ID CYC_SHEEP Reviewed; 105 AA. AC P62896; P00006; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 111. DE RecName: Full=Cytochrome c; GN Name=CYCS; Synonyms=CYC; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP AMINO-ACID COMPOSITION, AND MOBILITIES OF TRYPTIC AND CHYMOTRYPTIC RP PEPTIDES. RX PubMed=14236132; RA Smith E.L., Margoliash E.; RT "Evolution of cytochrome c."; RL Fed. Proc. 23:1243-1247(1964). CC -!- FUNCTION: Electron carrier protein. The oxidized form of the cytochrome CC c heme group can accept an electron from the heme group of the CC cytochrome c1 subunit of cytochrome reductase. Cytochrome c then CC transfers this electron to the cytochrome oxidase complex, the final CC protein carrier in the mitochondrial electron-transport chain. CC -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-apoptotic CC members or activation of the pro-apoptotic members of the Bcl-2 family CC leads to altered mitochondrial membrane permeability resulting in CC release of cytochrome c into the cytosol. Binding of cytochrome c to CC Apaf-1 triggers the activation of caspase-9, which then accelerates CC apoptosis by activating other caspases (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely CC associated with the inner membrane. CC -!- PTM: Binds 1 heme c group covalently per subunit. CC -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the CC turnover in the reaction with cytochrome c oxidase, down-regulating CC mitochondrial respiration. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of CC November 2006; CC URL="https://web.expasy.org/spotlight/back_issues/076"; 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 PIR; A91454; CCSH. DR RefSeq; XP_004007999.1; XM_004007950.2. DR AlphaFoldDB; P62896; -. DR BMRB; P62896; -. DR SMR; P62896; -. DR STRING; 9940.ENSOARP00000022795; -. DR PaxDb; 9940-ENSOARP00000022795; -. DR Ensembl; ENSOART00000027071.1; ENSOARP00000022795.1; ENSOARG00000025169.1. DR Ensembl; ENSOART00020000698; ENSOARP00020000550; ENSOARG00020000536. DR Ensembl; ENSOART00020021692; ENSOARP00020017966; ENSOARG00020014198. DR Ensembl; ENSOART00020034576; ENSOARP00020028552; ENSOARG00020022330. DR GeneID; 106990092; -. DR KEGG; oas:106990092; -. DR eggNOG; KOG3453; Eukaryota. DR HOGENOM; CLU_060944_3_0_1; -. DR OMA; WGCPASE; -. DR OrthoDB; 4150at2759; -. DR Proteomes; UP000002356; Chromosome 4. DR Bgee; ENSOARG00000025169; Expressed in longissimus thoracis muscle and 56 other cell types or tissues. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 1. DR InterPro; IPR009056; Cyt_c-like_dom. DR InterPro; IPR036909; Cyt_c-like_dom_sf. DR InterPro; IPR002327; Cyt_c_1A/1B. DR PANTHER; PTHR11961; CYTOCHROME C; 1. DR PANTHER; PTHR11961:SF15; CYTOCHROME C, SOMATIC; 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 Acetylation; Apoptosis; Electron transport; Heme; Iron; Metal-binding; KW Mitochondrion; Phosphoprotein; Reference proteome; Respiratory chain; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62894" FT CHAIN 2..105 FT /note="Cytochrome c" FT /id="PRO_0000108234" FT BINDING 15 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 18 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /note="covalent" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 19 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT BINDING 81 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433" FT MOD_RES 2 FT /note="N-acetylglycine" FT /evidence="ECO:0000250|UniProtKB:P62894" FT MOD_RES 49 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62894" FT MOD_RES 56 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P62897" FT MOD_RES 73 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62897" FT MOD_RES 73 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62897" FT MOD_RES 98 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P62894" FT MOD_RES 100 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62897" SQ SEQUENCE 105 AA; 11704 MW; AF0CA628EDF40483 CRC64; MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW GEETLMEYLE NPKKYIPGTK MIFAGIKKKG EREDLIAYLK KATNE //