(data stored in ACNUC9552 zone)

HOGENOM: RAT3_PE2164

ID   RAT3_PE2164                          STANDARD;      PRT;   233 AA.
AC   RAT3_PE2164;
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=Bcl-2-like protein 1; Short=Bcl2-L-1;AltName:
DE   Full=Apoptosis regulator Bcl-X; (RAT3.PE2164).
GN   Name=Bcl2l1; Synonyms=Bclx, Blc2l;
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 RAT3.PE2164.
CC       Rattus norvegicus chromosome 3 RGSC3.4  sequence 1..171063335 annotated
CC       by Ensembl
CC   -!- ANNOTATIONS ORIGIN:B2CL1_RAT
CC   -!- FUNCTION: Potent inhibitor of cell death. Inhibits activation of
CC       caspases (By similarity). Appears to regulate cell death by
CC       blocking the voltage-dependent anion channnel (VDAC) by binding to
CC       it and preventing the release of the caspase activator, CYC1, from
CC       the mitochondrial membrane.
CC   -!- SUBUNIT: Homodimer (By similarity). Isoform Bcl-X(L) forms
CC       heterodimers with BAX, BAK or BCL2. Heterodimerization with BAX
CC       does not seem to be required for anti-apoptotic activity.
CC       Interacts with BAD and BBC3. Interacts (isoform Bcl-X(L)) with
CC       SIVA1 (isoform 1); the interaction inhibits the anti-apoptotic
CC       activity. Interacts with BECN1 and PGAM5. Interacts (isoform Bcl-
CC       X(L)) with BAX (isoform Sigma). Interacts with BCL2L11 (By
CC       similarity). Interacts with DMN1L; the interaction stimulates the
CC       GTPase activity of DMN1L in synapses and increases the number of
CC       axonal mitochondria and the size and number of synaptic vesicle
CC       clusters. Isoform Bcl-X(L) interacts with IKZF3 (By similarity).
CC   -!- INTERACTION:
CC       O35303:Dnm1l; NbExp=2; IntAct=EBI-287204, EBI-1767447;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein (By similarity). Nucleus membrane; Single-pass membrane
CC       protein; Cytoplasmic side (By similarity). Note=Mitochondrial
CC       membranes and perinuclear envelope (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Bcl-X(L);
CC         IsoId=P53563-1; Sequence=Displayed;
CC       Name=Bcl-X(S);
CC         IsoId=P53563-2; Sequence=VSP_000520;
CC       Name=Bcl-X(beta);
CC         IsoId=P53563-3; Sequence=VSP_000521;
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues. Bcl-X(beta) is
CC       specifically expressed in cerebellum, heart, and thymus. In the
CC       ovary, the predominant form is Bcl-X(L), with a small but
CC       detectable level of Bcl-X(S).
CC   -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity. The
CC       BH1 and BH2 motifs are required for both heterodimerization with
CC       other Bcl-2 family members and for repression of cell death.
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. The
CC       cleaved protein, lacking the BH4 motif, has pro-apoptotic activity
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC60701.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=AAC60702.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -!- GENE_FAMILY: HOG000056452 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Rattus_norvegicus;ENSRNOG00000007946;ENSRNOT00000010762;ENSRNOP00000010762.
DR   EMBL; AJ495801; - ;
DR   EMBL; BC094213; - ;
DR   EMBL; S76513; - ;
DR   EMBL; S78284; - ;
DR   EMBL; U10579; - ;
DR   EMBL; U34963; - ;
DR   EMBL; U72349; - ;
DR   EMBL; U72350; - ;
DR   EMBL; X82537; - ;
DR   UniProtKB/Swiss-Prot; P53563; P70613; P70614; Q52KS0; Q62678; Q62836; Q64087; Q64128; -.
DR   EMBL; X82537; CAA57886.1; -; Genomic_DNA.
DR   EMBL; X82537; CAA57887.1; -; Genomic_DNA.
DR   EMBL; U10579; AAA19257.1; -; Unassigned_DNA.
DR   EMBL; U72350; AAB17353.1; -; mRNA.
DR   EMBL; U72349; AAB17352.1; -; mRNA.
DR   EMBL; U34963; AAA77686.1; -; mRNA.
DR   EMBL; S76513; AAC60701.2; ALT_INIT; mRNA.
DR   EMBL; S78284; AAC60702.1; ALT_INIT; mRNA.
DR   EMBL; BC094213; AAH94213.1; -; mRNA.
DR   IPI; IPI00211135; -.
DR   IPI; IPI00231893; -.
DR   IPI; IPI00231894; -.
DR   PIR; I67431; I67431.
DR   PIR; I67435; I67435.
DR   PIR; S51761; S51761.
DR   RefSeq; NP_001028842.1; NM_001033670.1.
DR   RefSeq; NP_001028843.1; NM_001033671.1.
DR   RefSeq; NP_113723.2; NM_031535.2.
DR   UniGene; Rn.10323; -.
DR   PDB; 1AF3; X-ray; 2.50 A; A=1-196.
DR   PDBsum; 1AF3; -.
DR   ProteinModelPortal; P53563; -.
DR   SMR; P53563; 1-210.
DR   DisProt; DP00449; -.
DR   DIP; DIP-29698N; -.
DR   IntAct; P53563; 6.
DR   STRING; P53563; -.
DR   PhosphoSite; P53563; -.
DR   PRIDE; P53563; -.
DR   Ensembl; ENSRNOT00000010762; ENSRNOP00000010762; ENSRNOG00000007946.
DR   GeneID; 24888; -.
DR   KEGG; rno:24888; -.
DR   UCSC; NM_001033670; rat.
DR   CTD; 598; -.
DR   RGD; 2200; Bcl2l1.
DR   eggNOG; maNOG14015; -.
DR   OMA; NGSPSWH; -.
DR   OrthoDB; EOG47PX6Z; -.
DR   NextBio; 604742; -.
DR   ArrayExpress; P53563; -.
DR   Genevestigator; P53563; -.
DR   GermOnline; ENSRNOG00000007946; Rattus norvegicus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000299; C:integral to membrane of membrane fraction; TAS:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051400; F:BH domain binding; IPI:RGD.
DR   GO; GO:0043027; F:caspase inhibitor activity; IDA:RGD.
DR   GO; GO:0070215; F:MDM2 binding; IPI:RGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:RGD.
DR   GO; GO:0006915; P:apoptosis; IEP:RGD.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0010243; P:response to organic nitrogen; IEP:RGD.
DR   GO; GO:0043434; P:response to peptide hormone stimulus; IEP:RGD.
DR   InterPro; IPR013279; Apop_reg_BclX.
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; PR01864; APOPREGBCLX.
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; RAT3.PE2164; -.
KW   ENSRNOG00000007946820036002503210000011;
KW   B2CL1_RAT; Q5K547_RAT; AJ495801; BC094213; S76513; S78284; U10579;
KW   U72349; U72350; X82537;
KW   3D-structure; Alternative splicing; Apoptosis; Complete proteome;
KW   Membrane; Mitochondrion; Nucleus; Reference proteome; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   233 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEPERETPSA INGNPSWHLA
     DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY
     QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP
     WIQENGGWDT FVDLYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
//

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