ID O96573_TIGCA Unreviewed; 105 AA. AC O96573; DT 01-MAY-1999, integrated into UniProtKB/TrEMBL. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 81. DE SubName: Full=Cytochrome c {ECO:0000313|EMBL:AAC80553.1}; GN Name=CYC {ECO:0000313|EMBL:AAC80553.1}; OS Tigriopus californicus (Marine copepod). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Hexanauplia; Copepoda; Harpacticoida; Harpacticidae; Tigriopus. OX NCBI_TaxID=6832 {ECO:0000313|EMBL:AAC80553.1}; RN [1] {ECO:0000313|EMBL:AAC80553.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=10806346; DOI=10.1016/S0378-1119(00)00145-1; RA Rawson P.D., Brazeau D.A., Burton R.S.; RT "Isolation and characterization of cytochrome c from the marine copepod RT Tigriopus californicus."; RL Gene 248:15-22(2000). 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 {ECO:0000256|RuleBase:RU004427}. CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space CC {ECO:0000256|ARBA:ARBA00004569}. CC -!- PTM: Binds 1 heme group per subunit. {ECO:0000256|RuleBase:RU004427}. CC -!- SIMILARITY: Belongs to the cytochrome c family. CC {ECO:0000256|ARBA:ARBA00006488, ECO:0000256|RuleBase:RU004426}. 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; AF091485; AAC80553.1; -; Genomic_DNA. DR AlphaFoldDB; O96573; -. 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 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:SF38; CYTOCHROME C ISO-1_ISO-2; 1. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR SUPFAM; SSF46626; Cytochrome c; 1. DR PROSITE; PS51007; CYTC; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU004427}; KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU00433}; Mitochondrion {ECO:0000256|RuleBase:RU004427}; KW Respiratory chain {ECO:0000256|RuleBase:RU004427}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU004427}. FT DOMAIN 2..103 FT /note="Cytochrome c" FT /evidence="ECO:0000259|PROSITE:PS51007" SQ SEQUENCE 105 AA; 11514 MW; 4407CD3D4B26CE2A CRC64; MGDIEKGKKI FVQKCTQCHT IEAGGKHKVG PNLHGMYGRQ TGKAAGYSYT DANKSKGVTW NEETLDIYLT NPKKYIPGTK MVFAGPKKKG DREDLIAYLK SASSS //