>P1;CCHU
cytochrome c [validated] - human
C;Species: Homo sapiens (man)
C;Date: 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 31-Dec-2004
C;Accession: A31764; A05676; I55192; A00001
R;Evans, M.J.; Scarpulla, R.C.
Proc. Natl. Acad. Sci. U.S.A. 85, 9625-9629, 1988
A;Title: The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution.
A;Reference number: A31764; MUID:89071748; PMID:2849112
A;Accession: A31764
A;Molecule type: DNA
A;Residues: 1-105 A;Cross-references: UNIPROT:P99999; UNIPARC:UPI000013EAA0; GB:M22877; NID:g181241; PIDN:AAA35732.1; PID:g181242
R;Matsubara, H.; Smith, E.L.
J. Biol. Chem. 238, 2732-2753, 1963
A;Title: Human heart cytochrome c. Chymotryptic peptides, tryptic peptides, and the complete amino acid sequence.
A;Reference number: A05676
A;Accession: A05676
A;Molecule type: protein
A;Residues: 2-28;29-46;47-100;101-105 A;Cross-references: UNIPARC:UPI0000171C77; UNIPARC:UPI0000171C78; UNIPARC:UPI0000171C79; UNIPARC:UPI0000171C7A
R;Matsubara, H.; Smith, E.L.
J. Biol. Chem. 237, 3575-3576, 1962
A;Title: The amino acid sequence of human heart cytochrome c.
A;Reference number: A00001
A;Contents: annotation
A;Note: 66-Leu is found in 10% of the molecules in pooled protein
R;Tanaka, Y.; Ashikari, T.; Shibano, Y.; Amachi, T.; Yoshizumi, H.; Matsubara, H.
J. Biochem. 103, 954-961, 1988
A;Title: Construction of a human cytochrome c gene and its functional expression in Saccharomyces cerevisiae.
A;Reference number: I55192; MUID:89008207; PMID:2844747
A;Accession: I55192
A;Status: translated from GB/EMBL/DDBJ
A;Molecule type: mRNA
A;Residues: 78-105 A;Cross-references: UNIPARC:UPI0000000359; GB:D00265; NID:g2897691; PIDN:BAA00187.1; PID:g219557
C;Genetics:
A;Introns: 57/1
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; polymorphism; respiratory chain
F;2-105/Product: cytochrome c #status experimental F;5-99/Domain: cytochrome c homology F;2/Modified site: acetylated amino end (Gly) (in mature form) #status experimental
F;15,18/Binding site: heme (Cys) (covalent) #status experimental
F;19,81/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCCZ
cytochrome c - chimpanzee (tentative sequence)
C;Species: Pan troglodytes (chimpanzee)
C;Date: 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 31-Dec-2004
C;Accession: A00002
R;Needleman, S.B.
submitted to the Atlas, October 1968
A;Reference number: A94601
A;Accession: A00002
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P99998; UNIPARC:UPI0000128BBF
R;Needleman, S.B.; Margoliash, E.
unpublished results, 1966, cited by Margoliash, E., and Fitch, W.M., Ann. N.Y. Acad. Sci. 151, 359-381, 1968
A;Reference number: A94455
A;Contents: annotation; compositions of chymotryptic peptides
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCMQR
cytochrome c - rhesus macaque (tentative sequence)
C;Species: Macaca mulatta (rhesus macaque)
C;Date: 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 31-Dec-2004
C;Accession: A00003
R;Rothfus, J.A.; Smith, E.L.
J. Biol. Chem. 240, 4277-4283, 1965
A;Title: Amino acid sequence of rhesus monkey heart cytochrome c.
A;Reference number: A00003; MUID:66045191; PMID:4954366
A;Contents: compositions of chymotryptic peptides; sequences of residues 55-61 and 68-70
A;Accession: A00003
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00002; UNIPARC:UPI0000128BC7
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCMKP
cytochrome c - spider monkey
C;Species: Ateles sp. (spider monkey)
C;Date: 17-Dec-1982 #sequence_revision 17-Dec-1982 #text_change 31-Dec-2004
C;Accession: A00004
R;Margoliash, E.
unpublished results, cited by Shelnutt, J.A., Rousseau, D.L., Dethmers, J.K., and Margoliash, E., Biochemistry 20, 6485-6497, 1981
A;Reference number: A00004
A;Accession: A00004
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00003; UNIPARC:UPI0000128B99
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCMS
cytochrome c [validated] - mouse
C;Species: Mus musculus (house mouse)
C;Date: 31-Dec-1990 #sequence_revision 30-Sep-1991 #text_change 31-Dec-2004
C;Accession: A23057; A04604; A00009
R;Limbach, K.J.; Wu, R.
Nucleic Acids Res. 13, 617-630, 1985
A;Title: Characterization of a mouse somatic cytochrome c gene and three cytochrome c pseudogenes.
A;Reference number: A23057; MUID:85215501; PMID:2987801
A;Accession: A23057
A;Molecule type: DNA
A;Residues: 1-105 A;Cross-references: UNIPROT:P00009; UNIPARC:UPI0000003E57; EMBL:X01756; NID:g50618; PIDN:CAA25899.1; PID:g50619
A;Experimental source: strain BALB/c
R;Carlson, S.S.; Mross, G.A.; Wilson, A.C.; Mead, R.T.; Wolin, L.D.; Bowers, S.F.; Foley, N.T.; Muijsers, A.O.; Margoliash, E.
Biochemistry 16, 1437-1442, 1977
A;Title: Primary structure of mouse, rat, and guinea pig cytochrome c.
