P R O T E I N S E Q U E N C E D A T A B A S E of PIR-International Release 70.03, November 09, 2001 262525 sequences, 89717977 residues Protein Information Resource (PIR)* National Biomedical Research Foundation 3900 Reservoir Road, N.W., Washington, DC 20007, USA Japan International Protein Munich Information Center for Information Database (JIPID) Protein Sequences (MIPS) Amakubo 1-16-1 GSF-Forschungszentrum f. Umwelt und Gesundheit Tsukuba 305-0005, Japan am Max-Planck-Instut f. Biochemie Am Klopferspitz 18, D-82152 Martinsried, FRG This database may be redistributed without prior consent, provided that this notice be given to each user and that the words "Derived from" shall precede this notice if the database has been altered by the redistributor. Copyright 2000, PIR-International. *PIR is a registered mark of NBRF.
CCHU A31764 A05676 I55192 A00001 24-Apr-1984 30-Sep-1991 28-Jul-2000
cytochrome c [validated] human man Homo sapiens Evans, M.J. Scarpulla, R.C. Proc. Natl. Acad. Sci. U.S.A. 8519889625-9629 The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution. MUID89071748 A31764 DNA 1-105 GBM22877 NIDg181241 PIDNAAA35732.1 PIDg181242 Matsubara, H. Smith, E.L. J. Biol. Chem. 23819632732-2753 Human heart cytochrome c. Chymotryptic peptides, tryptic peptides, and the complete amino acid sequence. A05676 protein 2-28;29-46;47-100;101-105 Matsubara, H. Smith, E.L. J. Biol. Chem. 23719623575-3576 The amino acid sequence of human heart cytochrome c. annotation 66-Leu is found in 10% of the molecules in pooled protein Tanaka, Y. Ashikari, T. Shibano, Y. Amachi, T. Yoshizumi, H. Matsubara, H. J. Biochem. 1031988954-961 Construction of a human cytochrome c gene and its functional expression in Saccharomyces cerevisiae. MUID89008207 I55192 translated from GB/EMBL/DDBJ mRNA 78-105 GBD00265 NIDg2897691 PIDNBAA00187.1 PIDg219557 57/1 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation polymorphism respiratory chain product cytochrome c 2-105 experimental domain cytochrome c homology 5-99 modified-site acetylated amino end (Gly) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIW GEDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCCZ A00002 17-Mar-1987 17-Mar-1987 03-Mar-2000
cytochrome c chimpanzee chimpanzee Pan troglodytes Needleman, S.B. submitted to the Atlas October1968 A00002 protein 1-104 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 annotation compositions of chymotryptic peptides cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGIIWG EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMQR A00003 17-Mar-1987 17-Mar-1987 03-Mar-2000
cytochrome c rhesus macaque rhesus macaque Macaca mulatta Rothfus, J.A. Smith, E.L. J. Biol. Chem. 24019654277-4283 Amino acid sequence of rhesus monkey heart cytochrome c. MUID66045191 compositions of chymotryptic peptides sequences of residues 55-61 and 68-70 A00003 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGYSYTAANKNKGITWG EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMKP A00004 17-Dec-1982 17-Dec-1982 03-Mar-2000
cytochrome c spider monkey spider monkey Ateles sp. Margoliash, E. unpublished results, cited by Shelnutt, J.A., Rousseau, D.L., Dethmers, J.K., and Margoliash, E., Biochemistry 20, 6485-6497 1981 A00004 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVFKGKRIFIMKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQASGFTYTEANKNKGIIWG EDTLMEYLENPKKYIPGTKMIFVGIKKKEERADLIAYLKKATNE
CCMS A23057 A04604 A00009 31-Dec-1990 30-Sep-1991 28-Jul-2000
