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   27-MAR-2024, entry version 156.
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";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   EMDB; EMD-5186; -.
DR   EMDB; EMD-8178; -.
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; 9913-ENSBTAP00000007918; -.
DR   PeptideAtlas; P62894; -.
DR   ABCD; P62894; 2 sequenced antibodies.
DR   Ensembl; ENSBTAT00000004594.2; ENSBTAP00000051780.1; ENSBTAG00000023823.2.
DR   Ensembl; ENSBTAT00000007918.3; ENSBTAP00000007918.2; ENSBTAG00000022613.4.
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; WGCPASE; -.
DR   OrthoDB; 4150at2759; -.
DR   TreeFam; TF300226; -.
DR   Reactome; R-BTA-111457; Release of apoptotic factors from the mitochondria.
DR   Reactome; R-BTA-111458; Formation of apoptosome.
DR   Reactome; R-BTA-111459; Activation of caspases through apoptosome-mediated cleavage.
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-9627069; Regulation of the apoptosome activity.
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 cell types or 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   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   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
//