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. 85 1988 9625-9629 MUID 89071748 A31764 DNA 1-105 GB M22877 NID g181241 PIDN AAA35732.1 PID g181242 Matsubara, H. Smith, E.L. J. Biol. Chem. 238 1963 2732-2753 A05676 protein 2-28;29-46;47-100;101-105 Matsubara, H. Smith, E.L. J. Biol. Chem. 237 1962 3575-3576 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. 103 1988 954-961 MUID 89008207 I55192 translated from GB/EMBL/DDBJ mRNA 78-105 GB D00265 NID g2897691 PIDN BAA00187.1 PID g219557 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Pan troglodytes Needleman, S.B. submitted to the Atlas October 1968 A00002 protein 1-104 Needleman, S.B. Margoliash, E. unpublished results, 1966, cited by Margoliash, E., and Fitch, W.M., Ann.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. 240 1965 4277-4283 MUID 66045191 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. 13 1985 617-630 MUID 85215501 A23057 DNA 1-105 EMBL X01756 NID g50618 PIDN CAA25899.1 PID g50619 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 16 1977 1437-1442 MUID 77134768 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. 256 1981 6480-6486 MUID 81215609 A04605 DNA 1-105 GB K00750 GB M28216 NID g550511 PIDN AAA21711.1 PID g203699 Virbasius, J.V. Scarpulla, R.C. J. Biol. Chem. 263 1988 6791-6796 MUID 88198250 C28160 mRNA 1-105 GB M20622 NID g203722 PIDN AAA41014.1 PID g203723 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 1977 1437-1442 MUID 77134768 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. 241 1966 853-863 MUID 66093127 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 16 1977 68-72 MUID 77087753 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 11 1972 145-149 MUID 72096652 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. 241 1966 4480-4486 MUID 67041932 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. 43 1965 1187-1206 MUID 66072936 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. 241 1966 1166-1177 MUID 66132521 A92022 protein 1-104 Tsunasawa, S. Narita, K. J. Biochem. 92 1982 607-613 ALERT: data truncated here for web previewing.