ID A0A2Y9ITK7_ENHLU Unreviewed; 105 AA.
AC A0A2Y9ITK7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=LOW QUALITY PROTEIN: cytochrome c, testis-specific-like {ECO:0000313|RefSeq:XP_022351656.1};
GN Name=LOC111142635 {ECO:0000313|RefSeq:XP_022351656.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022351656.1};
RN [1] {ECO:0000313|RefSeq:XP_022351656.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022351656.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00002555, ECO:0000256|RuleBase:RU004427}.
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.
CC {ECO:0000256|ARBA:ARBA00025038}.
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 RefSeq; XP_022351656.1; XM_022495948.1.
DR STRING; 391180.A0A2Y9ITK7; -.
DR KEGG; elk:111142635; -.
DR OrthoDB; 4150at2759; -.
DR Proteomes; UP000248482; Unplaced.
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:SF6; CYTOCHROME C, TESTIS-SPECIFIC; 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 Apoptosis {ECO:0000256|ARBA:ARBA00022703};
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 Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW 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; 11637 MW; 8D0ECFB8BC77C70A CRC64;
MGDAEAGKKI FIQKCAQCHT VEKGGKHKIG PNLWGLFGXK TGQAPGFSYS DANKNKGVIW
GEETLMEYLE NPKKYIPGTK MVFAGLKKKS EREDLIQYLK QATSS
//
