AC P62894; P00006; Q2KJD4;DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.DT 23-JAN-2007, sequence version 2.DT 05-SEP-2012, entry version 80.DE RecName: Full=Cytochrome c;GN Name=CYCS; Synonyms=CYC;OS Bos taurus (Bovine).OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;OC Pecora; Bovidae; Bovinae; Bos.OX NCBI_TaxID=9913;RN [1]RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].RC STRAIN=Hereford; TISSUE=Thymus;RG NIH - Mammalian Gene Collection (MGC) project;RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.RN [2]RP PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.RC TISSUE=Heart;RX MEDLINE=66132521; PubMed=5933874;RA Nakashima T., Higa H., Matsubara H., Benson A.M., Yasunobu K.T.;RT "The amino acid sequence of bovine heart cytochrome c.";RL J. Biol. Chem. 241:1166-1177(1966).RN [3]RP PHOSPHORYLATION AT TYR-49.RC TISSUE=Heart;RX PubMed=16866357; DOI=10.1021/bi060585v;RA Lee I., Salomon A.R., Yu K., Doan J.W., Grossman L.I., Huttemann M.;RT "New prospects for an old enzyme: mammalian cytochrome c is tyrosine-RT phosphorylated in vivo.";RL Biochemistry 45:9121-9128(2006).RN [4]RP PHOSPHORYLATION AT TYR-98.RC TISSUE=Liver;RX PubMed=18471988; DOI=10.1016/j.bbabio.2008.04.023;RA Yu H., Lee I., Salomon A.R., Yu K., Huttemann M.;RT "Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo,RT inhibiting mitochondrial respiration.";RL Biochim. Biophys. Acta 1777:1066-1071(2008).RN [5]RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-105, AND HEME-BINDINGRP SITES.RX PubMed=17634981; DOI=10.1002/prot.21452;RA Mirkin N., Jaconcic J., Stojanoff V., Moreno A.;RT "High resolution X-ray crystallographic structure of bovine heartRT cytochrome c and its application to the design of an electron transferRT biosensor.";RL Proteins 70:83-92(2008).CC -!- FUNCTION: Electron carrier protein. The oxidized form of theCC cytochrome c heme group can accept an electron from the heme groupCC of the cytochrome c1 subunit of cytochrome reductase. Cytochrome cCC then transfers this electron to the cytochrome oxidase complex,CC the final protein carrier in the mitochondrial electron-transportCC chain.CC -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-CC apoptotic members or activation of the pro-apoptotic members ofCC the Bcl-2 family leads to altered mitochondrial membraneCC permeability resulting in release of cytochrome c into theCC cytosol. Binding of cytochrome c to Apaf-1 triggers the activationCC of caspase-9, which then accelerates apoptosis by activating otherCC caspases (By similarity).CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.CC Note=Loosely associated with the inner membrane.CC -!- PTM: Binds 1 heme group per subunit.CC -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half theCC turnover in the reaction with cytochrome c oxidase, down-CC regulating mitochondrial respiration.CC -!- SIMILARITY: Belongs to the cytochrome c family.CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76CC of November 2006;CC URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";CC -----------------------------------------------------------------------CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/termsCC Distributed under the Creative Commons Attribution-NoDerivs LicenseCC -----------------------------------------------------------------------DR EMBL; BC105397; AAI05398.1; -; mRNA.DR IPI; IPI00906486; -.DR PIR; A92022; CCBO.DR RefSeq; NP_001039526.1; NM_001046061.1.DR RefSeq; XP_003582877.1; XM_003582829.1.DR RefSeq; XP_003582879.1; XM_003582831.1.DR RefSeq; XP_003586721.1; XM_003586673.1.DR UniGene; Bt.23981; -.DR PDB; 2B4Z; X-ray; 1.50 A; A=2-105.DR PDB; 2YBB; EM; 19.00 A; Y=2-105.DR PDBsum; 2B4Z; -.DR PDBsum; 2YBB; -.DR ProteinModelPortal; P62894; -.DR SMR; P62894; 2-105.DR DIP; DIP-58978N; -.DR IntAct; P62894; 1.DR STRING; P62894; -.DR PRIDE; P62894; -.DR Ensembl; ENSBTAT00000004594; ENSBTAP00000051780; ENSBTAG00000023823.DR Ensembl; ENSBTAT00000007918; ENSBTAP00000007918; ENSBTAG00000022613.DR GeneID; 100847700; -.DR GeneID; 100850794; -.DR GeneID; 510767; -.DR KEGG; bta:100847700; -.DR KEGG; bta:100850794; -.DR KEGG; bta:510767; -.DR CTD; 54205; -.DR eggNOG; COG3474; -.DR GeneTree; ENSGT00390000009405; -.DR HOGENOM; HOG000009762; -.DR HOVERGEN; HBG003023; -.DR InParanoid; P62894; -.DR KO; K08738; -.DR OMA; IAYLKQY; -.DR OrthoDB; EOG45DWQX; -.DR EvolutionaryTrace; P62894; -.DR NextBio; 20869605; -.DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.DR GO; GO:0020037; F:heme binding; IEA:InterPro.DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.DR Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.DR InterPro; IPR002327; Cyt_c_1A/1B.DR InterPro; IPR009056; Cyt_c_dom.DR InterPro; IPR003088; Cyt_c_I.DR PANTHER; PTHR11961; Cyt_CIAB; 1.DR Pfam; PF00034; Cytochrom_C; 1.DR PRINTS; PR00604; CYTCHRMECIAB.DR SUPFAM; SSF46626; Cytochrome_c; 1.DR PROSITE; PS51007; CYTC; 1.PE 1: Evidence at protein level;KW 3D-structure; Acetylation; Apoptosis; Complete proteome;KW Direct protein sequencing; Electron transport; Heme; Iron;KW Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome;KW Respiratory chain; Transport.FT INIT_MET 1 1 Removed.FT CHAIN 2 105 Cytochrome c.FT /FTId=PRO_0000108209.FT METAL 19 19 Iron (heme axial ligand).FT METAL 81 81 Iron (heme axial ligand).FT BINDING 15 15 Heme (covalent).FT BINDING 18 18 Heme (covalent).FT MOD_RES 2 2 N-acetylglycine.FT MOD_RES 49 49 Phosphotyrosine.FT MOD_RES 98 98 Phosphotyrosine.FT HELIX 4 14FT TURN 15 18FT HELIX 51 55FT HELIX 62 68FT HELIX 72 75FT HELIX 89 102SQ SEQUENCE 105 AA; 11704 MW; AF0CA628EDF40483 CRC64; MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW GEETLMEYLE NPKKYIPGTK MIFAGIKKKG EREDLIAYLK KATNE
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