(data stored in ACNUC9552 zone)

HOGENOM: RAT13_PE27

ID   RAT13_PE27                           STANDARD;      PRT;   236 AA.
AC   RAT13_PE27; P49950; Q62837; Q64032;
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=Apoptosis regulator Bcl-2; (RAT13.PE27).
GN   Name=Bcl2; Synonyms=Bcl-2;
OS   RATTUS NORVEGICUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT13.PE27.
CC       Rattus norvegicus chromosome 13 RGSC3.4  sequence 1..111154910
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:BCL2_RAT
CC   -!- FUNCTION: Suppresses apoptosis in a variety of cell systems
CC       including factor-dependent lymphohematopoietic and neural cells.
CC       Regulates cell death by controlling the mitochondrial membrane
CC       permeability. Appears to function in a feedback loop system with
CC       caspases. Inhibits caspase activity either by preventing the
CC       release of cytochrome c from the mitochondria and/or by binding to
CC       the apoptosis-activating factor (APAF-1).
CC   -!- SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and
CC       Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2
CC       motifs, and is necessary for anti-apoptotic activity. Also
CC       interacts with APAF1, BBC3, BCL2L1, BNIPL, EI24, FKBP8, MRPL41,
CC       RAF-1, TP53BP2. Interacts with BAG1 in an ATP-dependent manner (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein. Nucleus membrane; Single-pass membrane protein.
CC       Endoplasmic reticulum membrane; Single-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in a variety of tissues, with
CC       highest levels in reproductive tissues. In the adult brain,
CC       expression is localized in mitral cells of the olfactory bulb,
CC       granule and pyramidal neurons of hippocampus, pontine nuclei,
CC       cerebellar granule neurons, and in ependymal cells. In prenatal
CC       brain, expression is higher and localized in the neuroepithelium
CC       and in the cortical plate.
CC   -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity and
CC       for interaction with RAF-1 (By similarity).
CC   -!- PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-
CC       apoptotic activity. Growth factor-stimulated phosphorylation on
CC       Ser-70 by PKC is required for the anti-apoptosis activity and
CC       occurs during the G2/M phase of the cell cycle. In the absence of
CC       growth factors, BCL2 appears to be phosphorylated by other protein
CC       kinases such as ERKs and stress-activated kinases.
CC       Dephosphorylated by protein phosphatase 2A (PP2A) (By similarity).
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. The
CC       cleaved protein, lacking the BH4 motif, has pro-apoptotic
CC       activity, causes the release of cytochrome c into the cytosol
CC       promoting further caspase activity (By similarity).
CC   -!- PTM: Monoubiquitinated by PARK2, leading to increase its stability
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -!- GENE_FAMILY: HOG000056452 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000002791;ENSRNOT00000003768;ENSRNOP00000003768.
DR   EMBL; AF512835; - ;
DR   EMBL; L14680; - ;
DR   EMBL; S74122; - ;
DR   EMBL; U34964; - ;
DR   UniProtKB/Swiss-Prot; P49950; Q62837; Q64032; -.
DR   EMBL; L14680; AAA53662.1; -; mRNA.
DR   EMBL; U34964; AAA77687.1; -; mRNA.
DR   EMBL; S74122; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00325212; -.
DR   PIR; I53744; I53744.
DR   PIR; I67432; I67432.
DR   RefSeq; NP_058689.1; NM_016993.1.
DR   UniGene; Rn.9996; -.
DR   ProteinModelPortal; P49950; -.
DR   SMR; P49950; 3-204.
DR   DIP; DIP-30849N; -.
DR   IntAct; P49950; 5.
DR   STRING; P49950; -.
DR   PhosphoSite; P49950; -.
DR   GeneID; 24224; -.
DR   KEGG; rno:24224; -.
DR   UCSC; NM_016993; rat.
DR   CTD; 596; -.
DR   RGD; 2199; Bcl2.
DR   eggNOG; roNOG04876; -.
DR   InParanoid; P49950; -.
DR   OrthoDB; EOG4X97J4; -.
DR   NextBio; 602665; -.
DR   ArrayExpress; P49950; -.
DR   Genevestigator; P49950; -.
DR   GermOnline; ENSRNOG00000002791; Rattus norvegicus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:RGD.
DR   GO; GO:0034349; P:glial cell apoptosis; IEP:RGD.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
DR   GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:HGNC.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:HGNC.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:HGNC.
DR   GO; GO:0010044; P:response to aluminum ion; IEP:RGD.
DR   GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR   GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR   GO; GO:0051412; P:response to corticosterone stimulus; IEP:RGD.
DR   GO; GO:0034097; P:response to cytokine stimulus; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0043627; P:response to estrogen stimulus; IEP:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0051593; P:response to folic acid; IEP:RGD.
DR   GO; GO:0009408; P:response to heat; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0032868; P:response to insulin stimulus; IEP:RGD.
DR   GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
DR   GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR   InterPro; IPR013278; Apop_reg_Bcl2.
DR   InterPro; IPR002475; Bcl2-like_apoptosis.
DR   InterPro; IPR000712; Bcl2_BH.
DR   InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR   InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR   InterPro; IPR020728; Bcl2_BH3_motif_CS.
DR   InterPro; IPR003093; Bcl2_BH4.
DR   InterPro; IPR020731; Bcl2_BH4_motif_CS.
DR   InterPro; IPR004725; Bcl2_reg.
DR   Pfam; PF00452; Bcl-2; 1.
DR   Pfam; PF02180; BH4; 1.
DR   PRINTS; PR01863; APOPREGBCL2.
DR   PRINTS; PR01862; BCL2FAMILY.
DR   SMART; SM00337; BCL; 1.
DR   SMART; SM00265; BH4; 1.
DR   TIGRFAMs; TIGR00865; Bcl-2; 1.
DR   PROSITE; PS50062; BCL2_FAMILY; 1.
DR   PROSITE; PS01080; BH1; 1.
DR   PROSITE; PS01258; BH2; 1.
DR   PROSITE; PS01259; BH3; 1.
DR   PROSITE; PS01260; BH4_1; 1.
DR   PROSITE; PS50063; BH4_2; 1.
DR   HOGENOMDNA; RAT13.PE27; -.
KW   ENSRNOG00000002791820036002503210000011;
KW   Bcl2; BCL2_RAT; Q7TSN8_RAT; AF512835; L14680; S74122; U34964;
KW   Apoptosis; Complete proteome; Endoplasmic reticulum; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
SQ   SEQUENCE   236 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAQAGRTGYD NREIVMKYIH YKLSQRGYEW DTGDEDSAPL RAAPTPGIFS FQPESNRTPA
     VHRDTAARTS PLRPLVATAG PALSPVPPVV HLTLRRAGDD FSRRYRRDFA EMSSQLHLTP
     FTARGRFATV VEELFRDGVN WGRIVAFFEF GGVMCVESVN REMSPLVDNI ALWMTEYLNR
     HLHTWIQDNG GWDAFVELYG PSMRPLFDFS WLSLKTLLSL ALVGACITLG AYLGHK
//

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