cytochrome c [validated] mouse house mouse Mus musculus Limbach, K.J. Wu, R. Nucleic Acids Res. 131985617-630 Characterization of a mouse somatic cytochrome c gene and three cytochrome c pseudogenes. MUID85215501 A23057 DNA 1-105 EMBLX01756 NIDg50618 PIDNCAA25899.1 PIDg50619 strain BALB/c 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 1619771437-1442 Primary structure of mouse, rat, and guinea pig cytochrome c. MUID77134768 A04604 protein 2-105 strain BALB/c 57/1 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-105 experimental domain cytochrome c homology 5-99 modified-site acetylated amino end (Gly) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITW GEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCRT A04605 C28160 A00009 31-Dec-1990 30-Sep-1991 28-Jul-2000
cytochrome c [validated] rat Norway rat Rattus norvegicus Scarpulla, R.C. Agne, K.M. Wu, R. J. Biol. Chem. 25619816480-6486 Isolation and structure of a rat cytochrome c gene. MUID81215609 A04605 DNA 1-105 GBK00750 GBM28216 NIDg550511 PIDNAAA21711.1 PIDg203699 Virbasius, J.V. Scarpulla, R.C. J. Biol. Chem. 26319886791-6796 Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants. MUID88198250 C28160 mRNA 1-105 GBM20622 NIDg203722 PIDNAAA41014.1 PIDg203723 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 1619771437-1442 Primary structure of mouse, rat, and guinea pig cytochrome c. MUID77134768 annotation peptide mapping, compositional analysis, and partial sequencing indicate that rat cytochrome c is identical with that of mouse 57/1 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-105 experimental domain cytochrome c homology 5-99 modified-site blocked amino end (Gly) (in mature form) (probably acetylated) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAAGFSYTDANKNKGITW GEDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCRB A00009 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] rabbit domestic rabbit Oryctolagus cuniculus Needleman, S.B. Margoliash, E. J. Biol. Chem. 2411966853-863 Rabbit heart cytochrome c. MUID66093127 A00009 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKDERADLIAYLKKATNE
CCGW A04608 A00009 31-Dec-1990 31-Dec-1990 28-Jul-2000
cytochrome c [validated] guanaco guanaco Lama guanicoe Niece, R.L. Margoliash, E. Fitch, W.M. Biochemistry 16197768-72 Complete amino acid sequence of guanaco (Lama guanicoe) cytochrome c. MUID77087753 A04608 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCCM A04607 A00009 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c Arabian camel Arabian camel Camelus dromedarius Sokolovsky, M. Moldovan, M. Biochemistry 111972145-149 Primary structure of cytochrome c from the camel, Camelus dromedarius. MUID72096652 A04607 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCWHC A04606 A00009 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c California gray whale California gray whale Eschrichtius robustus, Eschrichtius gibbosus Goldstone, A. Smith, E.L. J. Biol. Chem. 24119664480-4486 Amino acid sequence of whale heart cytochrome c. MUID67041932 A04606 protein 1-104 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAVGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCPG A00007 17-Mar-1987 17-Mar-1987 28-Jul-2000
cytochrome c [validated] pig domestic pig Sus scrofa domestica Stewart, J.W. Margoliash, E. Can. J. Biochem. 4319651187-1206 The primary structure of the cytochrome c from various organs of the hog. MUID66072936 A00007 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE
CCBO A92022 A00007 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome c bovine cattle Bos primigenius taurus Nakashima, T. Higa, H. Matsubara, H. Benson, A. Yasunobu, K.T. J. Biol. Chem. 24119661166-1177 The amino acid sequence of bovine heart cytochrome c. MUID66132521 A92022 protein 1-104 Tsunasawa, S. Narita, K. J. Biochem. 921982607-613 Micro-identification of amino-terminal acetylamino acids in proteins. MUID83056735 annotation acetylation cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE
