ID CYC_HUMAN STANDARD; PRT; 104 AA. AC P00001; Q96BV4; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-MAR-2004 (Rel. 43, Last annotation update) DE Cytochrome c. GN CYCS OR CYC. OS Homo sapiens (Human), and OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 9598; RN [1] RP SEQUENCE. RC SPECIES=Human; TISSUE=Heart; RA Matsubara H., Smith E.L.; RT "The amino acid sequence of human heart cytochrome c."; RL J. Biol. Chem. 237:3575-3576(1962). RN [2] RP SEQUENCE. RC SPECIES=Human; TISSUE=Heart; RA Matsubara H., Smith E.L.; RT "Human heart cytochrome c. Chymotryptic peptides, tryptic peptides, RT and the complete amino acid sequence."; RL J. Biol. Chem. 238:2732-2753(1963). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Human; RX MEDLINE=89071748; PubMed=2849112; RA Evans M.J., Scarpulla R.C.; RT "The human somatic cytochrome c gene: two classes of processed RT pseudogenes demarcate a period of rapid molecular evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 85:9625-9629(1988). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Amygdala; RA Ansorge W., Wirkner U., Mewes H.-W., Weil B., Wiemann S.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC SPECIES=Human; RC TISSUE=Bone marrow, Brain, Skeletal muscle, Skin, and Urinary bladder; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP SEQUENCE, AND COMPOSITION OF CHYMOTRYPTIC PEPTIDES. RC SPECIES=P.troglodytes; RX MEDLINE=69150225; PubMed=4975694; RA Needleman S.B., Margoliash E.; RL Unpublished results, cited by: RL Margoliash E., Fitch W.M.; RL Ann. N. Y. Acad. Sci. 151:359-381(1968). RN [7] RP REVIEW ON ROLE IN APOPTOSIS. RX MEDLINE=98175474; PubMed=9515723; RA Skulachev V.P.; RT "Cytochrome c in the apoptotic and antioxidant cascades."; RL FEBS Lett. 423:275-280(1998). CC -!- FUNCTION: Electron carrier protein. The oxidized form of the CC cytochrome c heme group can accept an electron from the heme group CC of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c CC then transfers this electron to the cytochrome oxidase complex, CC the final protein carrier in the mitochondrial electron-transport CC chain. CC -!- FUNCTION: Play a role in apoptosis. Suppression of the anti- CC apoptotic members or activation of the pro-apoptotic members of CC the Bcl-2 family leads to altered mitochondrial membrane CC permeability resulting in release of cytochrome c into the CC cytosol. Binding of cytochrome c to Apaf-1 triggers the activation CC of caspase-9, which then accelerates apoptosis by activating other CC caspases. CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- PTM: Binds 1 heme group per molecule. CC -!- SIMILARITY: Belongs to the cytochrome c family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M22877; AAA35732.1; -. DR EMBL; AL713681; CAD28485.1; -. DR EMBL; BC005299; AAH05299.1; -. DR EMBL; BC008475; AAH08475.1; -. DR EMBL; BC008477; AAH08477.1; -. DR EMBL; BC009578; AAH09578.1; -. DR EMBL; BC009579; AAH09579.1; -. DR EMBL; BC009582; AAH09582.1; -. DR EMBL; BC009587; AAH09587.1; -. DR EMBL; BC009602; AAH09602.1; -. DR EMBL; BC009607; AAH09607.1; -. DR EMBL; BC014359; AAH14359.1; -. DR EMBL; BC014361; AAH14361.1; -. DR EMBL; BC015130; AAH15130.1; -. DR EMBL; BC016006; AAH16006.1; -. DR EMBL; BC021994; AAH21994.1; -. DR EMBL; BC022330; AAH22330.1; -. DR PIR; A00002; CCCZ. DR PIR; A31764; CCHU. DR HSSP; P00004; 1WEJ. DR Genew; HGNC:19986; CYCS. DR MIM; 123970; -. DR GO; GO:0005739; C:mitochondrion; TAS. DR GO; GO:0006917; P:induction of apoptosis; TAS. DR InterPro; IPR003088; Cyt_CI. DR InterPro; IPR002327; Cyt_CIAB. DR InterPro; IPR000345; CytC_heme_BS. DR Pfam; PF00034; cytochrome_c; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR ProDom; PD000375; Cyt_CIAB; 1. DR PROSITE; PS00190; CYTOCHROME_C; 1. KW Mitochondrion; Electron transport; Respiratory chain; Heme; KW Acetylation; Polymorphism; Apoptosis. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT BINDING 14 14 HEME (COVALENT). FT BINDING 17 17 HEME (COVALENT). FT METAL 18 18 IRON (HEME AXIAL LIGAND). FT METAL 80 80 IRON (HEME AXIAL LIGAND). FT VARIANT 65 65 M -> L (IN 10% OF HUMAN). FT /FTId=VAR_002204. FT CONFLICT 17 17 C -> Y (IN REF. 5; AAH15130). SQ SEQUENCE 104 AA; 11617 MW; D47C9B513DF1C5C2 CRC64; GDVEKGKKIF IMKCSQCHTV EKGGKHKTGP NLHGLFGRKT GQAPGYSYTA ANKNKGIIWG EDTLMEYLEN PKKYIPGTKM IFVGIKKKEE RADLIAYLKK ATNE //