(data stored in ACNUC9552 zone)

HOGENOM: MOUSE2_PE3870

ID   MOUSE2_PE3870                        STANDARD;      PRT;   233 AA.
AC   MOUSE2_PE3870; Q64373; O35844; Q60657; Q60658; Q61338;
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; (MOUSE2.PE3870).
GN   Name=Bcl2l1; Synonyms=Bcl2l, Bclx;
OS   MUS MUSCULUS.
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; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE2.PE3870.
CC       Mus musculus chromosome 2 NCBIM37  sequence 1..181748087 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:B2CL1_MOUSE
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   -!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis (By similarity).
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 DMN1L; the interaction stimulates the GTPase
CC       activity of DMN1L in synapses and increases the number of axonal
CC       mitochondria and the size and number of synaptic vesicle clusters.
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) (By similarity). Interacts with
CC       BCL2L11. Isoform Bcl-X(L) interacts with IKZF3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform Bcl-X(L): Mitochondrion membrane.
CC       Note=Mitochondrial membranes and perinuclear envelope.
CC   -!- SUBCELLULAR LOCATION: Isoform Bcl-X(delta-TM): Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Bcl-X(L);
CC         IsoId=Q64373-1; Sequence=Displayed;
CC       Name=Bcl-X(S);
CC         IsoId=Q64373-2; Sequence=VSP_000517;
CC       Name=Bcl-X(beta);
CC         IsoId=Q64373-3; Sequence=VSP_000518;
CC       Name=Bcl-X(delta-TM);
CC         IsoId=Q64373-4; Sequence=VSP_000519;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in the
CC       brain, thymus, bone marrow, and kidney. Bcl-X(L) and Bcl-X(delta-
CC       TM) expression is enhanced in B- and T-lymphocytes that have been
CC       activated.
CC   -!- DEVELOPMENTAL STAGE: Bcl-X(beta) is expressed in both embryonal
CC       and postnatal tissues, whereas Bcl-X(L) is predominantly found in
CC       postnatal tissues.
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 (By
CC       similarity). The cleaved protein, lacking the BH4 motif, has pro-
CC       apoptotic activity (By similarity).
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -!- GENE_FAMILY: HOG000056452 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000007659;ENSMUST00000007803;ENSMUSP00000007803.
DR   EMBL; AF088904; - ;
DR   EMBL; AF133281; - ;
DR   EMBL; AF133282; - ;
DR   EMBL; AK146461; - ;
DR   EMBL; AK172250; - ;
DR   EMBL; AL731857; - ;
DR   EMBL; AY902314; - ;
DR   EMBL; BC089016; - ;
DR   EMBL; BC089017; - ;
DR   EMBL; CH466551; - ;
DR   EMBL; L35048; - ;
DR   EMBL; L35049; - ;
DR   EMBL; U10100; - ;
DR   EMBL; U10101; - ;
DR   EMBL; U10102; - ;
DR   EMBL; U51278; - ;
DR   EMBL; U51279; - ;
DR   EMBL; U78030; - ;
DR   EMBL; U78031; - ;
DR   EMBL; X83574; - ;
DR   UniProtKB/Swiss-Prot; Q64373; O35844; Q60657; Q60658; Q61338; -.
DR   EMBL; X83574; CAA58557.1; -; mRNA.
DR   EMBL; L35049; AAA51039.1; -; mRNA.
DR   EMBL; L35048; AAA51040.1; -; mRNA.
DR   EMBL; U10102; AAA82174.1; -; mRNA.
DR   EMBL; U10101; AAA82173.1; -; mRNA.
DR   EMBL; U10100; AAA82172.1; -; mRNA.
DR   EMBL; U51278; AAC53459.1; -; mRNA.
DR   EMBL; U51279; AAC53460.1; -; mRNA.
DR   EMBL; U78031; AAB96881.1; -; Genomic_DNA.
DR   EMBL; U78030; AAB96881.1; JOINED; Genomic_DNA.
DR   IPI; IPI00133454; -.
DR   IPI; IPI00227922; -.
DR   IPI; IPI00227924; -.
DR   IPI; IPI00406354; -.