CCSH A91454 A00007 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome c sheep domestic sheep Ovis orientalis aries, Ovis ammon aries Smith, E.L. Margoliash, E. Fed. Proc. 2319641243-1247 Evolution of cytochrome c. A91454 protein 1-104 amino acid compositions and mobilities of tryptic and chymotryptic peptides were determined cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGEREDLIAYLKKATNE
CCHOD A00006 17-Mar-1987 17-Mar-1987 03-Mar-2000
cytochrome c donkey donkey Equus asinus Walasek, O.F. Margoliash, E. J. Biol. Chem. 2521977830-834 Transmission of the cytochrome c structural gene in horse-donkey crosses. MUID77118552 A00006 protein 1-104 compositions of chymotryptic peptides and the sequence of residues 47-48 were determined mules and hinnies are heterozygous, having equal amounts of horse and donkey cytochromes c cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
CCHOZ A91330 A00006 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome c common zebra common zebra, plains zebra Equus burchelli, Equus quagga Guertler, L. Horstmann, H.J. FEBS Lett. 181971106-108 Zur Primaerstruktur des Cytochromes c des Steppenzebras (Equus quagga boehmi). A91330 protein 1-104 the amino acid composition and the sequence of residues 40-48 were determined cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
CCHO A00005 S59487 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] horse domestic horse Equus caballus Margoliash, E. Smith, E.L. Kreil, G. Tuppy, H. Nature 19219611125-1127 The complete amino-acid sequence. A00005 protein 1-104 Theodorakis, J.L. Armes, L.G. Margoliash, E. Biochim. Biophys. Acta 12521995114-125 beta-Thiopropionyl cytochromes c modified at lysyl residues: preparation and characterization of the monosubstituted horse cytochromes c. MUID96001358 S59487 preliminary protein 1-10;11-18;19-26;27-34;38-47;50-54;55-58;60-67;68-74;75-82;83-97;98-104 Luo, Y. Brayer, G.D. submitted to the Brookhaven Protein Data Bank August1994 PDB1HRC annotation X-ray crystallography, 1.9 angstroms, residues 1-104 Dickerson, R.E. Takano, T. Eisenberg, D. Kallai, O.B. Samson, L. Cooper, A. Margoliash, E. J. Biol. Chem. 24619711511-1533 Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution. MUID71116428 annotation X-ray crystallography, 2.8 angstroms cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 experimental 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE
CCHP A00008 19-Feb-1984 19-Feb-1984 03-Mar-2000
cytochrome c hippopotamus hippopotamus Hippopotamus amphibius Thompson, R.B. Borden, D. Tarr, G.E. Margoliash, E. J. Biol. Chem. 25319788957-8961 Heterogeneity of amino acid sequence in hippopotamus cytochrome c. MUID79067782 A00008 protein 1-104 3-Ile was also found cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQSPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKQATNE
CCDG A00010 13-Jul-1981 13-Jul-1981 31-Mar-2000
cytochrome c dog dog Canis lupus familiaris McDowall, M.A. Smith, E.L. J. Biol. Chem. 24019654635-4647 Amino acid sequence of dog heart cytochrome c. MUID66047448 A00010 protein 1-104 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQK(C.A.Q.C.H.T.V.E)KGGKHKTGPNLHGLFGRKTGQAPGFSYTDA NKNKGITWGEETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKKATKE
CCSLE A04615 A00010 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c southern elephant seal southern elephant seal Mirounga leonina Augusteyn, R.C. McDowall, M.A. Webb, E.C. Zerner, B. Biochim. Biophys. Acta 2571972264-272 Primary structure of cytochrome c from the elephant seal, Mirounga leonina. MUID72170090 A04615 protein 1-104 peptides were positioned by homology cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EETLMEYLENPKKYIPGTKMIFAGIKKTGERADLIAYLKIATKE