A;Reference number: A04604; MUID:77134768; PMID:191069
A;Accession: A04604
A;Molecule type: protein
A;Residues: 2-105 A;Cross-references: UNIPARC:UPI00000291A5
A;Experimental source: strain BALB/c
C;Genetics:
A;Introns: 57/1
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;2-105/Product: cytochrome c #status experimental F;5-99/Domain: cytochrome c homology F;2/Modified site: acetylated amino end (Gly) (in mature form) #status experimental
F;15,18/Binding site: heme (Cys) (covalent) #status experimental
F;19,81/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCRT
cytochrome c [validated] - rat
C;Species: Rattus norvegicus (Norway rat)
C;Date: 31-Dec-1990 #sequence_revision 30-Sep-1991 #text_change 31-Dec-2004
C;Accession: A04605; C28160; A00009
R;Scarpulla, R.C.; Agne, K.M.; Wu, R.
J. Biol. Chem. 256, 6480-6486, 1981
A;Title: Isolation and structure of a rat cytochrome c gene.
A;Reference number: A04605; MUID:81215609; PMID:6263917
A;Accession: A04605
A;Molecule type: DNA
A;Residues: 1-105 A;Cross-references: UNIPROT:P00009; UNIPARC:UPI0000003E57; GB:K00750; GB:M28216; NID:g550511; PIDN:AAA21711.1; PID:g203699
R;Virbasius, J.V.; Scarpulla, R.C.
J. Biol. Chem. 263, 6791-6796, 1988
A;Title: Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants.
A;Reference number: A28160; MUID:88198250; PMID:2834389
A;Accession: C28160
A;Molecule type: mRNA
A;Residues: 1-105 A;Cross-references: UNIPARC:UPI0000003E57; GB:M20622; NID:g203722; PIDN:AAA41014.1; PID:g203723
R;Carlson, S.S.; Mross, G.A.; Wilson, A.C.; Mead, R.T.; Wolin, L.D.; Bowers, S.F.; Foley, N.T.; Muijsers, A.O.; Margoliash, E.
Biochemistry 16, 1437-1442, 1977
A;Title: Primary structure of mouse, rat, and guinea pig cytochrome c.
A;Reference number: A04604; MUID:77134768; PMID:191069
A;Contents: annotation
A;Note: peptide mapping, compositional analysis, and partial sequencing indicate that rat cytochrome c is identical with that of mouse
C;Genetics:
A;Introns: 57/1
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: blocked amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;2-105/Product: cytochrome c #status experimental F;5-99/Domain: cytochrome c homology F;2/Modified site: blocked amino end (Gly) (in mature form) (probably acetylated) #status experimental
F;15,18/Binding site: heme (Cys) (covalent) #status experimental
F;19,81/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCRB
cytochrome c [validated] - rabbit
C;Species: Oryctolagus cuniculus (domestic rabbit)
C;Date: 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 31-Dec-2004
C;Accession: A00009
R;Needleman, S.B.; Margoliash, E.
J. Biol. Chem. 241, 853-863, 1966
A;Title: Rabbit heart cytochrome c.
A;Reference number: A00009; MUID:66093127; PMID:5905125
A;Accession: A00009
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00008; UNIPARC:UPI0000128BD2
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCGW
cytochrome c [validated] - guanaco
C;Species: Lama guanicoe (guanaco)
C;Date: 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Dec-2004
C;Accession: A04608; A00009
R;Niece, R.L.; Margoliash, E.; Fitch, W.M.
Biochemistry 16, 68-72, 1977
A;Title: Complete amino acid sequence of guanaco (Lama guanicoe) cytochrome c.
A;Reference number: A04608; MUID:77087753; PMID:188448
A;Accession: A04608
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00010; UNIPARC:UPI0000128BB2
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCCM
cytochrome c - Arabian camel
C;Species: Camelus dromedarius (Arabian camel)
C;Date: 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Dec-2004
C;Accession: A04607; A00009
R;Sokolovsky, M.; Moldovan, M.
Biochemistry 11, 145-149, 1972
A;Title: Primary structure of cytochrome c from the camel, Camelus dromedarius.
A;Reference number: A04607; MUID:72096652; PMID:5061872
A;Accession: A04607
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00010; UNIPARC:UPI0000128BB2
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCWHC
cytochrome c - California gray whale
C;Species: Eschrichtius robustus, Eschrichtius gibbosus (California gray whale)
C;Date: 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Dec-2004
C;Accession: A04606; A00009
R;Goldstone, A.; Smith, E.L.
J. Biol. Chem. 241, 4480-4486, 1966
A;Title: Amino acid sequence of whale heart cytochrome c.
A;Reference number: A04606; MUID:67041932; PMID:5922971
A;Accession: A04606
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00010; UNIPARC:UPI0000128BB2
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: blocked amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: blocked amino end (Gly) (probably acetylated) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCPG
cytochrome c [validated] - pig
C;Species: Sus scrofa domestica (domestic pig)
C;Date: 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 31-Dec-2004
C;Accession: A00007
R;Stewart, J.W.; Margoliash, E.
Can. J. Biochem. 43, 1187-1206, 1965
A;Title: The primary structure of the cytochrome c from various organs of the hog.
A;Reference number: A90743; MUID:66072936; PMID:5855656
A;Accession: A00007
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00006; UNIPARC:UPI0000128B9A
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCBO
cytochrome c - bovine
C;Species: Bos primigenius taurus (cattle)
C;Date: 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Dec-2004
C;Accession: A92022; A00007
R;Nakashima, T.; Higa, H.; Matsubara, H.; Benson, A.; Yasunobu, K.T.
J. Biol. Chem. 241, 1166-1177, 1966
A;Title: The amino acid sequence of bovine heart cytochrome c.
A;Reference number: A92022; MUID:66132521; PMID:5933874
A;Accession: A92022
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00006; UNIPARC:UPI0000128B9A
R;Tsunasawa, S.; Narita, K.
J. Biochem. 92, 607-613, 1982
A;Title: Micro-identification of amino-terminal acetylamino acids in proteins.
A;Reference number: A61297; MUID:83056735; PMID:6754709
A;Contents: annotation; acetylation
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCSH
cytochrome c - sheep (tentative sequence)
C;Species: Ovis orientalis aries, Ovis ammon aries (domestic sheep)
C;Date: 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Dec-2004
C;Accession: A91454; A00007
R;Smith, E.L.; Margoliash, E.
