 MASCOT Search Results
Protein View: CYC_BOVIN
Cytochrome c OS=Bos taurus GN=CYCS PE=1 SV=2
AC P62894; P00006; Q2KJD4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 05-SEP-2012, entry version 80.
DE RecName: Full=Cytochrome c;
GN Name=CYCS; Synonyms=CYC;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC Pecora; Bovidae; 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 MEDLINE=66132521; PubMed=5933874;
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
RP 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
CC cytochrome c heme group can accept an electron from the heme group
CC of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC then transfers this electron to the cytochrome oxidase complex,
CC the final protein carrier in the mitochondrial electron-transport
CC chain.
CC -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC apoptotic members or activation of the pro-apoptotic members of
CC the Bcl-2 family leads to altered mitochondrial membrane
CC permeability resulting in release of cytochrome c into the
CC cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC of caspase-9, which then accelerates apoptosis by activating other
CC caspases (By similarity).
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC Note=Loosely associated with the inner membrane.
CC -!- PTM: Binds 1 heme group 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-
CC regulating mitochondrial respiration.
CC -!- SIMILARITY: Belongs to the cytochrome c family.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC of November 2006;
CC URL="http://web./spotlight/back_issues/sptlt076.shtml";
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DR EMBL; BC105397; AAI05398.1; -; mRNA.
DR IPI; IPI00906486; -.
DR PIR; A92022; CCBO.
DR RefSeq; NP_001039526.1; NM_001046061.1.
DR RefSeq; XP_003582877.1; XM_003582829.1.
DR RefSeq; XP_003582879.1; XM_003582831.1.
DR RefSeq; XP_003586721.1; XM_003586673.1.
DR UniGene; Bt.23981; -.
DR PDB; 2B4Z; X-ray; 1.50 A; A=2-105.
DR PDB; 2YBB; EM; 19.00 A; Y=2-105.
DR PDBsum; 2B4Z; -.
DR PDBsum; 2YBB; -.
DR ProteinModelPortal; P62894; -.
DR SMR; P62894; 2-105.
DR DIP; DIP-58978N; -.
DR IntAct; P62894; 1.
DR STRING; P62894; -.
DR PRIDE; P62894; -.
DR Ensembl; ENSBTAT00000004594; ENSBTAP00000051780; ENSBTAG00000023823.
DR Ensembl; ENSBTAT00000007918; ENSBTAP00000007918; ENSBTAG00000022613.
DR GeneID; 100847700; -.
DR GeneID; 100850794; -.
DR GeneID; 510767; -.
DR KEGG; bta:100847700; -.
DR KEGG; bta:100850794; -.
DR KEGG; bta:510767; -.
DR CTD; 54205; -.
DR eggNOG; COG3474; -.
DR GeneTree; ENSGT00390000009405; -.
DR HOGENOM; HOG000009762; -.
DR HOVERGEN; HBG003023; -.
DR InParanoid; P62894; -.
DR KO; K08738; -.
DR OMA; IAYLKQY; -.
DR OrthoDB; EOG45DWQX; -.
DR EvolutionaryTrace; P62894; -.
DR NextBio; 20869605; -.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR InterPro; IPR002327; Cyt_c_1A/1B.
DR InterPro; IPR009056; Cyt_c_dom.
DR InterPro; IPR003088; Cyt_c_I.
DR PANTHER; PTHR11961; Cyt_CIAB; 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; Complete proteome;
KW Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Mitochondrion; Phosphoprotein; Reference proteome;
KW Respiratory chain; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 105 Cytochrome c.
FT /FTId=PRO_0000108209.
FT METAL 19 19 Iron (heme axial ligand).
FT METAL 81 81 Iron (heme axial ligand).
FT BINDING 15 15 Heme (covalent).
FT BINDING 18 18 Heme (covalent).
FT MOD_RES 2 2 N-acetylglycine.
FT MOD_RES 49 49 Phosphotyrosine.
FT MOD_RES 98 98 Phosphotyrosine.
FT HELIX 4 14
FT TURN 15 18
FT HELIX 51 55
FT HELIX 62 68
FT HELIX 72 75
FT HELIX 89 102
SQ SEQUENCE 105 AA; 11704 MW; AF0CA628EDF40483 CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW
GEETLMEYLE NPKKYIPGTK MIFAGIKKKG EREDLIAYLK KATNE
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