B2CL1_MOUSE
ID B2CL1_MOUSE Reviewed; 233 AA.
AC Q64373; O35844; Q60657; Q60658; Q61338;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Bcl-2-like protein 1;
DE Short=Bcl2-L-1;
DE AltName: Full=Apoptosis regulator Bcl-X;
GN Name=Bcl2l1; Synonyms=Bcl2l, Bclx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BCL-X(L)).
RC STRAIN=2A4B; TISSUE=B-cell;
RA Kamesaki H., Michaud G.Y., Takatsu K., Okuma M.;
RT "IL-5 inhibits anti-IgM-induced apoptosis in an immature B cell line
RT through induction of bcl-Xl.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)),
RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=7607090; DOI=10.1242/dev.120.10.3033;
RA Gonzalez-Garcia M., Perez-Ballestero R., Ding L., Duan L., Boise L.H.,
RA Thompson C.B., Nunez G.;
RT "bcl-XL is the major bcl-x mRNA form expressed during murine development
RT and its product localizes to mitochondria.";
RL Development 120:3033-3042(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L); BCL-X(S) AND
RP BCL-X(DELTA-TM)).
RC TISSUE=Pre-B cell;
RX PubMed=7963517;
RA Fang W., Rivard J.J., Mueller D.L., Behrens T.W.;
RT "Cloning and molecular characterization of mouse bcl-x in B and T
RT lymphocytes.";
RL J. Immunol. 153:4388-4398(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)), AND
RP FUNCTION.
RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX PubMed=9390687; DOI=10.1016/s1074-7613(00)80384-2;
RA Yang X.-F., Weber G.F., Cantor H.;
RT "A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis
RT in T cells.";
RL Immunity 7:629-639(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9144489;
RA Grillot D.A., Gonzalez-Garcia M., Ekhterae D., Duan L., Inohara N.,
RA Ohta S., Seldin M.F., Nunez G.;
RT "Genomic organization, promoter region analysis, and chromosome
RT localization of the mouse bcl-x gene.";
RL J. Immunol. 158:4750-4757(1997).
RN [6]
RP INTERACTION WITH GIMAP3 AND GIMAP5.
RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103;
RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T.,
RA Kanno M., Takahama Y.;
RT "IAN family critically regulates survival and development of T
RT lymphocytes.";
RL PLoS Biol. 4:593-605(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH GIMAP5 AND HSPA8.
RX PubMed=21502331; DOI=10.1084/jem.20101192;
RA Chen Y., Yu M., Dai X., Zogg M., Wen R., Weiler H., Wang D.;
RT "Critical role for Gimap5 in the survival of mouse hematopoietic stem and
RT progenitor cells.";
RL J. Exp. Med. 208:923-935(2011).
RN [9]
RP INTERACTION WITH BCL2L11.
RX PubMed=27013495; DOI=10.15252/embr.201541392;
RA Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.;
RT "The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and enhances
RT apoptosis.";
RL EMBO Rep. 17:724-738(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-196 IN COMPLEX WITH BCL2L11.
RX PubMed=14499110; DOI=10.1016/s1074-7613(03)00234-6;
RA Liu X., Dai S., Zhu Y., Marrack P., Kappler J.W.;
RT "The structure of a Bcl-xL/Bim fragment complex: implications for Bim
RT function.";
RL Immunity 19:341-352(2003).
CC -!- FUNCTION: Potent inhibitor of cell death. Inhibits activation of
CC caspases. Appears to regulate cell death by blocking the voltage-
CC dependent anion channel (VDAC) by binding to it and preventing the
CC release of the caspase activator, CYC1, from the mitochondrial
CC membrane. Also acts as a regulator of G2 checkpoint and progression to
CC cytokinesis during mitosis. {ECO:0000269|PubMed:9390687}.
CC -!- FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity,
CC including neurotransmitter release and recovery, number of axonal
CC mitochondria as well as size and number of synaptic vesicle clusters.
CC During synaptic stimulation, increases ATP availability from
CC mitochondria through regulation of mitochondrial membrane ATP synthase
CC F(1)F(0) activity and regulates endocytic vesicle retrieval in
CC hippocampal neurons through association with DMN1L and stimulation of
CC its GTPase activity in synaptic vesicles (By similarity). May attenuate
CC inflammation impairing NLRP1-inflammasome activation, hence CASP1
CC activation and IL1B release (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q07817}.
CC -!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with BAD. Interacts with PGAM5. Interacts
CC with HEBP2. Interacts with p53/TP53 and BBC3; interaction with BBC3
CC disrupts the interaction with p53/TP53. Interacts with ATP5F1A and
CC ATP5F1B; the interactions mediate the association of isoform Bcl-X(L)
CC with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase (By
CC similarity). Interacts with VDAC1 (By similarity). Interacts with
CC BCL2L11 (via BH3) (PubMed:14499110, PubMed:27013495). Interacts with
CC RNF183 (By similarity). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5
CC (PubMed:16509771). Interacts with GIMAP5 and HSPA8/HSC70; the
CC interaction between HSPA8 and BCL2L1 is impaired in the absence of
CC GIMAP5 (PubMed:21502331). Interacts with isoform 4 of CLU; this
CC interaction releases and activates BAX and promotes cell death (By
CC similarity). {ECO:0000250|UniProtKB:P53563,
CC ECO:0000250|UniProtKB:Q07817, ECO:0000269|PubMed:14499110,
CC ECO:0000269|PubMed:16509771, ECO:0000269|PubMed:21502331,
CC ECO:0000269|PubMed:27013495}.