Fed. Proc. 23, 1243-1247, 1964
A;Title: Evolution of cytochrome c.
A;Reference number: A91454
A;Accession: A91454
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00006; UNIPARC:UPI0000128B9A
A;Note: amino acid compositions and mobilities of tryptic and chymotryptic peptides were determined
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCHOD
cytochrome c - donkey (tentative sequence)
C;Species: Equus asinus (donkey)
C;Date: 17-Mar-1987 #sequence_revision 17-Mar-1987 #text_change 31-Dec-2004
C;Accession: A00006
R;Walasek, O.F.; Margoliash, E.
J. Biol. Chem. 252, 830-834, 1977
A;Title: Transmission of the cytochrome c structural gene in horse-donkey crosses.
A;Reference number: A92217; MUID:77118552; PMID:190219
A;Accession: A00006
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00005; UNIPARC:UPI0000128BB1
A;Note: compositions of chymotryptic peptides and the sequence of residues 47-48 were determined
A;Note: mules and hinnies are heterozygous, having equal amounts of horse and donkey cytochromes c
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCHOZ
cytochrome c - common zebra (tentative sequence)
C;Species: Equus burchelli, Equus quagga (common zebra, plains zebra)
C;Date: 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Dec-2004
C;Accession: A91330; A00006
R;Guertler, L.; Horstmann, H.J.
FEBS Lett. 18, 106-108, 1971
A;Title: Zur Primaerstruktur des Cytochromes c des Steppenzebras (Equus quagga boehmi).
A;Reference number: A91330
A;Accession: A91330
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00005; UNIPARC:UPI0000128BB1
A;Note: the amino acid composition and the sequence of residues 40-48 were determined
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCHO
cytochrome c [validated] - horse
C;Species: Equus caballus (domestic horse)
C;Date: 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 31-Dec-2004
C;Accession: A00005; S59487
R;Margoliash, E.; Smith, E.L.; Kreil, G.; Tuppy, H.
Nature 192, 1125-1127, 1961
A;Title: The complete amino-acid sequence.
A;Reference number: A93145
A;Accession: A00005
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00004; UNIPARC:UPI000011054E
R;Theodorakis, J.L.; Armes, L.G.; Margoliash, E.
Biochim. Biophys. Acta 1252, 114-125, 1995
A;Title: beta-Thiopropionyl cytochromes c modified at lysyl residues: preparation and characterization of the monosubstituted horse cytochromes c.
A;Reference number: S59487; MUID:96001358; PMID:7548153
A;Accession: S59487
A;Status: preliminary
A;Molecule type: protein
A;Residues: 1-10;11-18;19-26;27-34;38-47;50-54;55-58;60-67;68-74;75-82;83-97;98-104 A;Cross-references: UNIPARC:UPI0000171C7B; UNIPARC:UPI0000171C7C; UNIPARC:UPI0000171C7D; UNIPARC:UPI0000171C7E; UNIPARC:UPI0000171C7F; UNIPARC:UPI0000171C80; UNIPARC:UPI0000171C81; UNIPARC:UPI0000171C82; UNIPARC:UPI0000171C83; UNIPARC:UPI0000171C84; UNIPARC:UPI0000171C85; UNIPARC:UPI0000171C86
R;Luo, Y.; Brayer, G.D.
submitted to the Brookhaven Protein Data Bank, August 1994
A;Reference number: A52805; PDB:1HRC
A;Contents: annotation; X-ray crystallography, 1.9 angstroms, residues 1-104
R;Dickerson, R.E.; Takano, T.; Eisenberg, D.; Kallai, O.B.; Samson, L.; Cooper, A.; Margoliash, E.
J. Biol. Chem. 246, 1511-1533, 1971
A;Title: Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution.
A;Reference number: A92076; MUID:71116428; PMID:5545094
A;Contents: annotation; X-ray crystallography, 2.8 angstroms
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status experimental
>P1;CCHP
cytochrome c - hippopotamus
C;Species: Hippopotamus amphibius (hippopotamus)
C;Date: 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 31-Dec-2004
C;Accession: A00008
R;Thompson, R.B.; Borden, D.; Tarr, G.E.; Margoliash, E.
J. Biol. Chem. 253, 8957-8961, 1978
A;Title: Heterogeneity of amino acid sequence in hippopotamus cytochrome c.
A;Reference number: A00008; MUID:79067782; PMID:214435
A;Accession: A00008
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00007; UNIPARC:UPI0000128BBE
A;Note: 3-Ile was also found
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCDG
cytochrome c - dog (tentative sequence)
C;Species: Canis lupus familiaris (dog)
C;Date: 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 31-Dec-2004
C;Accession: A00010
R;McDowall, M.A.; Smith, E.L.
J. Biol. Chem. 240, 4635-4647, 1965
A;Title: Amino acid sequence of dog heart cytochrome c.
A;Reference number: A00010; MUID:66047448; PMID:5846985
A;Accession: A00010
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00011; UNIPARC:UPI0000128B9E
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: blocked amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: blocked amino end (Gly) (probably acetylated) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCSLE
cytochrome c - southern elephant seal (tentative sequence)
C;Species: Mirounga leonina (southern elephant seal)
C;Date: 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Dec-2004
C;Accession: A04615; A00010
R;Augusteyn, R.C.; McDowall, M.A.; Webb, E.C.; Zerner, B.
Biochim. Biophys. Acta 257, 264-272, 1972
A;Title: Primary structure of cytochrome c from the elephant seal, Mirounga leonina.
A;Reference number: A04615; MUID:72170090; PMID:4553890
A;Accession: A04615
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00012; UNIPARC:UPI0000128BCB
A;Note: peptides were positioned by homology
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCBTS
cytochrome c - Schreibers's long-fingered bat (tentative sequence)
C;Species: Miniopterus schreibersi (Schreibers's long-fingered bat)
C;Date: 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Dec-2004
C;Accession: A04614; A00010
R;Strydom, D.J.; van der Walt, S.J.; Botes, D.P.