DR   PIR; I49055; I49055.
DR   PIR; I49056; I49056.
DR   PIR; I49057; I49057.
DR   RefSeq; NP_033873.3; NM_009743.4.
DR   UniGene; Mm.238213; -.
DR   PDB; 1PQ0; X-ray; 2.20 A; A=1-196.
DR   PDB; 1PQ1; X-ray; 1.65 A; A=1-196.
DR   PDB; 2BZW; X-ray; 2.30 A; A=1-211.
DR   PDB; 3IHC; X-ray; 1.85 A; A=1-196.
DR   PDB; 3IHD; X-ray; 1.88 A; A=1-196.
DR   PDB; 3IHE; X-ray; 3.00 A; A=1-196.
DR   PDB; 3IHF; X-ray; 2.28 A; A/B/C/D=1-196.
DR   PDB; 3IIG; X-ray; 2.30 A; A=1-196.
DR   PDB; 3IIH; X-ray; 2.75 A; A=1-196.
DR   PDB; 3ILB; X-ray; 2.38 A; A/N=1-196.
DR   PDB; 3ILC; X-ray; 1.64 A; A=1-196.
DR   PDBsum; 1PQ0; -.
DR   PDBsum; 1PQ1; -.
DR   PDBsum; 2BZW; -.
DR   PDBsum; 3IHC; -.
DR   PDBsum; 3IHD; -.
DR   PDBsum; 3IHE; -.
DR   PDBsum; 3IHF; -.
DR   PDBsum; 3IIG; -.
DR   PDBsum; 3IIH; -.
DR   PDBsum; 3ILB; -.
DR   PDBsum; 3ILC; -.
DR   ProteinModelPortal; Q64373; -.
DR   SMR; Q64373; 1-210.
DR   IntAct; Q64373; 9.
DR   MINT; MINT-87027; -.
DR   STRING; Q64373; -.
DR   PhosphoSite; Q64373; -.
DR   PRIDE; Q64373; -.
DR   Ensembl; ENSMUST00000007803; ENSMUSP00000007803; ENSMUSG00000007659.
DR   Ensembl; ENSMUST00000109820; ENSMUSP00000105445; ENSMUSG00000007659.
DR   GeneID; 12048; -.
DR   KEGG; mmu:12048; -.
DR   UCSC; uc008ngi.1; mouse.
DR   UCSC; uc008ngn.1; mouse.
DR   CTD; 598; -.
DR   MGI; MGI:88139; Bcl2l1.
DR   OMA; NGSPSWH; -.
DR   OrthoDB; EOG47PX6Z; -.
DR   NextBio; 280335; -.
DR   PMAP-CutDB; Q64373; -.
DR   ArrayExpress; Q64373; -.
DR   Bgee; Q64373; -.
DR   CleanEx; MM_BCL2L1; -.
DR   Genevestigator; Q64373; -.
DR   GermOnline; ENSMUSG00000007659; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IMP:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; IDA:MGI.
DR   GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IMP:MGI.
DR   GO; GO:0071312; P:cellular response to alkaloid; IDA:MGI.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:MGI.
DR   GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
DR   GO; GO:0009566; P:fertilization; IGI:MGI.
DR   GO; GO:0007281; P:germ cell development; IMP:MGI.
DR   GO; GO:0040007; P:growth; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0008584; P:male gonad development; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IDA:MGI.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR   GO; GO:0045768; P:positive regulation of anti-apoptosis; IDA:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IGI:MGI.
DR   GO; GO:0046898; P:response to cycloheximide; IDA:MGI.
DR   GO; GO:0051789; P:response to protein stimulus; IDA:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IGI:MGI.
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; MOUSE2.PE3870; -.
KW   ENSMUSG000000076595old_1320000031; ENSMUSP000000078031old_1320000031;
KW   A2AHX7_MOUSE; A2AHX8_MOUSE; A2AHX9_MOUSE; Q3T9W4_MOUSE; Q5HZH3_MOUSE;
KW   Q9QWX2_MOUSE; AF088904; AF133281; AF133282; AK146461; AK172250; AL731857;
KW   BC089016; BC089017; CH466551; L35048; L35049; U10100; U10101; U10102;
KW   U51279; U78030; U78031; X83574;
KW   3D-structure; Alternative splicing; Apoptosis; Complete proteome;
KW   Cytoplasm; Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   233 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEAERETPSA INGNPSWHLA
     DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY
     QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP
     WIQENGGWDT FVDLYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
//

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