000016250.
DR   GeneID; 945674; -.
DR   GenomeReviews; AP009048_GR; JW0333.
DR   GenomeReviews; U00096_GR; b0342.
DR   KEGG; eco:b0342; -.
DR   PATRIC; 32115817; VBIEscCol129921_0350.
DR   EchoBASE; EB0519; -.
DR   EcoGene; EG10524; lacA.
DR   eggNOG; COG0110; -.
DR   HOGENOM; HOG000049435; -.
DR   KO; K00633; -.
DR   OMA; PMTERIK; -.
DR   ProtClustDB; PRK09527; -.
DR   BioCyc; EcoCyc:GALACTOACETYLTRAN-MONOMER; -.
DR   BioCyc; MetaCyc:GALACTOACETYLTRAN-MONOMER; -.
DR   EvolutionaryTrace; P07464; -.
DR   Genevestigator; P07464; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008870; F:galactoside O-acetyltransferase activity; IEA:EC.
DR   GO; GO:0005989; P:lactose biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001451; Hexapep_transf.
DR   InterPro; IPR018357; Hexapep_transf_CS.
DR   InterPro; IPR024688; Maltose/galactoside_AcTrfase.
DR   InterPro; IPR011004; Trimer_LpxA-like.
DR   Pfam; PF00132; Hexapep; 1.
DR   Pfam; PF12464; Mac; 1.
DR   SUPFAM; SSF51161; Trimer_LpxA_like; 1.
DR   PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Lactose biosynthesis; Reference proteome;
KW   Repeat; Transferase.
FT   CHAIN         1    203       Galactoside O-acetyltransferase.
FT                                /FTId=PRO_0000068696.
FT   HELIX         5     11
FT   HELIX        22     37
FT   HELIX        44     54
FT   STRAND       55     57
FT   STRAND       68     71
FT   STRAND       76     78
FT   STRAND       88     91
FT   STRAND       96     98
FT   STRAND      109    114
FT   TURN        119    121
FT   STRAND      127    129
FT   STRAND      132    134
FT   STRAND      172    175
FT   TURN        176    179
FT   STRAND      180    184
FT   HELIX       187    189
SQ   SEQUENCE   203 AA;  22799 MW;  31C7FEA0B0150D70 CRC64;
     MNMPMTERIR AGKLFTDMCE GLPEKRLRGK TLMYEFNHSH PSEVEKRESL IKEMFATVGE
     NAWVEPPVYF SYGSNIHIGR NFYANFNLTI VDDYTVTIGD NVLIAPNVTL SVTGHPVHHE
     LRKNGEMYSF PITIGNNVWI GSHVVINPGV TIGDNSVIGA GSIVTKDIPP NVVAAGVPCR
     VIREINDRDK HYYFKDYKVE SSV
//
ID   UBR5_RAT                Reviewed;        2788 AA.
AC   Q62671; F1LRS0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 3.
DT   16-MAY-2012, entry version 90.
DE   RecName: Full=E3 ubiquitin-protein ligase UBR5;
DE            EC=6.3.2.-;
DE   AltName: Full=100 kDa protein;
DE   AltName: Full=E3 ubiquitin-protein ligase, HECT domain-containing 1;
DE   AltName: Full=Hyperplastic discs protein homolog;
GN   Name=Ubr5; Synonyms=Dd5, Edd, Edd1, Hyd;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1868-2788.
RC   STRAIN=Wistar; TISSUE=Testis;
RX   MEDLINE=92253337; PubMed=1533713; DOI=10.1093/nar/20.7.1471;
RA   Mueller D., Rehbein M., Baumeister H., Richter D.;
RT   "Molecular characterization of a novel rat protein structurally
RT   related to poly(A) binding proteins and the 70K protein of the U1
RT   small nuclear ribonucleoprotein particle (snRNP).";
RL   Nucleic Acids Res. 20:1471-1475(1992).
RN   [3]
RP   ERRATUM.
RA   Mueller D., Rehbein M., Baumeister H., Richter D.;
RL   Nucleic Acids Res. 20:2624-2624(1992).
RN   [4]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFT.
