ID CYC2_BOVIN Reviewed; 105 AA.
AC Q3SZT9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 123.
DE RecName: Full=Cytochrome c 2;
GN Name=CYCT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC Note=Loosely associated with the inner membrane. {ECO:0000250}.
CC -!- PTM: Binds 1 heme c group covalently per subunit. {ECO:0000250}.
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; BC102714; AAI02715.1; -; mRNA.
DR RefSeq; NP_001071431.1; NM_001077963.2.
DR AlphaFoldDB; Q3SZT9; -.
DR SMR; Q3SZT9; -.
DR STRING; 9913.ENSBTAP00000031831; -.
DR PaxDb; 9913-ENSBTAP00000031831; -.
DR Ensembl; ENSBTAT00000031885.3; ENSBTAP00000031831.2; ENSBTAG00000039522.2.
DR GeneID; 781996; -.
DR KEGG; bta:781996; -.
DR CTD; 13067; -.
DR VEuPathDB; HostDB:ENSBTAG00000039522; -.
DR VGNC; VGNC:108924; CYCT.
DR eggNOG; KOG3453; Eukaryota.
DR GeneTree; ENSGT00940000157883; -.
DR HOGENOM; CLU_060944_3_0_1; -.
DR InParanoid; Q3SZT9; -.
DR OMA; NKGVIWG; -.
DR OrthoDB; 4150at2759; -.
DR TreeFam; TF300226; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000039522; Expressed in semen and 31 other cell types or tissues.
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:Ensembl.
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; IEA:Ensembl.
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:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 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; CYTOCHROME C; 1.
DR PANTHER; PTHR11961:SF6; CYTOCHROME C, TESTIS-SPECIFIC; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR PRINTS; PR00604; CYTCHRMECIAB.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 3: Inferred from homology;
KW Apoptosis; Electron transport; Heme; Iron; Metal-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Respiratory chain; Transport.
FT CHAIN 1..105
FT /note="Cytochrome c 2"
FT /id="PRO_0000266018"
FT BINDING 15
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 18
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ SEQUENCE 105 AA; 11740 MW; 9E5AA14E7AAE7F39 CRC64;
MADAEAGKKI FIQKCAQCHT VEKGGKHKTG PNLWGLFGRK TGQAPGFSYT EANKNKGIIW
GEQTLMEYLE NPKKYIPGTK MIFAGLKKKS EREDLIEYLK QATSS
//
