CYC_PANTR
ID CYC_PANTR Reviewed; 105 AA.
AC P99998; P00001; Q96BV4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome c;
GN Name=CYCS; Synonyms=CYC;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12766228; DOI=10.1073/pnas.1232172100;
RA Wildman D.E., Uddin M., Liu G., Grossman L.I., Goodman M.;
RT "Implications of natural selection in shaping 99.4% nonsynonymous DNA
RT identity between humans and chimpanzees: enlarging genus Homo.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7181-7188(2003).
RN [2]
RP PROTEIN SEQUENCE OF 2-105.
RX PubMed=4975694; DOI=10.1111/j.1749-6632.1968.tb11901.x;
RA Margoliash E., Fitch W.M.;
RT "Evolutionary variability of cytochrome c primary structures.";
RL Ann. N. Y. Acad. Sci. 151:359-381(1968).
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 (By
CC similarity). {ECO:0000250}.
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; AY268594; AAP49489.1; -; Genomic_DNA.
DR PIR; A00002; CCCZ.
DR RefSeq; NP_001065289.1; NM_001071821.1.
DR RefSeq; XP_001140708.1; XM_001140708.5.
DR RefSeq; XP_009450812.1; XM_009452537.2.
DR RefSeq; XP_016802858.1; XM_016947369.1.
DR RefSeq; XP_016812394.1; XM_016956905.1.
DR AlphaFoldDB; P99998; -.
DR BMRB; P99998; -.
DR SMR; P99998; -.
DR MINT; P99998; -.
DR STRING; 9598.ENSPTRP00000032465; -.
DR PaxDb; P99998; -.
DR Ensembl; ENSPTRT00000035122; ENSPTRP00000032465; ENSPTRG00000018996.
DR Ensembl; ENSPTRT00000077588; ENSPTRP00000063547; ENSPTRG00000043922.
DR GeneID; 744779; -.
DR KEGG; ptr:744779; -.
DR CTD; 54205; -.
DR VGNC; VGNC:14767; CYCS.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00390000009405; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; P99998; -.
DR OMA; AQCHTIN; -.
DR OrthoDB; 1533604at2759; -.
DR TreeFam; TF300226; -.
DR Proteomes; UP000002277; Chromosome 7.
DR Bgee; ENSPTRG00000018996; Expressed in heart and 21 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:4975694"
FT CHAIN 2..105
FT /note="Cytochrome c"
FT /id="PRO_0000108227"
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; 11749 MW; 8EE9689E0102506B CRC64;
MGDVEKGKKI FIMKCSQCHT VEKGGKHKTG PNLHGLFGRK TGQAPGYSYT AANKNKGIIW
GEDTLMEYLE NPKKYIPGTK MIFVGIKKKE ERADLIAYLK KATNE
