CYC_PIG
ID CYC_PIG Reviewed; 105 AA.
AC P62895; P00006; Q56P24;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cytochrome c;
GN Name=CYCS; Synonyms=CYC;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu G.Y., Xiong Z.Y.;
RT "Isolation and prediction of one novel swine gene that is differentially
RT expressed in the longissimus dorsi muscle tissues from Landrace Large White
RT cross combination.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-105.
RX PubMed=5855656; DOI=10.1139/o65-131;
RA Stewart J.W., Margoliash E.;
RT "The primary structure of the cytochrome c from various organs of the
RT hog.";
RL Can. J. Biochem. 43:1187-1206(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 EMBL; AY864613; AAX77008.1; -; mRNA.
DR PIR; A00007; CCPG.
DR RefSeq; NP_001123442.1; NM_001129970.1.
DR AlphaFoldDB; P62895; -.
DR BMRB; P62895; -.
DR SMR; P62895; -.
DR STRING; 9823.ENSSSCP00000017704; -.
DR iPTMnet; P62895; -.
DR PaxDb; P62895; -.
DR PeptideAtlas; P62895; -.
DR PRIDE; P62895; -.
DR Ensembl; ENSSSCT00000018195; ENSSSCP00000017704; ENSSSCG00000016714.
DR Ensembl; ENSSSCT00005061435; ENSSSCP00005037986; ENSSSCG00005038422.
DR Ensembl; ENSSSCT00005061457; ENSSSCP00005037996; ENSSSCG00005038422.
DR Ensembl; ENSSSCT00005061462; ENSSSCP00005038000; ENSSSCG00005038422.
DR Ensembl; ENSSSCT00015077795; ENSSSCP00015031338; ENSSSCG00015058229.
DR Ensembl; ENSSSCT00025016702; ENSSSCP00025006661; ENSSSCG00025012632.
DR Ensembl; ENSSSCT00030003474; ENSSSCP00030001365; ENSSSCG00030002705.
DR Ensembl; ENSSSCT00035099861; ENSSSCP00035042328; ENSSSCG00035073660.
DR Ensembl; ENSSSCT00040010932; ENSSSCP00040004216; ENSSSCG00040008367.
DR Ensembl; ENSSSCT00045028997; ENSSSCP00045020076; ENSSSCG00045017039.
DR Ensembl; ENSSSCT00050065643; ENSSSCP00050028275; ENSSSCG00050048183.
DR Ensembl; ENSSSCT00055004346; ENSSSCP00055003333; ENSSSCG00055002302.
DR Ensembl; ENSSSCT00060046609; ENSSSCP00060019964; ENSSSCG00060034366.
DR Ensembl; ENSSSCT00065048025; ENSSSCP00065020701; ENSSSCG00065035264.
DR Ensembl; ENSSSCT00070027397; ENSSSCP00070022790; ENSSSCG00070014000.
DR GeneID; 100170131; -.
DR KEGG; ssc:100170131; -.
DR CTD; 54205; -.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00940000157883; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; P62895; -.
DR OMA; ARCKACH; -.
DR OrthoDB; 1533604at2759; -.
DR TreeFam; TF300226; -.
DR Reactome; R-SSC-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SSC-111458; Formation of apoptosome.
DR Reactome; R-SSC-111459; Activation of caspases through apoptosome-mediated cleavage.
DR Reactome; R-SSC-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-SSC-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-SSC-5620971; Pyroptosis.
DR Reactome; R-SSC-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SSC-611105; Respiratory electron transport.
DR Reactome; R-SSC-9627069; Regulation of the apoptosome activity.
DR Reactome; R-SSC-9707564; Cytoprotection by HMOX1.
DR Proteomes; UP000008227; Chromosome 18.
DR Proteomes; UP000314985; Chromosome 18.
DR Bgee; ENSSSCG00000016714; Expressed in heart left ventricle and 44 other tissues.
DR Genevisible; P62895; SS.
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 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:0000250|UniProtKB:P62894,
FT ECO:0000269|PubMed:5855656"
FT CHAIN 2..105
FT /note="Cytochrome c"
FT /id="PRO_0000108228"
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:0000250|UniProtKB:P62894"
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; 11704 MW; AF0CA628EDF40483 CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGFSYT DANKNKGITW
GEETLMEYLE NPKKYIPGTK MIFAGIKKKG EREDLIAYLK KATNE