CCBTS A04614 A00010 31-Dec-1990 31-Dec-1990 11-May-2000
cytochrome c Schreibers's long-fingered bat Schreibers's long-fingered bat Miniopterus schreibersi Strydom, D.J. van der Walt, S.J. Botes, D.P. Comp. Biochem. Physiol. B 43197221-24 The amino acid sequence of bat (Miniopteris schreibersi) cytochrome c. MUID73123526 A04614 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFSYTDANKNKGITWG EATLMEYLENPKKYIPGTKMIFAGIKKSAERADLIAYLKKATKE
CCKGG A00011 24-Apr-1984 24-Apr-1984 28-Jul-2000
cytochrome c [validated] eastern gray kangaroo eastern gray kangaroo Macropus giganteus Nolan, C. Margoliash, E. J. Biol. Chem. 24119661049-1059 Primary structure of the cytochrome c from the great grey kangaroo, Macropus canguru. MUID66132505 A00011 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLNGIFGRKTGQAPGFTYTDANKNKGIIWG EDTLMEYLENPKKYIPGTKMIFAGIKKKGERADLIAYLKKATNE
CCMST B28160 A00012 I48313 24-Apr-1984 30-Sep-1991 28-Jul-2000
cytochrome c, testis-specific [validated] cytochrome c T mouse house mouse Mus musculus Virbasius, J.V. Scarpulla, R.C. J. Biol. Chem. 26319886791-6796 Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants. MUID88198250 B28160 mRNA 1-105 GBM20625 NIDg192875 PIDNAAA37501.1 PIDg309203 Hennig, B. Eur. J. Biochem. 551975167-183 Change of cytochrome c structure during development of the mouse. MUID76022386 A00012 protein 2-57,'IV',60-61,'ZZ',64-66,'Z',68-69,'ZB',72-105 strain BALB/c Hake, L.E. Alcivar, A.A. Hecht, N.B. Development 1101990249-257 Changes in mRNA length accompany translational regulation of the somatic and testis-specific cytochrome c genes during spermatogenesis in the mouse. MUID91184013 I48313 translated from GB/EMBL/DDBJ mRNA 1-105 EMBLX55771 NIDg288155 PIDNCAA39293.1 PIDg288156 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. cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain sperm testis product cytochrome c, testis-specific 2-105 experimental domain cytochrome c homology 5-99 modified-site blocked amino end (Gly) (in mature form) (probably acetylated) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDAEAGKKIFVQKCAQCHTVEKGGKHKTGPNLWGLFGRKTGQAPGFSYTDANKNKGVIW SEETLMEYLENPKKYIPGTKMIFAGIKKKSEREDLIKYLKQATSS
CCRTT A28160 30-Sep-1991 30-Sep-1991 03-Mar-2000
cytochrome c, testis-specific rat Norway rat Rattus norvegicus Virbasius, J.V. Scarpulla, R.C. J. Biol. Chem. 26319886791-6796 Structure and expression of rodent genes encoding the testis-specific cytochrome c. Differences in gene structure and evolution between somatic and testicular variants. MUID88198250 A28160 DNA mRNA 1-105 GBM20627 GBM20628 NIDg203727 PIDNAAA41015.1 PIDg203729 GBM20623 NIDg203730 PIDg203731 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. 57/1 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain sperm testis product cytochrome c, testis-specific 2-105 predicted domain cytochrome c homology 5-99 modified-site acetylated amino end (Gly) (in mature form) 2 predicted binding-site heme (Cys) (covalent) 15,18 predicted binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDAEAGKKIFIQKCAQCHTVEKGGKHKTGPNLWGLFGRKTGQAPGFSYTDANKNKGVIW TEETLMEYLENPKKYIPGTKMIFAGIKKKSEREDLIQYLKEATSS
CCPY A00013 04-Dec-1986 04-Dec-1986 03-Mar-2000
cytochrome c pigeon domestic pigeon Columba livia 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 A00013 protein 1-104 compositions of tryptic peptides and sequences of residues 89-91, 92-99, and 100-104 were determined cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKAERADLIAYLKQATAK
CCCH A00014 A04611 24-Apr-1984 20-Aug-1994 28-Jul-2000
