ID O96572_TIGCA Unreviewed; 105 AA.
AC O96572;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Cytochrome c {ECO:0000313|EMBL:AAC80535.1};
GN Name=CYC {ECO:0000313|EMBL:AAC80535.1};
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:AAC80535.1};
RN [1] {ECO:0000313|EMBL:AAC80535.1}
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}.
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DR EMBL; AF091467; AAC80535.1; -; Genomic_DNA.
DR AlphaFoldDB; O96572; -.
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:SF12; CYTOCHROME C; 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; 11469 MW; 511B6AC099CE7A9B CRC64;
MGDIDKGKKI FVQKCTQCHT IEAGGKHKVG PNLHGMYGRQ TGQAAGFNYT DANKSKGVTW
NEETLDIYLT NPKKYIPGTK MVFAGLKKKG DREGLIAYLK SASSS
//