CYC_BOVIN
ID CYC_BOVIN Reviewed; 105 AA.
AC P62894; P00006; Q2KJD4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cytochrome c;
GN Name=CYCS; Synonyms=CYC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
RC TISSUE=Heart;
RX PubMed=5933874; DOI=10.1016/s0021-9258(18)96817-1;
RA Nakashima T., Higa H., Matsubara H., Benson A.M., Yasunobu K.T.;
RT "The amino acid sequence of bovine heart cytochrome c.";
RL J. Biol. Chem. 241:1166-1177(1966).
RN [3]
RP PHOSPHORYLATION AT TYR-49.
RC TISSUE=Heart;
RX PubMed=16866357; DOI=10.1021/bi060585v;
RA Lee I., Salomon A.R., Yu K., Doan J.W., Grossman L.I., Huttemann M.;
RT "New prospects for an old enzyme: mammalian cytochrome c is tyrosine-
RT phosphorylated in vivo.";
RL Biochemistry 45:9121-9128(2006).
RN [4]
RP PHOSPHORYLATION AT TYR-98.
RC TISSUE=Liver;
RX PubMed=18471988; DOI=10.1016/j.bbabio.2008.04.023;
RA Yu H., Lee I., Salomon A.R., Yu K., Huttemann M.;
RT "Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo,
RT inhibiting mitochondrial respiration.";
RL Biochim. Biophys. Acta 1777:1066-1071(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-105, AND HEME-BINDING SITES.
RX PubMed=17634981; DOI=10.1002/prot.21452;
RA Mirkin N., Jaconcic J., Stojanoff V., Moreno A.;
RT "High resolution X-ray crystallographic structure of bovine heart
RT cytochrome c and its application to the design of an electron transfer
RT biosensor.";
RL Proteins 70:83-92(2008).
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:0000269|PubMed:16866357,
CC ECO:0000269|PubMed:18471988}.
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 EMBL; BC105397; AAI05398.1; -; mRNA.
DR PIR; A92022; CCBO.
DR RefSeq; NP_001039526.1; NM_001046061.2.
DR RefSeq; XP_005194076.1; XM_005194019.3.
DR RefSeq; XP_010802623.1; XM_010804321.2.
DR RefSeq; XP_010808799.1; XM_010810497.2.
DR PDB; 2B4Z; X-ray; 1.50 A; A=2-105.
DR PDB; 2YBB; EM; 19.00 A; Y=2-105.
DR PDB; 3J2T; EM; 9.50 A; H/I/J/K/L/M/N=2-105.
DR PDB; 5JUY; EM; 4.10 A; H/I/J/K/L/M/N=2-105.
DR PDB; 6FF5; X-ray; 1.74 A; A=2-105.
DR PDBsum; 2B4Z; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 3J2T; -.
DR PDBsum; 5JUY; -.
DR PDBsum; 6FF5; -.
DR AlphaFoldDB; P62894; -.
DR BMRB; P62894; -.
DR SASBDB; P62894; -.
DR SMR; P62894; -.
DR BioGRID; 167399; 1.
DR DIP; DIP-58978N; -.
DR IntAct; P62894; 1.
DR STRING; 9913.ENSBTAP00000007918; -.
DR ChEMBL; CHEMBL3396942; -.
DR CarbonylDB; P62894; -.
DR iPTMnet; P62894; -.
DR PaxDb; P62894; -.
DR PeptideAtlas; P62894; -.
DR PRIDE; P62894; -.
DR ABCD; P62894; 1 sequenced antibody.
DR Ensembl; ENSBTAT00000004594; ENSBTAP00000051780; ENSBTAG00000023823.
DR Ensembl; ENSBTAT00000007918; ENSBTAP00000007918; ENSBTAG00000022613.
DR GeneID; 100847700; -.
DR GeneID; 510767; -.
DR KEGG; bta:100847700; -.
DR KEGG; bta:510767; -.
DR CTD; 54205; -.
DR VEuPathDB; HostDB:ENSBTAG00000022613; -.
DR VEuPathDB; HostDB:ENSBTAG00000023823; -.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00940000157883; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; P62894; -.
DR OMA; AQCHTIN; -.
DR OrthoDB; 1533604at2759; -.
DR TreeFam; TF300226; -.
DR Reactome; R-BTA-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-BTA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-BTA-5620971; Pyroptosis.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR EvolutionaryTrace; P62894; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000022613; Expressed in cardiac ventricle and 105 other tissues.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
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 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 3D-structure; Acetylation; Apoptosis; Direct protein sequencing;
KW Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:5933874"
FT CHAIN 2..105
FT /note="Cytochrome c"
FT /id="PRO_0000108209"
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:5933874"
FT MOD_RES 49
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:16866357"
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:0000269|PubMed:18471988"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62897"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:2B4Z"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:2B4Z"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:2B4Z"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:2B4Z"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:2B4Z"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:2B4Z"
SQ SEQUENCE 105 AA; 11704 MW; AF0CA628EDF40483 CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW
GEETLMEYLE NPKKYIPGTK MIFAGIKKKG EREDLIAYLK KATNE