RX   MEDLINE=99153743; PubMed=10030672; DOI=10.1038/sj.onc.1202249;
RA   Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R.,
RA   Sutherland R.L., Watts C.K.W.;
RT   "Identification of a human HECT family protein with homology to the
RT   Drosophila tumor suppressor gene hyperplastic discs.";
RL   Oncogene 17:3479-3491(1998).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12239083; DOI=10.1210/en.2002-220262;
RA   Oughtred R., Bedard N., Adegoke O.A.J., Morales C.R., Trasler J.,
RA   Rajapurohitam V., Wing S.S.;
RT   "Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase
RT   induced in germ cells of the rat testis and similar to the Drosophila
RT   hyperplastic discs gene.";
RL   Endocrinology 143:3740-3747(2002).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the
CC       N-end rule pathway. Recognizes and binds to proteins bearing
CC       specific N-terminal residues that are destabilizing according to
CC       the N-end rule, leading to their ubiquitination and subsequent
CC       degradation (By similarity). Involved in maturation and/or
CC       transcriptional regulation of mRNA by activating CDK9 by
CC       polyubiquitination. May play a role in control of cell cycle
CC       progression. May have tumor suppressor function. Regulates DNA
CC       topoisomerase II binding protein (TopBP1) for the DNA damage
CC       response. Plays an essential role in extraembryonic development
CC       (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Binds TOPBP1. Associates with CDK9 and TFIIS/TCEA1 and
CC       forms a transcription regulatory complex made of CDK9, RNAP II,
CC       UBR5 and TFIIS/TCEA1 that can stimulates target gene transcription
CC       by recruiting their promoters (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Highest levels found in testis. Also present
CC       in liver, kidney, lung and brain.
CC   -!- DEVELOPMENTAL STAGE: In early postnatal life, expression in the
CC       testis increases to reach a maximum around day 28.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
CC       thioester formation.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 1 PABC domain.
CC   -!- SIMILARITY: Contains 1 UBR-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA45756.1; Type=Frameshift; Positions=30;
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DR   EMBL; X64411; CAA45756.1; ALT_FRAME; mRNA.
DR   IPI; IPI00768617; -.
DR   PIR; S22659; S22659.
DR   UniGene; Rn.54812; -.
DR   PDB; 3NTW; X-ray; 2.60 A; A/C=2383-2442.
DR   PDBsum; 3NTW; -.
DR   STRING; Q62671; -.
DR   PhosphoSite; Q62671; -.
DR   PRIDE; Q62671; -.
DR   UCSC; X64411; rat.
DR   RGD; 621236; Ubr5.
DR   eggNOG; COG5021; -.
DR   HOGENOM; HOG000046848; -.
DR   InParanoid; Q62671; -.
DR   OrthoDB; EOG4QVCB2; -.
DR   ArrayExpress; Q62671; -.
DR   Genevestigator; Q62671; -.
DR   GermOnline; ENSRNOG00000006816; Rattus norvegicus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:RefGenome.
DR   Gene3D; G3DSA:1.10.1900.10; PABP_HYD; 1.
DR   Gene3D; G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 3.
DR   InterPro; IPR024725; E3_UbLigase_EDD_UBA.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR002004; PABP_HYD.
DR   InterPro; IPR009091; Reg_csome_cond/b-lactamase_inh.
DR   InterPro; IPR003126; Znf_N-recognin.
DR   InterPro; IPR013993; Znf_N-recognin_met.
DR   Pfam; PF11547; E3_UbLigase_EDD; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00658; PABP; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF63570; PABP_HYD; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS51309; PABC; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Ligase; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   2788       E3 ubiquitin-protein ligase UBR5.
FT                                /FTId=PRO_0000086933.
FT   DOMAIN     2367   2444       PABC.
FT   DOMAIN     2451   2788       HECT.
FT   ZN_FING    1166   1234       UBR-type.
FT   COMPBIAS   1613   1670       Ser-rich.
FT   COMPBIAS   2319   2366       Arg-rich.
FT   ACT_SITE   2757   2757       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     100    100       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphoserine (By similarity).
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   MOD_RES     626    626       Phosphothreonine (By similarity).
FT   MOD_RES     797    797       Phosphoserine (By similarity).
FT   MOD_RES     917    917       Phosphoserine (By similarity).
FT   MOD_RES    1007   1007       Phosphoserine (By similarity).
FT   MOD_RES    1104   1104       Phosphothreonine (By similarity).
FT   MOD_RES    1124   1124       Phosphothreonine (By similarity).
