ID G3VSB9_SARHA Unreviewed; 104 AA.
AC G3VSB9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Cytochrome c domain-containing protein {ECO:0000259|PROSITE:PS51007};
GN Name=LOC100919671 {ECO:0000313|Ensembl:ENSSHAP00000006074.1};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000006074.1, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000006074.1, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000006074.1}
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 RefSeq; XP_003764050.1; XM_003764002.1.
DR RefSeq; XP_003764051.1; XM_003764003.2.
DR RefSeq; XP_012400310.1; XM_012544856.1.
DR RefSeq; XP_012400311.1; XM_012544857.1.
DR AlphaFoldDB; G3VSB9; -.
DR STRING; 9305.ENSSHAP00000006074; -.
DR Ensembl; ENSSHAT00000006128.2; ENSSHAP00000006074.1; ENSSHAG00000005285.2.
DR GeneID; 100919671; -.
DR KEGG; shr:100919671; -.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00940000157883; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; G3VSB9; -.
DR OMA; ARCKACH; -.
DR OrthoDB; 4150at2759; -.
DR TreeFam; TF300226; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
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:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IEA:Ensembl.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
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 Reference proteome {ECO:0000313|Proteomes:UP000007648};
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 104 AA; 12015 MW; 8241F50E9E70CF1F CRC64;
MEDVEEGRKI FVQKCAQCHT VEKNGKHKTG PNLWGLFGRR TGQASGYSYS EANKNKGIIW
NETNLVEYLE NPKKFIPGTK MIFPGIRKRR EREALVAYLK RVTK
//