Comp. Biochem. Physiol. B 43, 21-24, 1972
A;Title: The amino acid sequence of bat (Miniopteris schreibersi) cytochrome c.
A;Reference number: A04614; MUID:73123526; PMID:4347193
A;Accession: A04614
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00013; UNIPARC:UPI0000128BCA
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCKGG
cytochrome c [validated] - eastern gray kangaroo
C;Species: Macropus giganteus (eastern gray kangaroo)
C;Date: 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Dec-2004
C;Accession: A00011
R;Nolan, C.; Margoliash, E.
J. Biol. Chem. 241, 1049-1059, 1966
A;Title: Primary structure of the cytochrome c from the great grey kangaroo, Macropus canguru.
A;Reference number: A00011; MUID:66132505; PMID:5933863
A;Accession: A00011
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00014; UNIPARC:UPI0000128BC5
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCMST
cytochrome c, testis-specific [validated] - mouse
N;Alternate names: cytochrome c T
C;Species: Mus musculus (house mouse)
C;Date: 24-Apr-1984 #sequence_revision 30-Sep-1991 #text_change 31-Dec-2004
C;Accession: B28160; A00012; I48313
R;Virbasius, J.V.; Scarpulla, R.C.
J. Biol. Chem. 263, 6791-6796, 1988
A;Title: Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants.
A;Reference number: A28160; MUID:88198250; PMID:2834389
A;Accession: B28160
A;Molecule type: mRNA
A;Residues: 1-105 A;Cross-references: UNIPROT:P00015; UNIPARC:UPI0000022AAF; GB:M20625; NID:g192875; PIDN:AAA37501.1; PID:g309203
R;Hennig, B.
Eur. J. Biochem. 55, 167-183, 1975
A;Title: Change of cytochrome c structure during development of the mouse.
A;Reference number: A00012; MUID:76022386; PMID:240690
A;Accession: A00012
A;Molecule type: protein
A;Residues: 2-57,'IV',60-61,'ZZ',64-66,'Z',68-69,'ZB',72-105 A;Cross-references: UNIPARC:UPI0000171C87
A;Experimental source: strain BALB/c
R;Hake, L.E.; Alcivar, A.A.; Hecht, N.B.
Development 110, 249-257, 1990
A;Title: Changes in mRNA length accompany translational regulation of the somatic and testis-specific cytochrome c genes during spermatogenesis in the mouse.
A;Reference number: I48313; MUID:91184013; PMID:1964409
A;Accession: I48313
A;Status: translated from GB/EMBL/DDBJ
A;Molecule type: mRNA
A;Residues: 1-105 A;Cross-references: UNIPARC:UPI0000022AAF; EMBL:X55771; NID:g288155; PIDN:CAA39293.1; PID:g288156
C;Comment: Mammalian testis contains two forms of cytochrome c, one identical with the form found in somatic tissues and another that is expressed in a stage-specific manner during spermatogenic differentiation.
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: blocked amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain; sperm; testis
F;2-105/Product: cytochrome c, testis-specific #status experimental F;5-99/Domain: cytochrome c homology F;2/Modified site: blocked amino end (Gly) (in mature form) (probably acetylated) #status experimental
F;15,18/Binding site: heme (Cys) (covalent) #status experimental
F;19,81/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCRTT
cytochrome c, testis-specific - rat
C;Species: Rattus norvegicus (Norway rat)
C;Date: 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 31-Dec-2004
C;Accession: A28160
R;Virbasius, J.V.; Scarpulla, R.C.
J. Biol. Chem. 263, 6791-6796, 1988
A;Title: Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants.
A;Reference number: A28160; MUID:88198250; PMID:2834389
A;Accession: A28160
A;Molecule type: DNA; mRNA
A;Residues: 1-105 A;Cross-references: UNIPROT:P10715; UNIPARC:UPI0000167AA4; GB:M20627; GB:M20628; NID:g203727; PIDN:AAA41015.1; PID:g203729; GB:M20623; NID:g203730; PID:g203731
C;Comment: Mammalian testis contains two forms of cytochrome c, one identical to the form found in somatic tissues and another that is expressed in a stage-specific manner during spermatogenic differentiation.
C;Genetics:
A;Introns: 57/1
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain; sperm; testis
F;2-105/Product: cytochrome c, testis-specific #status predicted F;5-99/Domain: cytochrome c homology F;2/Modified site: acetylated amino end (Gly) (in mature form) #status predicted
F;15,18/Binding site: heme (Cys) (covalent) #status predicted
F;19,81/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCPY
cytochrome c - pigeon (tentative sequence)
C;Species: Columba livia (domestic pigeon)
C;Date: 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 31-Dec-2004
C;Accession: A00013
R;Chan, S.K.; Tulloss, I.; Margoliash, E.
unpublished results, cited by Wojciech, R., and Margoliash, E., in Handbook of Biochemistry, Sober, H.A., ed., pp.C158-C161, Chemical Rubber Co., Cleveland, 1968
A;Reference number: A94490
A;Accession: A00013
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00021; UNIPARC:UPI0000128BA4
A;Note: compositions of tryptic peptides and sequences of residues 89-91, 92-99, and 100-104 were determined
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCCH
cytochrome c [validated] - chicken
C;Species: Gallus gallus (chicken)
C;Date: 24-Apr-1984 #sequence_revision 20-Aug-1994 #text_change 31-Dec-2004
C;Accession: A00014; A04611
R;Limbach, K.J.; Wu, R.
Nucleic Acids Res. 11, 8931-8950, 1983
A;Title: Isolation and characterization of two alleles of the chicken cytochrome c gene.