cytochrome c [validated] chicken chicken Gallus gallus Limbach, K.J. Wu, R. Nucleic Acids Res. 1119838931-8950 Isolation and characterization of two alleles of the chicken cytochrome c gene. MUID84169527 A00014 DNA 1-105 GBK02303 NIDg211708 PIDNAAA48741.1 PIDg211709 Chan, S.K. Margoliash, E. J. Biol. Chem. 2411966507-515 Amino acid sequence of chicken heart cytochrome. MUID66080352 A04611 protein 2-105 57/1 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c 2-105 experimental domain cytochrome c homology 5-99 modified-site acetylated amino end (Gly) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 15,18 experimental binding-site heme iron (His, Met) (axial ligands) 19,81 predicted 105 complete MGDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGITW GEDTLMEYLENPKKYIPGTKMIFAGIKKKSERVDLIAYLKDATSK
CCTK A04612 A00014 31-Dec-1990 31-Dec-1990 03-Mar-2000
cytochrome c turkey common turkey Meleagris gallopavo Chan, S.K. Tulloss, I. Margoliash, E. submitted to the Atlas June1966 A04612 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERVDLIAYLKDATSK
CCDK A00015 04-Dec-1986 04-Dec-1986 03-Mar-2000
cytochrome c duck domestic duck Anas platyrhynchos Chan, S.K. Tulloss, I. Margoliash, E. submitted to the Atlas June1966 compositions of tryptic peptides sequences of residues 1-5, 92-99, and 100-104 A00015 protein 1-104 Pekin breed cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATAK
CCOS A00016 04-Dec-1986 04-Dec-1986 28-Jul-2000
cytochrome c [validated] ostrich ostrich Struthio camelus Howard, N.L. Joubert, F.J. Strydom, D.J. Comp. Biochem. Physiol. B 48197475-85 The amino acid sequence of ostrich (Struthio camelus) cytochrome C. MUID74175476 A00016 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLDGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATSK
CCEU A00017 04-Dec-1986 04-Dec-1986 28-Jul-2000
cytochrome c [validated] emu emu Dromaius novaehollandiae Augusteyn, R.C. Biochim. Biophys. Acta 30319731-7 Primary structure of cytochrome c from the emu, Dromaeus novaehollandiae. MUID73171069 A00017 protein 1-104 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLNGLFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATSK
CCPN A00018 04-Dec-1986 04-Dec-1986 03-Mar-2000
cytochrome c king penguin king penguin Aptenodytes patagonicus Chan, S.K. Tulloss, I. Margoliash, E. submitted to the Atlas July1967 A00018 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDIEKGKKIFVQKCSQCHTVEKGGKHKTGPNLHGIFGRKTGQAEGFSYTDANKNKGITWG EDTLMEYLENPKKYIPGTKMIFAGIKKKSERADLIAYLKDATSK
CCST A00019 24-Apr-1984 30-Sep-1988 31-Mar-2000
cytochrome c snapping turtle snapping turtle Chelydra serpentina Chan, S.K. Tulloss, I. Margoliash, E. Biochemistry 519662586-2597 Primary structure of the cytochrome c from the snapping turtle, Chelydra serpentina. MUID67172948 A00019 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete tentative GDVEK.GKKIF.VQKCAQCHTVEKGGKH.KTGPNLNGL.IGRKTGQAEGF.SYTEANKN. KGITWG.EETLM.EY.LENPKKY.IPGTKM.IF.AGIKKKAERADL.IAY.LKDATSK
CCFG A00021 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c bullfrog bullfrog Rana catesbeiana Chan, S.K. Walasek, O.F. Barlow, G.H. Margoliash, E. submitted to the Atlas July1967 A00021 protein 1-104 The presence of Lys-104 is not certain. 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'. cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted disulfide-bonds 20-102 experimental 104 complete tentative GDVEKGKKIF(V,Q.K.C.A.Q.C.H.T.C,E.K.G.G.K.H)KVGPNLYGLIGRKTGQA AGFSYTDANKNKGITW(G.E,D,T.L.M.E.Y)LENPKKYIPGTKMIFAGI(K.K.K.G. E.R.Q)DLIAY(L.K.S,A,C,S,K)
CCBN A00022 13-Jul-1981 10-Oct-1997 28-Jul-2000