FT   MOD_RES    1216   1216       Phosphoserine (By similarity).
FT   MOD_RES    1344   1344       Phosphoserine (By similarity).
FT   MOD_RES    1364   1364       Phosphoserine (By similarity).
FT   MOD_RES    1470   1470       Phosphoserine (By similarity).
FT   MOD_RES    1725   1725       Phosphothreonine (By similarity).
FT   MOD_RES    1730   1730       Phosphoserine (By similarity).
FT   MOD_RES    1769   1769       Phosphoserine (By similarity).
FT   MOD_RES    1959   1959       Phosphothreonine (By similarity).
FT   MOD_RES    2016   2016       Phosphoserine (By similarity).
FT   MOD_RES    2018   2018       Phosphoserine (By similarity).
FT   MOD_RES    2020   2020       Phosphothreonine (By similarity).
FT   MOD_RES    2061   2061       Phosphoserine (By similarity).
FT   MOD_RES    2066   2066       Phosphoserine (By similarity).
FT   MOD_RES    2203   2203       Phosphothreonine (By similarity).
FT   MOD_RES    2279   2279       Phosphoserine (By similarity).
FT   MOD_RES    2473   2473       Phosphoserine (By similarity).
FT   MOD_RES    2475   2475       Phosphoserine (By similarity).
FT   CONFLICT   1890   1890       Missing (in Ref. 2; CAA45756).
FT   HELIX      2383   2386
FT   HELIX      2392   2396
FT   HELIX      2400   2402
FT   HELIX      2403   2406
FT   HELIX      2410   2412
FT   HELIX      2415   2423
FT   HELIX      2425   2439
SQ   SEQUENCE   2788 AA;  308027 MW;  C2EA68B962627231 CRC64;
     MNKQAVKRLH MLREVSEKLN KYNLNSHPPL NVLEQATIKQ CVVGPNHAAF LLEDGRICRI
     GFSVQPDRLE LGKPDNNDGS KLNSSSGTGR TSRPGRTSDS PWFLSGSETL GRLAGNTLGS
     RWSSGVGGSG GGSSGRSSAG ARDSRRQTRV IRTGRDRGSG LLGSQPQPVI PASVIPEELI
     SQAQVVLQGK SRSVIIRELQ RTNLDVNLAV NNLLSRDDED GDDGDDTASE SYLPGEDLMS
     LLDADIHSAH PSVIIDADAM FSEDISYFGY PSFRRSSLSR LGSSRVLLLP LERDSELLRE
     RESVLRLRER RWLDGASFDN ERGSTSKEGE PNPDKKNTPV QSPVSLGEDL QWWPDKDGTK
     FTCIGALYSE LVAVSSKGEL YQWKWTESEP YRNAQNPSLH HPRATFLGLT NEKIVLLSAN
     SIRATVATEN NKVATWVDET LSSVASKLEH TAQTYSELQG ERIVSLHCCA LYTCAQLENN
     LYWWGVVPFS QRKKMLEKAR AKNKKPKSSA GVQSLNVRGG RQVCLRNNPL YHAGAVAFSI
     SAGIPKVGVL MESVWNMNDS CRFQLRSPES LKSMEKASKT IETKPESKQE PVKTEMGPPP
     SPASTCSDAS SIASSASMPY KRRRSTPAPK EEEKVNEEQW SLREVVFVED VKNVPVGKVL
     KVDGAYVAVK FPGTSSNTNC QNSSGPDADP SSLLQDCRLL RIDELQVVKT GGTPKVPDCF
     QRTPKKLCIP EKTEILAVNV DSKGVHAVLK TGNWVRYCIF DLATGKAEQE NNFPTSSVAF
