(data stored in ACNUC11016 zone)

HOGENOM: RABIT10_11_PE3

ID   RABIT10_11_PE3                       STANDARD;      PRT;   105 AA.
AC   RABIT10_11_PE3; P00008;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Cytochrome c; (RABIT10_11.PE3).
GN   Name=CYCS; Synonyms=CYC;
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABIT10_11.PE3.
CC       Oryctolagus cuniculus chromosome 10 oryCun2 partial sequence
CC       9670117..10670116 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:CYC_RABIT
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- FUNCTION: Plays a role in apoptosis. Suppression of the anti-
CC       apoptotic members or activation of the pro-apoptotic members of
CC       the Bcl-2 family leads to altered mitochondrial membrane
CC       permeability resulting in release of cytochrome c into the
CC       cytosol. Binding of cytochrome c to Apaf-1 triggers the activation
CC       of caspase-9, which then accelerates apoptosis by activating other
CC       caspases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Binds 1 heme group 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-
CC       regulating mitochondrial respiration (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://web.expasy.org/spotlight/back_issues/sptlt076.shtml";
CC   -!- GENE_FAMILY: HOG000009762 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Oryctolagus_cuniculus;ENSOCUG00000025605;ENSOCUT00000028776;ENSOCUP00000019830.
DR   UniProtKB/Swiss-Prot; P00008; -.
DR   PIR; A00009; CCRB.
DR   ProteinModelPortal; P00008; -.
DR   SMR; P00008; 2-105.
DR   Ensembl; ENSOCUT00000023880; ENSOCUP00000019281; ENSOCUG00000028125.
DR   Ensembl; ENSOCUT00000026233; ENSOCUP00000022793; ENSOCUG00000027375.
DR   Ensembl; ENSOCUT00000028776; ENSOCUP00000019830; ENSOCUG00000025605.
DR   eggNOG; maNOG20053; -.
DR   GeneTree; ENSGT00390000009405; -.
DR   OrthoDB; EOG45DWQX; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0045155; F:electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochDR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   HOGENOMDNA; RABIT10_11.PE3; -.
KW   ENSOCUG00000025605820036002503210000011;
KW   CYC_RABIT;
KW   Acetylation; Apoptosis; Direct protein sequencing; Electron transport;
KW   Heme; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Respiratory chain; Transport.
SQ   SEQUENCE   105 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAVGFSYT DANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFAGIKKKN ERADLIAYLK KATNE
//

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