cytochrome c [validated] skipjack tuna skipjack tuna Euthynnus pelamis, Katsuwonus pelamis Nakayama, T. Titani, K. Narita, K. J. Biochem. 701971311-326 The amino acid sequence of cytochrome c from bonito (Katsuwonus pelamis, Linnaeus). MUID72003272 A00022 protein 1-103 Tanaka, N. Yamane, T. Tsukihara, T. Ashida, T. Kakudo, M. submitted to the Brookhaven Protein Data Bank August1976 PDB1CYC annotation X-ray crystallography, 2.3 angstroms, residues 1-103 Tanaka, N. Yamane, T. Tsukihara, T. Ashida, T. Kakudo, M. J. Biochem. 771975147-162 The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function. MUID75170243 annotation X-ray crystallography, reduced form, 2.3 angstroms Matsuura, Y. Hata, Y. Yamaguchi, T. Tanaka, N. Kakudo, M. J. Biochem. 851979729-737 Structure of bonito heart ferricytochrome c and some remarks on molecular interaction in its crystalline state. MUID79150869 annotation X-ray crystallography, oxidized form, 2.8 angstroms Mandel, N. Mandel, G. Trus, B.L. Rosenburg, J. Carlson, G. Dickerson, R.E. J. Biol. Chem. 25219774619-4636 Tuna cytochrome c at 2.0 A resolution. III. Coordinate optimization and comparison of structures. MUID77207068 annotation commercial Scombridae, X-ray crystallography, oxidized and reduced forms, 2.0 angstroms this is the final paper in a series cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 experimental 103 complete GDVAKGKKTFVQKCAQCHTVENGGKHKVGPNLWGLFGRKTGQAEGYSYTDANKSKGIVWN ENTLMEYLENPKKYIPGTKMIFAGIKKKGERQDLVAYLKSATS
CCCA A00023 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c common carp common carp Cyprinus carpio Guertler, L. Horstmann, H.J. Eur. J. Biochem. 12197048-57 Die Aminosaeure-sequenz vom Cytochrom c des Karpfens, Cyprinus carpio. MUID70137310 A00023 protein 1-103 the sequence of iso-2-cytochrome c differs from that shown in having 4-Asp 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 The sequence shown is iso-1-cytochrome c. cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 103 complete tentative GDVEK.GKK.VFVQK.CAQCHTVZBGGK.HK.VGPNLWGLFGRK.TGQAPGFSYTBABK. SK.GIVWBZZTLMEYLZBPK.KYIPGTK.MIFAGIK.KKGER.ADLIAYLK.SATS
CCDF A00024 23-Oct-1981 23-Oct-1981 28-Jul-2000
cytochrome c [validated] Puget Sound dogfish Puget Sound dogfish Squalus sucklii Goldstone, A. Smith, E.L. J. Biol. Chem. 24219674702-4710 Amino acid sequence of the cytochrome c from the dogfish, Squalus sucklii. MUID68054790 A00024 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKVFVQKCAQCHTVENGGKHKTGPNLSGLFGRKTGQAQGFSYTDANKSKGITWQ QETLRIYLENPKKYIPGTKMIFAGLKKKSERQDLIAYLKKTAAS
CCLM A00025 13-Jul-1981 13-Jul-1981 28-Jul-2000
cytochrome c [validated] Pacific lamprey Pacific lamprey Lampetra tridentata, Entosphenus tridentatus Nolan, C. Fitch, W.M. Uzzell, T. Weiss, L.J. Margoliash, E. Biochemistry 1219734052-4060 Amino acid sequence of a cytochrome c from the common Pacific lamprey, Entosphenus tridentatus. MUID74011773 A00025 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 experimental binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKVFVQKCSQCHTVEKAGKHKTGPNLSGLFGRKTGQAPGFSYTDANKSKGIVWN QETLFVYLENPKKYIPGTKMIFAGIKKEGERKDLIAYLKKSTSE
CCRS A94624 A92021 A00020 19-Feb-1984 19-Feb-1984 03-Mar-2000
cytochrome c eastern diamondback rattlesnake eastern diamondback rattlesnake Crotalus adamanteus Ambler, R. submitted to the Protein Sequence Database January1984 A94624 protein 1-104 Bahl, O.P. Smith, E.L. J. Biol. Chem. 24019653585-3593 Amino acid sequence of rattlesnake heart cytochrome c. MUID66019642 A92021 protein 1-85,'SK',88-92,'N',94-100,'K',102-103,'A' cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFSMKCGTCHTVEEGGKHKTGPNLHGLFGRKTGQAVGYSYTAANKNKGIIWG DDTLMEYLENPKKYIPGTKMVFTGLKSKKERTDLIAYLKEATAK
CCRSW S14358 31-Mar-1992 31-Mar-1992 03-Mar-2000
