ID CYC_CANLF Reviewed; 105 AA.
AC P00011;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Cytochrome c;
GN Name=CYCS; Synonyms=CYC;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
RX PubMed=5846985; DOI=10.1016/s0021-9258(18)97002-x;
RA McDowall M.A., Smith E.L.;
RT "Amino acid sequence of dog heart cytochrome c.";
RL J. Biol. Chem. 240:4635-4647(1965).
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 -!- 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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Note=Loosely
CC associated with the inner membrane.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- PTM: Phosphorylation at Tyr-49 and Tyr-98 both reduce by half the
CC turnover in the reaction with cytochrome c oxidase, down-regulating
CC mitochondrial respiration. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome c family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76 of
CC November 2006;
CC URL="https://web.expasy.org/spotlight/back_issues/076";
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DR PIR; A00010; CCDG.
DR RefSeq; NP_001183974.1; NM_001197045.1.
DR AlphaFoldDB; P00011; -.
DR SMR; P00011; -.
DR STRING; 9615.ENSCAFP00000004225; -.
DR iPTMnet; P00011; -.
DR SwissPalm; P00011; -.
DR PaxDb; 9612-ENSCAFP00000004225; -.
DR Ensembl; ENSCAFT00000097490.1; ENSCAFP00000071485.1; ENSCAFG00000057599.1.
DR Ensembl; ENSCAFT00030009189.1; ENSCAFP00030008057.1; ENSCAFG00030004991.1.
DR Ensembl; ENSCAFT00040015592.1; ENSCAFP00040013514.1; ENSCAFG00040008341.1.
DR Ensembl; ENSCAFT00805019812; ENSCAFP00805015624; ENSCAFG00805010802.
DR Ensembl; ENSCAFT00845018890.1; ENSCAFP00845014758.1; ENSCAFG00845010713.1.
DR GeneID; 475258; -.
DR KEGG; cfa:475258; -.
DR CTD; 54205; -.
DR VEuPathDB; HostDB:ENSCAFG00845010713; -.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00390000009405; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; P00011; -.
DR OMA; WGCPASE; -.
DR OrthoDB; 4150at2759; -.
DR TreeFam; TF300226; -.
DR Reactome; R-CFA-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-CFA-111458; Formation of apoptosome.
DR Reactome; R-CFA-111459; Activation of caspases through apoptosome-mediated cleavage.
DR Reactome; R-CFA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-CFA-5620971; Pyroptosis.
DR Reactome; R-CFA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-CFA-611105; Respiratory electron transport.
DR Reactome; R-CFA-9627069; Regulation of the apoptosome activity.
DR Reactome; R-CFA-9707564; Cytoprotection by HMOX1.
DR Proteomes; UP000002254; Chromosome 14.
DR Proteomes; UP000694429; Chromosome 14.
DR Proteomes; UP000694542; Chromosome 14.
DR Proteomes; UP000805418; Chromosome 14.
DR Bgee; ENSCAFG00000002856; Expressed in cardiac muscle of left ventricle and 48 other cell types or tissues.
DR GO; GO:0043293; C:apoptosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
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 GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW Reference proteome; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5846985"
FT CHAIN 2..105
FT /note="Cytochrome c"
FT /id="PRO_0000108211"
FT BINDING 15
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 18
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 19
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 81
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000269|PubMed:5846985"
FT MOD_RES 49
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62894"
FT MOD_RES 56
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62897"
FT MOD_RES 73
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62897"
FT MOD_RES 73
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62897"
FT MOD_RES 98
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P62894"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62897"
SQ SEQUENCE 105 AA; 11633 MW; B9670628E8E00483 CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW
GEETLMEYLE NPKKYIPGTK MIFAGIKKTG ERADLIAYLK KATKE
//
