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CYC_CANLF
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   03-AUG-2022, entry version 156.
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; 9612.ENSCAFP00000004225; -.
DR   iPTMnet; P00011; -.
DR   PaxDb; P00011; -.
DR   Ensembl; ENSCAFT00000097490; ENSCAFP00000071485; ENSCAFG00000057599.
DR   Ensembl; ENSCAFT00030009189; ENSCAFP00030008057; ENSCAFG00030004991.
DR   Ensembl; ENSCAFT00040015592; ENSCAFP00040013514; ENSCAFG00040008341.
DR   Ensembl; ENSCAFT00845018890; ENSCAFP00845014758; ENSCAFG00845010713.
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; AQCHTIN; -.
DR   OrthoDB; 1533604at2759; -.
DR   TreeFam; TF300226; -.
DR   Reactome; R-CFA-111457; Release of apoptotic factors from the mitochondria.
DR   Reactome; R-CFA-2151201; Transcriptional activation of mitochondrial biogenesis.
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-9707564; Cytoprotection by HMOX1.
DR   Proteomes; UP000002254; Chromosome 14.
DR   Bgee; ENSCAFG00000002856; Expressed in cardiac muscle of left ventricle and 48 other 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:0097202; P:activation of cysteine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; IEA:Ensembl.
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   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.10.760.10; -; 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; PTHR11961; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; SSF46626; 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
 
 
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