A;Reference number: A00014; MUID:84169527; PMID:6324108
A;Accession: A00014
A;Molecule type: DNA
A;Residues: 1-105 A;Cross-references: UNIPROT:P00016; UNIPARC:UPI0000171302; GB:K02303; NID:g211708; PIDN:AAA48741.1; PID:g211709
R;Chan, S.K.; Margoliash, E.
J. Biol. Chem. 241, 507-515, 1966
A;Title: Amino acid sequence of chicken heart cytochrome.
A;Reference number: A04611; MUID:66080352; PMID:5903744
A;Accession: A04611
A;Molecule type: protein
A;Residues: 2-105 A;Cross-references: UNIPARC:UPI0000128BA2
C;Genetics:
A;Introns: 57/1
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;2-105/Product: cytochrome c #status experimental F;5-99/Domain: cytochrome c homology F;2/Modified site: acetylated amino end (Gly) (in mature form) #status experimental
F;15,18/Binding site: heme (Cys) (covalent) #status experimental
F;19,81/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCTK
cytochrome c - turkey (tentative sequence)
C;Species: Meleagris gallopavo (common turkey)
C;Date: 31-Dec-1990 #sequence_revision 31-Dec-1990 #text_change 31-Dec-2004
C;Accession: A04612; A00014
R;Chan, S.K.; Tulloss, I.; Margoliash, E.
submitted to the Atlas, June 1966
A;Reference number: A04612
A;Accession: A04612
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00016; UNIPARC:UPI0000128BA2
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCDK
cytochrome c - duck (tentative sequence)
C;Species: Anas platyrhynchos (domestic duck)
C;Date: 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 31-Dec-2004
C;Accession: A00015
R;Chan, S.K.; Tulloss, I.; Margoliash, E.
submitted to the Atlas, June 1966
A;Reference number: A04612
A;Contents: compositions of tryptic peptides; sequences of residues 1-5, 92-99, and 100-104
A;Accession: A00015
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00020; UNIPARC:UPI0000128B93
A;Experimental source: Pekin breed
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCOS
cytochrome c [validated] - ostrich
C;Species: Struthio camelus (ostrich)
C;Date: 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 31-Dec-2004
C;Accession: A00016
R;Howard, N.L.; Joubert, F.J.; Strydom, D.J.
Comp. Biochem. Physiol. B 48, 75-85, 1974
A;Title: The amino acid sequence of ostrich (Struthio camelus) cytochrome C.
A;Reference number: A00016; MUID:74175476; PMID:4364857
A;Accession: A00016
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00019; UNIPARC:UPI0000128BE0
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCEU
cytochrome c [validated] - emu
C;Species: Dromaius novaehollandiae (emu)
C;Date: 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 31-Dec-2004
C;Accession: A00017
R;Augusteyn, R.C.
Biochim. Biophys. Acta 303, 1-7, 1973
A;Title: Primary structure of cytochrome c from the emu, Dromaeus novaehollandiae.
A;Reference number: A00017; MUID:73171069; PMID:4349739
A;Accession: A00017
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00018; UNIPARC:UPI0000128BAD
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: blocked amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: blocked amino end (Gly) (probably acetylated) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCPN
cytochrome c - king penguin
C;Species: Aptenodytes patagonicus (king penguin)
C;Date: 04-Dec-1986 #sequence_revision 04-Dec-1986 #text_change 31-Dec-2004
C;Accession: A00018
R;Chan, S.K.; Tulloss, I.; Margoliash, E.
submitted to the Atlas, July 1967
A;Reference number: A38040
A;Accession: A00018
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00017; UNIPARC:UPI0000128B95
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCST
cytochrome c - snapping turtle (tentative sequence)
C;Species: Chelydra serpentina (snapping turtle)
C;Date: 24-Apr-1984 #sequence_revision 30-Sep-1988 #text_change 31-Dec-2004
C;Accession: A00019
R;Chan, S.K.; Tulloss, I.; Margoliash, E.
Biochemistry 5, 2586-2597, 1966
A;Title: Primary structure of the cytochrome c from the snapping turtle, Chelydra serpentina.
A;Reference number: A00019; MUID:67172948; PMID:5968568
A;Accession: A00019
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00022; UNIPARC:UPI0000128BA1
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCFG
cytochrome c - bullfrog (tentative sequence)
C;Species: Rana catesbeiana (bullfrog)
C;Date: 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Dec-2004
C;Accession: A00021
R;Chan, S.K.; Walasek, O.F.; Barlow, G.H.; Margoliash, E.
submitted to the Atlas, July 1967
A;Reference number: A00021
A;Accession: A00021
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00024; UNIPARC:UPI0000128BD3
C;Comment: The presence of Lys-104 is not certain.
C;Comment: We have arranged the amino acids in positions 88-92 by homology with the other cytochrome c sequences. This arrangement is contrary to the authors'.
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
F;20-102/Disulfide bonds: #status experimental
>P1;CCBN
cytochrome c [validated] - skipjack tuna
C;Species: Euthynnus pelamis, Katsuwonus pelamis (skipjack tuna)
C;Date: 13-Jul-1981 #sequence_revision 10-Oct-1997 #text_change 31-Dec-2004
C;Accession: A00022
R;Nakayama, T.; Titani, K.; Narita, K.
J. Biochem. 70, 311-326, 1971
A;Title: The amino acid sequence of cytochrome c from bonito (Katsuwonus pelamis, Linnaeus).
A;Reference number: A00022; MUID:72003272; PMID:5106585
A;Accession: A00022
A;Molecule type: protein
A;Residues: 1-103 A;Cross-references: UNIPROT:P00025; UNIPARC:UPI0000110E3B
R;Tanaka, N.; Yamane, T.; Tsukihara, T.; Ashida, T.; Kakudo, M.
submitted to the Brookhaven Protein Data Bank, August 1976
A;Reference number: A50107; PDB:1CYC
A;Contents: annotation; X-ray crystallography, 2.3 angstroms, residues 1-103
R;Tanaka, N.; Yamane, T.; Tsukihara, T.; Ashida, T.; Kakudo, M.