cytochrome c western rattlesnake western rattlesnake Crotalus viridis Ambler, R.P. Daniel, M. Biochem. J. 2741991825-831 Rattlesnake cytochrome c. A re-appraisal of the reported amino acid sequence. MUID91190099 S14358 protein 1-104 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site acetylated amino end (Gly) 1 predicted binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFSMKCGTCHTVEEGGKHKTGPNLHGLFGRKTGQAVGYSYTAANKNKGIIWG DDTLMEYLENPKKYIPGTKMVFTGLKSKKERTDLIAYLKEATAK
CCSF A00026 24-Apr-1984 24-Apr-1984 31-Mar-2000
cytochrome c starfish (Asterias rubens) common European starfish Asterias rubens Lyddiatt, A. Boulter, D. FEBS Lett. 671976331-334 The amino acid sequence of cytochrome c from Asterias rubens L. (common starfish). MUID77003681 A00026 protein 1-103 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 103 complete tentative GQVEKGKKIFVQRCAQCHTVEKAGKHK.TGPNLNGILGRKTGQAAGFSYTDANRNKGITW K.NETLFEYLENPKKYIPGTKMVFAGLK.KQKERQDLIAYLEAATK
T32611 T32611 S13048 03-Mar-2000 03-Mar-2000 28-Jul-2000
cytochrome c [validated] protein E04A4.7 Caenorhabditis elegans Caenorhabditis elegans Sammons, L. Wohldmann, P. Biewald, T. submitted to the EMBL Data Library December1997 The sequence of C. elegans cosmid E04A4. T32611 translated from GB/EMBL/DDBJ DNA 1-111 EMBLAF038611 PIDNAAB92035.1 GSPDBGN00022 CESPE04A4.7 strain Bristol N2; clone E04A4 Vanfleteren, J.R. Evers, E.A.I.M. van de Werken, G. van Beeumen, J.J. Biochem. J. 2711990613-620 The primary structure of cytochrome c from the nematode Caenorhabditis elegans. MUID91058490 S13048 protein 2-65,'K',67-111 CESPE04A4.7 4 60/3 cytochrome c cytochrome c homology acetylated amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion domain cytochrome c homology 10-103 modified-site acetylated amino end (Ser) (in mature form) 2 experimental binding-site heme (Cys) (covalent) 20,23 experimental binding-site heme iron (His, Met) (axial ligands) 24,85 predicted 111 complete MSDIPAGDYEKGKKVYKQRCLQCHVVDSTATKTGPTLHGVIGRTSGTVSGFDYSAANKNK GVVWTRETLFEYLLNPKKYIPGTKMVFAGLKKADERADLIKYIEVESAKSL
T27492 T27492 03-Nov-2000 03-Nov-2000 03-Nov-2000
cytochrome c ZC116.2 Caenorhabditis elegans Caenorhabditis elegans Smye, R. submitted to the EMBL Data Library June1996 T27492 translated from GB/EMBL/DDBJ DNA 1-123 EMBLZ74046 PIDNCAA98555.1 GSPDBGN00023 CESPZC116.2 clone ZC116 CESPZC116.2 5 24/3; 94/3 cytochrome c cytochrome c homology chromoprotein heme iron metalloprotein domain cytochrome c homology 20-113 binding-site heme (Cys) (covalent) 30,33 predicted binding-site heme iron (His, Met) (axial ligands) 34,95 predicted 123 complete MGKKKSDTASGGAIPEGDNEKGKKIFKQRCEQCHVVNSLQTKTGPTLNGVIGRQSGQVAG FDYSAANKNKGVVWDRQTLFDYLADPKKYIPGTKMVFAGLKKADERADLIKFIEVEAAKK PSA
CCWB A00027 24-Apr-1984 01-Feb-1985 03-Mar-2000
cytochrome c earthworm (Eisenia foetida) common brandling worm, common dung-worm Eisenia foetida Lyddiatt, A. Boulter, D. FEBS Lett. 62197685-88 The amino acid sequence of cytochrome c from Eisenia foetida (Savigny) (common brandling worm). MUID76118291 A00027 protein 1-108 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 9-103 binding-site heme (Cys) (covalent) 19,22 predicted binding-site heme iron (His, Met) (axial ligands) 23,85 predicted 108 complete GGIPAGDVEKGKTIFKQRCAQCHTVDKGGPHKTGPNLHGIFGRATGQAAGFAYTDANKSK GITWTKDTLYEYLENPKKYIPGTKMVFAGLKNEKQRANLIAYLEQETK
CCMM A00028 24-Apr-1984 24-Apr-1984 11-May-2000
cytochrome c monsoon river-prawn monsoon river-prawn Macrobrachium malcolmsonii Lyddiatt, A. Boulter, D. Comp. Biochem. Physiol. B 551976337-342 A comparison of cytochrome C from Macrobrachium malcomsonii with other invertebrate cytochromes C. MUID77024998 A00028 protein 1-104 cytochrome c cytochrome c homology blocked amino end chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 modified-site blocked amino end (Gly) (probably acetylated) 1 experimental binding-site heme (Cys) (covalent) 14,17 predicted binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GDVEKGKKIFVQRCAQCHSAQANLKHKTGPNLNGLFGRQTGQASGYVYTDANKAKGITWQ ADTLDVYLENPKKYIPGTKMVFAGLKKANERADLIAYLKQATNL
