CYC2_RAT
ID CYC2_RAT Reviewed; 105 AA.
AC P10715;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cytochrome c, testis-specific;
GN Name=Cyct;
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 / 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).
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: This is one of two isocytochromes C found in the
CC testis. The other is identical with the form found in other rat
CC tissues. These cytochromes are assumed to be located in the sperm.
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; M20623; AAA41016.1; -; mRNA.
DR EMBL; M20628; AAA41015.1; -; Genomic_DNA.
DR EMBL; M20627; AAA41015.1; JOINED; Genomic_DNA.
DR PIR; A28160; CCRTT.
DR RefSeq; NP_036972.1; NM_012840.3.
DR AlphaFoldDB; P10715; -.
DR SMR; P10715; -.
DR iPTMnet; P10715; -.
DR PhosphoSitePlus; P10715; -.
DR PRIDE; P10715; -.
DR Ensembl; ENSRNOT00000008371; ENSRNOP00000008371; ENSRNOG00000024457.
DR GeneID; 25310; -.
DR KEGG; rno:25310; -.
DR UCSC; RGD:2452; rat.
DR CTD; 13067; -.
DR RGD; 2452; Cyct.
DR GeneTree; ENSGT00940000162151; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR OrthoDB; 1533604at2759; -.
DR PRO; PR:P10715; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000024457; Expressed in testis and 8 other tissues.
DR ExpressionAtlas; P10715; baseline and differential.
DR Genevisible; P10715; RN.
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; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; ISO:RGD.
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 GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO: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 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Electron transport; Heme; Iron; Metal-binding;
KW Mitochondrion; Phosphoprotein; Reference proteome; Respiratory chain;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00015"
FT CHAIN 2..105
FT /note="Cytochrome c, testis-specific"
FT /id="PRO_0000108232"
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:P00015"
SQ SEQUENCE 105 AA; 11743 MW; 840BF657FBDD9E8C CRC64;
MGDAEAGKKI FIQKCAQCHT VEKGGKHKTG PNLWGLFGRK TGQAPGFSYT DANKNKGVIW
TEETLMEYLE NPKKYIPGTK MIFAGIKKKS EREDLIQYLK EATSS