CC -!- SUBUNIT: [Isoform Bcl-X(L)]: Forms heterodimers with BAX, BAK or BCL2;
CC heterodimerization with BAX does not seem to be required for anti-
CC apoptotic activity (By similarity). Interacts with isoform 1 of SIVA1;
CC the interaction inhibits the anti-apoptotic activity (By similarity).
CC Interacts with IKZF3 (By similarity). Interacts with RTL10/BOP (By
CC similarity). Interacts with DNM1L and CLTA; DNM1L and BCL2L1 isoform
CC BCL-X(L) may form a complex in synaptic vesicles that also contains
CC clathrin and MFF (By similarity). Interacts (via the loop between
CC motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2,
CC NLRP3, NLRP4, PYCARD, nor MEFV (By similarity). Interacts with BECN1
CC (By similarity). {ECO:0000250|UniProtKB:P53563,
CC ECO:0000250|UniProtKB:Q07817}.
CC -!- INTERACTION:
CC Q64373; P59637: E; Xeno; NbExp=2; IntAct=EBI-526361, EBI-25487741;
CC Q64373-1; Q61337: Bad; NbExp=2; IntAct=EBI-526380, EBI-400328;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000269|PubMed:7607090}; Single-pass membrane protein
CC {ECO:0000269|PubMed:7607090}. Nucleus membrane {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:7607090}. Note=Localizes to the centrosome when
CC phosphorylated at Ser-49.
CC -!- SUBCELLULAR LOCATION: [Isoform Bcl-X(L)]: Mitochondrion inner membrane.
CC Mitochondrion outer membrane. Mitochondrion matrix {ECO:0000250}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=After neuronal
CC stimulation, translocates from cytosol to synaptic vesicle and
CC mitochondrion membrane in a calmodulin-dependent manner. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Bcl-X(delta-TM)]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Bcl-X(L); Synonyms=Bcl-xL;
CC IsoId=Q64373-1; Sequence=Displayed;
CC Name=Bcl-X(S); Synonyms=Bcl-xS;
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 brain,
CC thymus, bone marrow, and kidney. Bcl-X(L) and Bcl-X(delta-TM)
CC expression is enhanced in B- and T-lymphocytes that have been
CC activated. {ECO:0000269|PubMed:7607090}.
CC -!- DEVELOPMENTAL STAGE: Bcl-X(beta) is expressed in both embryonal and
CC postnatal tissues, whereas Bcl-X(L) is predominantly found in postnatal
CC tissues. {ECO:0000269|PubMed:7607090}.
CC -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity. The BH1
CC and BH2 motifs are required for both heterodimerization with other Bcl-
CC 2 family members and for repression of cell death.
CC -!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
CC interaction with NLRP1. {ECO:0000250|UniProtKB:Q07817}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved
CC protein, lacking the BH4 motif, has pro-apoptotic activity.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial
CC in normal mitotic cells, but complete in G2-arrested cells upon DNA-
CC damage, thus promoting subsequent apoptosis probably by triggering
CC caspases-mediated proteolysis. Phosphorylated by PLK3, leading to
CC regulate the G2 checkpoint and progression to cytokinesis during
CC mitosis. Phosphorylation at Ser-49 appears during the S phase and G2,
CC disappears rapidly in early mitosis during prometaphase, metaphase and
CC early anaphase, and re-appears during telophase and cytokinesis (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RNF183 during prolonged ER stress, leading to
CC degradation by the proteosome. {ECO:0000250|UniProtKB:Q07817}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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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 CCDS; CCDS16899.1; -. [Q64373-1]
DR PIR; I49055; I49055.
DR PIR; I49056; I49056.
DR PIR; I49057; I49057.
DR RefSeq; NP_001276645.1; NM_001289716.1. [Q64373-1]
DR RefSeq; NP_001276646.1; NM_001289717.1. [Q64373-1]
DR RefSeq; NP_033873.3; NM_009743.5. [Q64373-1]
DR RefSeq; XP_006498672.1; XM_006498609.3.
DR RefSeq; XP_006498674.1; XM_006498611.3. [Q64373-1]
DR RefSeq; XP_006498675.1; XM_006498612.2. [Q64373-1]
DR RefSeq; XP_011237562.1; XM_011239260.2. [Q64373-1]
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 PDB; 4YJ4; X-ray; 2.10 A; A=1-196.
DR PDB; 4YK9; X-ray; 1.70 A; A/F=2-196.
DR PDB; 5C3G; X-ray; 2.45 A; A=1-26.
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 PDBsum; 4YJ4; -.