J. Biochem. 77, 147-162, 1975
A;Title: The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function.
A;Reference number: A38036; MUID:75170243; PMID:166072
A;Contents: annotation; X-ray crystallography, reduced form, 2.3 angstroms
R;Matsuura, Y.; Hata, Y.; Yamaguchi, T.; Tanaka, N.; Kakudo, M.
J. Biochem. 85, 729-737, 1979
A;Title: Structure of bonito heart ferricytochrome c and some remarks on molecular interaction in its crystalline state.
A;Reference number: A38037; MUID:79150869; PMID:218921
A;Contents: annotation; X-ray crystallography, oxidized form, 2.8 angstroms
R;Mandel, N.; Mandel, G.; Trus, B.L.; Rosenburg, J.; Carlson, G.; Dickerson, R.E.
J. Biol. Chem. 252, 4619-4636, 1977
A;Title: Tuna cytochrome c at 2.0 A resolution. III. Coordinate optimization and comparison of structures.
A;Reference number: A38038; MUID:77207068; PMID:194885
A;Contents: annotation; commercial Scombridae, X-ray crystallography, oxidized and reduced forms, 2.0 angstroms
A;Note: this is the final paper in a series
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status experimental
>P1;CCCA
cytochrome c - common carp (tentative sequence)
C;Species: Cyprinus carpio (common carp)
C;Date: 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Dec-2004
C;Accession: A00023
R;Guertler, L.; Horstmann, H.J.
Eur. J. Biochem. 12, 48-57, 1970
A;Title: Die Aminosaeure-sequenz vom Cytochrom c des Karpfens, Cyprinus carpio.
A;Reference number: A00023; MUID:70137310; PMID:5434283
A;Accession: A00023
A;Molecule type: protein
A;Residues: 1-103 A;Cross-references: UNIPROT:P00026; UNIPARC:UPI0000128BAA
A;Note: the sequence of iso-2-cytochrome c differs from that shown in having 4-Asp
A;Note: the protein was obtained from food carp that consisted of two cross-bred strains, the European carp and the Amur carp; the isocytochromes may be the result of strain differences
C;Comment: The sequence shown is iso-1-cytochrome c.
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: blocked amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: blocked amino end (Gly) (probably acetylated) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCDF
cytochrome c [validated] - Puget Sound dogfish
C;Species: Squalus sucklii (Puget Sound dogfish)
C;Date: 23-Oct-1981 #sequence_revision 23-Oct-1981 #text_change 31-Dec-2004
C;Accession: A00024
R;Goldstone, A.; Smith, E.L.
J. Biol. Chem. 242, 4702-4710, 1967
A;Title: Amino acid sequence of the cytochrome c from the dogfish, Squalus sucklii.
A;Reference number: A00024; MUID:68054790; PMID:6061416
A;Accession: A00024
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00027; UNIPARC:UPI0000128BDE
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCLM
cytochrome c [validated] - Pacific lamprey
C;Species: Lampetra tridentata, Entosphenus tridentatus (Pacific lamprey)
C;Date: 13-Jul-1981 #sequence_revision 13-Jul-1981 #text_change 31-Dec-2004
C;Accession: A00025
R;Nolan, C.; Fitch, W.M.; Uzzell, T.; Weiss, L.J.; Margoliash, E.
Biochemistry 12, 4052-4060, 1973
A;Title: Amino acid sequence of a cytochrome c from the common Pacific lamprey, Entosphenus tridentatus.
A;Reference number: A00025; MUID:74011773; PMID:4355549
A;Accession: A00025
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00028; UNIPARC:UPI0000128BC2
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCRS
cytochrome c - eastern diamondback rattlesnake
C;Species: Crotalus adamanteus (eastern diamondback rattlesnake)
C;Date: 19-Feb-1984 #sequence_revision 19-Feb-1984 #text_change 31-Dec-2004
C;Accession: A94624; A92021; A00020
R;Ambler, R.
submitted to the Protein Sequence Database, January 1984
A;Reference number: A94624
A;Accession: A94624
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00023; UNIPARC:UPI0000128BA7
R;Bahl, O.P.; Smith, E.L.
J. Biol. Chem. 240, 3585-3593, 1965
A;Title: Amino acid sequence of rattlesnake heart cytochrome c.
A;Reference number: A92021; MUID:66019642; PMID:5835940
A;Accession: A92021
A;Molecule type: protein
A;Residues: 1-85,'SK',88-92,'N',94-100,'K',102-103,'A' A;Cross-references: UNIPARC:UPI0000171C88
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: blocked amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: blocked amino end (Gly) (probably acetylated) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCRSW
cytochrome c - western rattlesnake
C;Species: Crotalus viridis (western rattlesnake)
C;Date: 31-Mar-1992 #sequence_revision 31-Mar-1992 #text_change 31-Dec-2004
C;Accession: S14358
R;Ambler, R.P.; Daniel, M.
Biochem. J. 274, 825-831, 1991
A;Title: Rattlesnake cytochrome c. A re-appraisal of the reported amino acid sequence.
A;Reference number: S14358; MUID:91190099; PMID:1849408
A;Accession: S14358
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00023; UNIPARC:UPI0000128BA7
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: acetylated amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: acetylated amino end (Gly) #status predicted
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCSF
cytochrome c - starfish (Asterias rubens) (tentative sequence)
C;Species: Asterias rubens (common European starfish)
C;Date: 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Dec-2004
C;Accession: A00026
R;Lyddiatt, A.; Boulter, D.
FEBS Lett. 67, 331-334, 1976
A;Title: The amino acid sequence of cytochrome c from Asterias rubens L. (common starfish).