CCHA A00029 24-Apr-1984 24-Apr-1984 28-Jul-2000
cytochrome c [validated] brown garden snail brown garden snail Helix aspersa Brown, R.H. Richardson, M. Boulter, D. Ramshaw, J.A.M. Jefferies, R.P.S. Biochem. J. 1281972971-974 The amino acid sequence of cytochrome c from Helix aspersa Mueller (garden snail). MUID73054484 A00029 protein 1-104 the amidation states of residues 16, 21, 52, 70, and 90 were assigned by homology with other cytochromes c cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 4-98 binding-site heme (Cys) (covalent) 14,17 experimental binding-site heme iron (His, Met) (axial ligands) 18,80 predicted 104 complete GZAZKGKKIFTQKCLQCHTVEAGGKHKTGPNLSGLFGRKQGQAPGFAYTDANKGKGITWK NQTLFEYLENPKKYIPGTKMVFAGLKBZTERVHLIAYLZZATKK
CCFFCM A00030 13-Jul-1981 30-Jun-1991 03-Mar-2000
cytochrome c Mediterranean fruit fly Mediterranean fruit fly Ceratitis capitata Fernandez-Sousa, J.M. Gavilanes, J.G. Municio, A.M. Paredes, J.A. Perez-Aranda, A. Rodriguez, R. Biochim. Biophys. Acta 3931975358-367 Primary structure of cytochrome c from the insect Ceratitis capitata. MUID75205681 A00030 protein 1-107 some peptides were positioned by homology cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 predicted binding-site heme iron (His, Met) (axial ligands) 22,84 predicted 107 complete GVPAGDVEKGKKLFVQRCAQCHTVEAGGKHKVGPNLHGLIGRKTGQAAGFAYTDANKAKG ITWNEDTLFEYLENPKKYIPGTKMIFAGLKKPNERGDLIAYLKSATK
CCFFDM A22945 A23058 A25506 A38039 A00030 30-Jun-1991 20-Aug-1994 03-Mar-2000
cytochrome c DC4 fruit fly (Drosophila melanogaster) Drosophila melanogaster Swanson, M.S. Zieminn, S.M. Miller, D.D. Garber, E.A.E. Margoliash, E. Proc. Natl. Acad. Sci. U.S.A. 8219851964-1968 Developmental expression of nuclear genes that encode mitochondrial proteins: insect cytochromes c. MUID85166253 A22945 DNA 1-108 GBM11381 NIDg157160 PIDNAAA28437.1 PIDg157161 Limbach, K.J. Wu, R. Nucleic Acids Res. 131985631-644 Characterization of two Drosophila melanogaster cytochrome c genes and their transcripts. MUID85215502 A23058 DNA 1-108 GBX01760 NIDg7782 PIDNCAA25900.1 PIDg7783 Inoue, S. Inoue, H. Hiroyoshi, T. Matsubara, H. Yamanaka, T. J. Biochem. 1001986955-965 Developmental variation and amino acid sequences of cytochromes c of the fruit fly Drosophila melanogaster and the flesh fly Boettcherisca peregrina. MUID87137362 A25506 protein 2-108 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 A38039 protein 2-54,'N',56-64,'QD',67-108 some peptides were positioned by homology This protein is expressed at varying, but relatively high levels throughout development. DC4 FlyBaseFBgn0000409 2 36A 10-11 cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain product cytochrome c DC4 2-108 experimental domain cytochrome c homology 9-103 binding-site heme (Cys) (covalent) 19,22 predicted binding-site heme iron (His, Met) (axial ligands) 23,85 predicted 108 complete MGVPAGDVEKGKKLFVQRCAQCHTVEAGGKHKVGPNLHGLIGRKTGQAAGFAYTDANKAK GITWNEDTLFEYLENPKKYIPGTKMIFAGLKKPNERGDLIAYLKSATK
CCFHHF A38040 A00030 30-Jun-1991 30-Jun-1991 03-Mar-2000
cytochrome c horn fly horn fly Haematobia irritans Chan, S.K. Tulloss, I. Margoliash, E. submitted to the Atlas July1967 A38040 protein 1-107 some peptides were positioned by homology cytochrome c cytochrome c homology chromoprotein electron transfer heme iron metalloprotein mitochondrion oxidative phosphorylation respiratory chain domain cytochrome c homology 8-102 binding-site heme (Cys) (covalent) 18,21 predicted binding-site heme iron (His, Met) (axial ligands) 22,84 predicted