     LGQNERSVAI FTAGQESPII LRDGNGTIYP MAKDCMGGIR DPDWLDLPPI SSLGMGVHSL
     INLPANSTIK KKAAIIIMAV EKQTLMQHIL RCDYEACRQY LVNLEQAVVL EQNLQMLQTF
     ISHRCDGNRN ILHACVSVCF PTSNKETKEE EEAERSERNT FAERLSAVEA IANAISVVSS
     NGPGNRAGSS SSRSLRLREM MRRSLRAAGL GRHEAGASSS DHQDPVSPPI APPSWVPDPP
     SMDPDGDIDF ILAPAVGSLT TAATGGGQGP STSTIPGPST EPSVVESKDR KANAHFILKL
     LCDSAVLQPY LRELLSAKDA RGMTPFMSAV SGRAYPAAIT ILETAQKIAK AEVSGSEKEE
     DVFMGMVCPS GTNPDDSPLY VLCCNDTCSF TWTGAEHINQ DIFECRTCGL LESLCCCTEC
     ARVCHKGHDC KLKRTSPTAY CDCWEKCKCK TLIAGQKSAR LDLLYRLLTA TNLVTLPNSR
     GEHLLLFLVQ TVARQTVEHC QYRPPRIRED RNRKTASPDD SDMPDHDLEP PRFAQLALER
     VLQDWNALRS MIMFGSQENK DPLSASSRIG HLLPEEQVYL NQQSGTIRLD CFTHCLIVKC
     TADILLLDTL LGTLVKELQN KYTPGRREEA IAVTMRFLRS VARVFVILSV EMASSKKKNN
     FIPQPIGKCK RVFQALLPYA VEELCNVAES LIVPVRMGIA RPTAPFTLAS TSIDAMQGSE
     ELFSVEPLPP RPSSDQSSSS SQSQSSYIIR NPQQRRISQS QPVRGREEEQ DDIVSADVEE
     VEVVEGVAGE EDHHDEQEEH GEENAEAEGH HDEHDEDGSD MELDLLAAAE TESDSESNHS
     NQDNASGRRS VVTAATAGSE AGASSVPAFF SEDDSQSNDS SDSDSSSSQS DDIEQETFML
     DEPLERTTNS SHANGAAQAP RSMQWAVRNT QHQRAASTAP SSTSTPAASS AGLIYIDPSN
     LRRSGTISTS AAAAAAALEA SNASSYLTSA SSLARAYSIV IRQISDLMGL IPKYNHLVYS
     QIPAAVKLTY QDAVNLQNYV EEKLIPTWNW MVSIMDSTEA QLRYGSALAS AGDPGHPNHP
     LHASQNSARR ERMTAREEAS LRTLEGRRRR ATLLSARQGM MSARGDFLNY ALSLMRSHND
     EHSDVLPVLD VCSLKHVAYV FQALIYWIKA MNQQTTLDTP QLERKRTREL LELGIDNEDS
     EHENDDDTSQ SATLNDKDDE SLPAETGQNH PFFRRSDSMT FLGCIPPNPF EVPLAEAIPL
     ADQPHLLQPN ARKEDLFGRP SQGLYSSSAG SGKCLVEVTM DRNCLEVLPT KMSYAANLKN
     VMNMQNRQKK AGEDQSMLAE EADSSKPGPS AHDVAAQLKS SLLAEIGLTE SEGPPLTSFR
     PQCSFMGMVI SHDMLLGRWR LSLELFGRVF MEDVGAEPGS ILTELGGFEV KESKFRREME
     KLRNQQSRDL SLEVDRDRDL LIQQTMRQLN NHFGRRCATT PMAVHRVKVT FKDEPGEGSG
     VARSFYTAIA QAFLSNEKLP NLDCIQNANK GTHTSLMQRL RNRGERDRER EREREMRRSS
     GLRAGSRRDR DRDFRRQLSI DTRPFRPASE GNPSDDPDPL PAHRQALGER LYPRVQAMQP
     AFASKITGML LELSPAQLLL LLASEDSLRA RVEEAMELIV AHGRENGADS ILDLGLLDSS
     EKVQENRKRH GSSRSVVDMD LDDTDDGDDN APLFYQPGKR GFYTPRPGKN TEARLNCFRN
     IGRILGLCLL QNELCPITLN RHVIKVLLGR KVNWHDFAFF DPVMYESLRQ LILASQSSDA
     DAVFSAMDLA FAVDLCKEEG GGQVELIPNG VNIPVTPQNV YEYVRKYAEH RMLVVAEQPL
     HAMRKGLLDV LPKNSLEDLT AEDFRLLVNG CGEVNVQMLI SFTSFNDESG ENAEKLLQFK
     RWFWSIVERM SMTERQDLVY FWTSSPSLPA SEEGFQPMPS ITIRPPDDQH LPTANTCISR
     LYVPLYSSKQ ILKQKLLLAI KTKNFGFV
//