A;Reference number: A00026; MUID:77003681; PMID:183984
A;Accession: A00026
A;Molecule type: protein
A;Residues: 1-103 A;Cross-references: UNIPROT:P00029; UNIPARC:UPI0000128B98
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCWB
cytochrome c - earthworm (Eisenia foetida)
C;Species: Eisenia foetida (common brandling worm, common dung-worm)
C;Date: 24-Apr-1984 #sequence_revision 01-Feb-1985 #text_change 31-Dec-2004
C;Accession: A00027
R;Lyddiatt, A.; Boulter, D.
FEBS Lett. 62, 85-88, 1976
A;Title: The amino acid sequence of cytochrome c from Eisenia foetida (Savigny) (common brandling worm).
A;Reference number: A00027; MUID:76118291; PMID:174956
A;Accession: A00027
A;Molecule type: protein
A;Residues: 1-108 A;Cross-references: UNIPROT:P00030; UNIPARC:UPI0000128BAE
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;9-103/Domain: cytochrome c homology F;19,22/Binding site: heme (Cys) (covalent) #status predicted
F;23,85/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCMM
cytochrome c - monsoon river-prawn
C;Species: Macrobrachium malcolmsonii (monsoon river-prawn)
C;Date: 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Dec-2004
C;Accession: A00028
R;Lyddiatt, A.; Boulter, D.
Comp. Biochem. Physiol. B 55, 337-342, 1976
A;Title: A comparison of cytochrome C from Macrobrachium malcomsonii with other invertebrate cytochromes C.
A;Reference number: A00028; MUID:77024998; PMID:185001
A;Accession: A00028
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00031; UNIPARC:UPI0000128BC6
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: blocked amino end; chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;1/Modified site: blocked amino end (Gly) (probably acetylated) #status experimental
F;14,17/Binding site: heme (Cys) (covalent) #status predicted
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCHA
cytochrome c [validated] - brown garden snail
C;Species: Helix aspersa (brown garden snail)
C;Date: 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Dec-2004
C;Accession: A00029
R;Brown, R.H.; Richardson, M.; Boulter, D.; Ramshaw, J.A.M.; Jefferies, R.P.S.
Biochem. J. 128, 971-974, 1972
A;Title: The amino acid sequence of cytochrome c from Helix aspersa Mueller (garden snail).
A;Reference number: A00029; MUID:73054484; PMID:4344699
A;Accession: A00029
A;Molecule type: protein
A;Residues: 1-104 A;Cross-references: UNIPROT:P00032; UNIPARC:UPI0000128BBD
A;Note: the amidation states of residues 16, 21, 52, 70, and 90 were assigned by homology with other cytochromes c
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;4-98/Domain: cytochrome c homology F;14,17/Binding site: heme (Cys) (covalent) #status experimental
F;18,80/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCFFCM
cytochrome c - Mediterranean fruit fly
C;Species: Ceratitis capitata (Mediterranean fruit fly)
C;Date: 13-Jul-1981 #sequence_revision 30-Jun-1991 #text_change 31-Dec-2004
C;Accession: A00030
R;Fernandez-Sousa, J.M.; Gavilanes, J.G.; Municio, A.M.; Paredes, J.A.; Perez-Aranda, A.; Rodriguez, R.
Biochim. Biophys. Acta 393, 358-367, 1975
A;Title: Primary structure of cytochrome c from the insect Ceratitis capitata.
A;Reference number: A00030; MUID:75205681; PMID:167835
A;Accession: A00030
A;Molecule type: protein
A;Residues: 1-107 A;Cross-references: UNIPROT:P00034; UNIPARC:UPI0000128B46
A;Note: some peptides were positioned by homology
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;8-102/Domain: cytochrome c homology F;18,21/Binding site: heme (Cys) (covalent) #status predicted
F;22,84/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCFFDM
cytochrome c DC4 - fruit fly (Drosophila melanogaster)
C;Species: Drosophila melanogaster
C;Date: 30-Jun-1991 #sequence_revision 20-Aug-1994 #text_change 31-Dec-2004
C;Accession: A22945; A23058; A25506; A38039; A00030
R;Swanson, M.S.; Zieminn, S.M.; Miller, D.D.; Garber, E.A.E.; Margoliash, E.
Proc. Natl. Acad. Sci. U.S.A. 82, 1964-1968, 1985
A;Title: Developmental expression of nuclear genes that encode mitochondrial proteins: insect cytochromes c.
A;Reference number: A94704; MUID:85166253; PMID:2984675
A;Accession: A22945
A;Molecule type: DNA
A;Residues: 1-108 A;Cross-references: UNIPROT:P00034; UNIPARC:UPI0000000FDA; GB:M11381; NID:g157160; PIDN:AAA28437.1; PID:g157161
R;Limbach, K.J.; Wu, R.
Nucleic Acids Res. 13, 631-644, 1985
A;Title: Characterization of two Drosophila melanogaster cytochrome c genes and their transcripts.
A;Reference number: A93584; MUID:85215502; PMID:2987802
A;Accession: A23058
A;Molecule type: DNA
A;Residues: 1-108 A;Cross-references: UNIPARC:UPI0000000FDA; GB:X01760; NID:g7782; PIDN:CAA25900.1; PID:g7783
R;Inoue, S.; Inoue, H.; Hiroyoshi, T.; Matsubara, H.; Yamanaka, T.
J. Biochem. 100, 955-965, 1986
A;Title: Developmental variation and amino acid sequences of cytochromes c of the fruit fly Drosophila melanogaster and the flesh fly Boettcherisca peregrina.
A;Reference number: A91907; MUID:87137362; PMID:3029051
A;Accession: A25506
A;Molecule type: protein
A;Residues: 2-108 A;Cross-references: UNIPARC:UPI0000128B46
R;Nolan, C.; Weiss, L.J.; Adams, J.J.; Margoliash, E.
unpublished results, cited by Wojciech, R., and Margoliash, E., in Handbook of Biochemistry, Sober, H.A., ed., pp.C160-C161, Chemical Rubber Co., Cleveland, 1968
A;Reference number: A38039
A;Accession: A38039
A;Molecule type: protein
A;Residues: 2-54,'N',56-64,'QD',67-108 A;Cross-references: UNIPARC:UPI0000171C89
A;Note: some peptides were positioned by homology
C;Comment: This protein is expressed at varying, but relatively high levels throughout development.
