CYC_RAT
ID CYC_RAT Reviewed; 105 AA.
AC P62898; P00009; Q8C2S2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cytochrome c, somatic;
GN Name=Cycs;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6263917; DOI=10.1016/s0021-9258(19)69190-8;
RA Scarpulla R.C., Agne K.M., Wu R.;
RT "Isolation and structure of a rat cytochrome c gene.";
RL J. Biol. Chem. 256:6480-6486(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6130852; DOI=10.1016/0092-8674(83)90467-1;
RA Scarpulla R.C., Wu R.;
RT "Nonallelic members of the cytochrome c multigene family of the rat may
RT arise through different messenger RNAs.";
RL Cell 32:473-482(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2834389; DOI=10.1016/s0021-9258(18)68712-5;
RA Virbasius J.V., Scarpulla R.C.;
RT "Structure and expression of rodent genes encoding the testis-specific
RT cytochrome c. Differences in gene structure and evolution between somatic
RT and testicular variants.";
RL J. Biol. Chem. 263:6791-6796(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
RX PubMed=191069; DOI=10.1021/bi00626a031;
RA Carlson S.S., Mross G.A., Wilson A.C., Mead R.T., Wolin L.D., Bowers S.F.,
RA Foley N.T., Muijsers A.O., Margoliash E.;
RT "Primary structure of mouse, rat, and guinea pig cytochrome c.";
RL Biochemistry 16:1437-1442(1977).
RN [6]
RP PROTEIN SEQUENCE OF 40-54; 57-73 AND 93-100, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
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 -!- TISSUE SPECIFICITY: Found in embryos and in adult liver and heart.
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; K00750; AAA21711.1; -; Genomic_DNA.
DR EMBL; M20622; AAA41014.1; -; mRNA.
DR EMBL; BC081849; AAH81849.1; -; mRNA.
DR EMBL; BC089051; AAH89051.1; -; mRNA.
DR PIR; A04605; CCRT.
DR RefSeq; NP_036971.1; NM_012839.2.
DR RefSeq; XP_003751847.1; XM_003751799.4.
DR RefSeq; XP_003753106.1; XM_003753058.4.
DR PDB; 5C0Z; X-ray; 1.12 A; A/B/C/D=1-105.
DR PDB; 5C9M; X-ray; 1.36 A; A/B/C/D=1-105.
DR PDB; 5DF5; X-ray; 1.30 A; A/B/C/D=2-105.
DR PDB; 6N1O; X-ray; 1.55 A; A/B/C/D=2-105.
DR PDB; 7LJX; X-ray; 1.31 A; A/B=2-105.
DR PDBsum; 5C0Z; -.
DR PDBsum; 5C9M; -.
DR PDBsum; 5DF5; -.
DR PDBsum; 6N1O; -.
DR PDBsum; 7LJX; -.
DR AlphaFoldDB; P62898; -.
DR SMR; P62898; -.
DR BioGRID; 247348; 5.
DR MINT; P62898; -.
DR STRING; 10116.ENSRNOP00000014058; -.
DR CarbonylDB; P62898; -.
DR iPTMnet; P62898; -.
DR PhosphoSitePlus; P62898; -.
DR SwissPalm; P62898; -.
DR jPOST; P62898; -.
DR PaxDb; P62898; -.
DR PRIDE; P62898; -.
DR ABCD; P62898; 25 sequenced antibodies.
DR Ensembl; ENSRNOT00000014058; ENSRNOP00000014058; ENSRNOG00000010452.
DR Ensembl; ENSRNOT00000102631; ENSRNOP00000094836; ENSRNOG00000065095.
DR GeneID; 100363502; -.
DR GeneID; 25309; -.
DR KEGG; rno:100363502; -.
DR KEGG; rno:25309; -.
DR UCSC; RGD:2451; rat.
DR CTD; 54205; -.
DR RGD; 2451; Cycs.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00390000009405; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; P62898; -.
DR OMA; ARCKACH; -.
DR OrthoDB; 1533604at2759; -.
DR PhylomeDB; P62898; -.
DR TreeFam; TF300226; -.
DR Reactome; R-RNO-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-RNO-111458; Formation of apoptosome.
DR Reactome; R-RNO-111459; Activation of caspases through apoptosome-mediated cleavage.
DR Reactome; R-RNO-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-RNO-5620971; Pyroptosis.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-RNO-611105; Respiratory electron transport.
DR Reactome; R-RNO-9627069; Regulation of the apoptosome activity.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR PRO; PR:P62898; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000010452; Expressed in duodenum and 18 other tissues.
DR Genevisible; P62898; RN.
DR GO; GO:0043293; C:apoptosome; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; IDA:RGD.
DR GO; GO:0020037; F:heme binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IMP:RGD.
DR GO; GO:0034349; P:glial cell apoptotic process; IEP:RGD.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; ISO:RGD.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IMP:RGD.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IBA:GO_Central.
DR GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; IMP:RGD.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:RGD.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0043393; P:regulation of protein binding; ISO:RGD.
DR GO; GO:0034465; P:response to carbon monoxide; IEP:RGD.
DR GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IDA:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
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:191069"
FT CHAIN 2..105
FT /note="Cytochrome c, somatic"
FT /id="PRO_0000108231"
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:191069"
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"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:5C0Z"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:5C0Z"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:5C0Z"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:5C0Z"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:5C0Z"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:5C0Z"
SQ SEQUENCE 105 AA; 11605 MW; B5BCA779BCE40492 CRC64;
MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAAGFSYT DANKNKGITW
GEDTLMEYLE NPKKYIPGTK MIFAGIKKKG ERADLIAYLK KATNE
