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Database: UniProt
Entry: W5P4S3_SHEEP
LinkDB: W5P4S3_SHEEP
Original site: W5P4S3_SHEEP 
ID   W5P4S3_SHEEP            Unreviewed;       105 AA.
AC   W5P4S3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Cytochrome c domain-containing protein {ECO:0000259|PROSITE:PS51007};
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 {ECO:0000313|Ensembl:ENSOARP00000005426.1, ECO:0000313|Proteomes:UP000002356};
RN   [1] {ECO:0000313|Ensembl:ENSOARP00000005426.1, ECO:0000313|Proteomes:UP000002356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000005426.1,
RC   ECO:0000313|Proteomes:UP000002356};
RX   PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA   Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA   Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA   Wang W., Xun X.;
RT   "The sheep genome reference sequence: a work in progress.";
RL   Anim. Genet. 41:449-453(2010).
RN   [2] {ECO:0000313|Ensembl:ENSOARP00000005426.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; AMGL01021051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5P4S3; -.
DR   SMR; W5P4S3; -.
DR   STRING; 9940.ENSOARP00000005426; -.
DR   PaxDb; 9940-ENSOARP00000005426; -.
DR   Ensembl; ENSOART00000005513.1; ENSOARP00000005426.1; ENSOARG00000005063.1.
DR   eggNOG; KOG3453; Eukaryota.
DR   HOGENOM; CLU_060944_3_0_1; -.
DR   OMA; SQCHTVT; -.
DR   Proteomes; UP000002356; Chromosome 12.
DR   Bgee; ENSOARG00000005063; Expressed in leukocyte and 6 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   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
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   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002356};
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;  11647 MW;  DB4755E5603D2036 CRC64;
     VGDTEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAAGFSYT DANKNKGITW
     GEETLMEYLE NPKKYIPGTK MIFAGIKKKG EREDLIAYLK KATNE
//
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