C;Genetics:
A;Gene: DC4
A;Cross-references: FlyBase:FBgn0000409
A;Map position: 2 36A 10-11
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;2-108/Product: cytochrome c DC4 #status experimental F;9-103/Domain: cytochrome c homology F;19,22/Binding site: heme (Cys) (covalent) #status predicted
F;23,85/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCFHHF
cytochrome c - horn fly
C;Species: Haematobia irritans (horn fly)
C;Date: 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 31-Dec-2004
C;Accession: A38040; A00030
R;Chan, S.K.; Tulloss, I.; Margoliash, E.
submitted to the Atlas, July 1967
A;Reference number: A38040
A;Accession: A38040
A;Molecule type: protein
A;Residues: 1-107 A;Cross-references: UNIPROT:P00035; UNIPARC:UPI0000128BBA
A;Note: some peptides were positioned by homology
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;8-102/Domain: cytochrome c homology F;18,21/Binding site: heme (Cys) (covalent) #status predicted
F;22,84/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCHFGB
cytochrome c - greenbottle fly (Lucilia cuprina) (tentative sequence)
C;Species: Lucilia cuprina
C;Date: 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 31-Dec-2004
C;Accession: A38041; A00030
R;Shaw, D.C.; Williams, K.L.; Smith, E.; Birt, L.M.
Biochim. Biophys. Acta 532, 179-184, 1978
A;Title: The amino acid sequence of cytochrome c from the blowfly Lucilia cuprina.
A;Reference number: A38041; MUID:78080930; PMID:202328
A;Accession: A38041
A;Molecule type: protein
A;Residues: 1-107 A;Cross-references: UNIPROT:P00036; UNIPARC:UPI0000128BC3
A;Note: the compositions of the tryptic peptides and the sequence of residues 44-49 were determined
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;8-102/Domain: cytochrome c homology F;18,21/Binding site: heme (Cys) (covalent) #status predicted
F;22,84/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCLQ
cytochrome c - desert locust
C;Species: Schistocerca gregaria (desert locust)
C;Date: 24-Apr-1984 #sequence_revision 24-Apr-1984 #text_change 31-Dec-2004
C;Accession: A00033
R;Lyddiatt, A.; Boulter, D.
Biochem. J. 163, 333-338, 1977
A;Title: The amino acid sequence of cytochrome c from the locust, Schistocerca gregaria Forskal.
A;Reference number: A00033; MUID:77201499; PMID:194585
A;Accession: A00033
A;Molecule type: protein
A;Residues: 1-107 A;Cross-references: UNIPROT:P00040; UNIPARC:UPI0000128BD9
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;8-102/Domain: cytochrome c homology F;18,21/Binding site: heme (Cys) (covalent) #status predicted
F;22,84/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCMT
cytochrome c [validated] - ailanthus silkmoth
C;Species: Samia cynthia (ailanthus silkmoth)
C;Date: 13-Jul-1981 #sequence_revision 23-Oct-1981 #text_change 31-Dec-2004
C;Accession: A00032
R;Chan, S.K.; Margoliash, E.
J. Biol. Chem. 241, 335-348, 1966
A;Title: Properties and primary structure of the cytochrome c from the flight muscles of the moth, Samia cynthia.
A;Reference number: A92025; MUID:66080329; PMID:5903726
A;Accession: A00032
A;Molecule type: protein
A;Residues: 1-107 A;Cross-references: UNIPROT:P00037; UNIPARC:UPI0000128BD6
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;8-102/Domain: cytochrome c homology F;18,21/Binding site: heme (Cys) (covalent) #status experimental
F;22,84/Binding site: heme iron (His, Met) (axial ligands) #status predicted
>P1;CCWOT
cytochrome c - tobacco hornworm (tentative sequence)
C;Species: Manduca sexta (tobacco hornworm)
C;Date: 30-Sep-1991 #sequence_revision 30-Sep-1991 #text_change 31-Dec-2004
C;Accession: A90578; B22945; A00032
R;Chan, S.K.
Biochim. Biophys. Acta 221, 497-501, 1970
A;Title: Biochemical studies in the developing thoracic muscles of the tobacco horn worm.
A;Reference number: A90578; MUID:71108407; PMID:5499433
A;Accession: A90578
A;Molecule type: protein
A;Residues: 1-107 A;Cross-references: UNIPROT:P00039; UNIPARC:UPI0000171C8A
A;Note: the compositions of chymotryptic peptides were determined and residues were ordered by homology with silkmoth cytochrome c
R;Swanson, M.S.; Zieminn, S.M.; Miller, D.D.; Garber, E.A.E.; Margoliash, E.
Proc. Natl. Acad. Sci. U.S.A. 82, 1964-1968, 1985
A;Title: Developmental expression of nuclear genes that encode mitochondrial proteins: insect cytochromes c.
A;Reference number: A94704; MUID:85166253; PMID:2984675
A;Accession: B22945
A;Molecule type: mRNA
A;Residues: 26-31,'I',33-53,'D',55-63,'NE',66-107 A;Cross-references: UNIPARC:UPI000016BF44; GB:M11382; NID:g159496; PIDN:AAA29308.1; PID:g159497
A;Note: the authors translated the codon GAT for residue 29 as Asn, AAT for residue 39 as Gln, and GAG for residue 40 as Asp
C;Superfamily: cytochrome c/cytochrome c2; cytochrome c homology
C;Keywords: chromoprotein; electron transfer; heme; iron; metalloprotein; mitochondrion; oxidative phosphorylation; respiratory chain
F;8-102/Domain: cytochrome c homology F;18,21/Binding site: heme (Cys) (covalent) #status predicted
F;22,84/Binding site: heme iron (His, Met) (axial ligands) #status predicted