DR PDBsum; 4YK9; -.
DR PDBsum; 5C3G; -.
DR AlphaFoldDB; Q64373; -.
DR BMRB; Q64373; -.
DR SMR; Q64373; -.
DR BioGRID; 198323; 25.
DR ComplexPortal; CPX-2021; BAD:BCL-XL complex. [Q64373-1]
DR ComplexPortal; CPX-2025; BIM:BCL-XL complex. [Q64373-1]
DR ComplexPortal; CPX-2029; PUMA:BCL-XL complex. [Q64373-1]
DR ComplexPortal; CPX-2037; BID:BCL-XL complex. [Q64373-1]
DR ComplexPortal; CPX-299; BCL-XL complex. [Q64373-1]
DR CORUM; Q64373; -.
DR ELM; Q64373; -.
DR IntAct; Q64373; 9.
DR STRING; 10090.ENSMUSP00000007803; -.
DR BindingDB; Q64373; -.
DR ChEMBL; CHEMBL3309112; -.
DR iPTMnet; Q64373; -.
DR PhosphoSitePlus; Q64373; -.
DR EPD; Q64373; -.
DR MaxQB; Q64373; -.
DR PaxDb; Q64373; -.
DR PRIDE; Q64373; -.
DR ProteomicsDB; 273510; -. [Q64373-1]
DR ProteomicsDB; 273511; -. [Q64373-2]
DR ProteomicsDB; 273512; -. [Q64373-3]
DR ProteomicsDB; 273513; -. [Q64373-4]
DR Antibodypedia; 3430; 2028 antibodies from 52 providers.
DR DNASU; 12048; -.
DR Ensembl; ENSMUST00000007803; ENSMUSP00000007803; ENSMUSG00000007659. [Q64373-1]
DR Ensembl; ENSMUST00000109820; ENSMUSP00000105445; ENSMUSG00000007659. [Q64373-1]
DR Ensembl; ENSMUST00000134902; ENSMUSP00000134614; ENSMUSG00000007659. [Q64373-3]
DR Ensembl; ENSMUST00000140436; ENSMUSP00000134596; ENSMUSG00000007659. [Q64373-3]
DR GeneID; 12048; -.
DR KEGG; mmu:12048; -.
DR UCSC; uc008ngi.2; mouse. [Q64373-2]
DR UCSC; uc008ngj.2; mouse. [Q64373-1]
DR UCSC; uc008ngn.2; mouse. [Q64373-3]
DR CTD; 598; -.
DR MGI; MGI:88139; Bcl2l1.
DR VEuPathDB; HostDB:ENSMUSG00000007659; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244953; -.
DR InParanoid; Q64373; -.
DR OMA; SPNRTDG; -.
DR PhylomeDB; Q64373; -.
DR TreeFam; TF315834; -.
DR Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-MMU-844455; The NLRP1 inflammasome.
DR Reactome; R-MMU-9648002; RAS processing.
DR BioGRID-ORCS; 12048; 18 hits in 75 CRISPR screens.
DR ChiTaRS; Bcl2l1; mouse.
DR EvolutionaryTrace; Q64373; -.
DR PRO; PR:Q64373; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q64373; protein.
DR Bgee; ENSMUSG00000007659; Expressed in spermatocyte and 260 other tissues.
DR ExpressionAtlas; Q64373; baseline and differential.
DR Genevisible; Q64373; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097136; C:Bcl-2 family protein complex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005740; C:mitochondrial envelope; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0097143; C:PUMA-BCL-xl complex; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0051400; F:BH domain binding; ISO:MGI.
DR GO; GO:0051434; F:BH3 domain binding; ISO:MGI.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0071839; P:apoptotic process in bone marrow cell; 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:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0097048; P:dendritic cell apoptotic process; IDA:MGI.
DR GO; GO:0044565; P:dendritic cell proliferation; IDA:MGI.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
DR GO; GO:0009566; P:fertilization; IGI:MGI.
DR GO; GO:0007281; P:germ cell development; IMP:MGI.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IGI:MGI.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IDA:MGI.
DR GO; GO:0051093; P:negative regulation of developmental process; IMP:MGI.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:MGI.
DR GO; GO:2000242; P:negative regulation of reproductive process; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IDA:MGI.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:MGI.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; ISO:MGI.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISO:MGI.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO: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:0034097; P:response to cytokine; ISO:MGI.
DR GO; GO:0002931; P:response to ischemia; ISO:MGI.
DR GO; GO:0009314; P:response to radiation; IMP:MGI.
DR GO; GO:0009615; P:response to virus; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; ISO:MGI.
DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; ISO:MGI.
DR CDD; cd06845; Bcl-2_like; 1.
DR DisProt; DP02817; -.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR013279; Apop_reg_BclX.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR004725; Bcl2/BclX.
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 PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF12; PTHR11256:SF12; 1.
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 SUPFAM; SSF56854; SSF56854; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..233
FT /note="Bcl-2-like protein 1"
FT /id="PRO_0000143063"
FT TRANSMEM 210..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 27..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..24
FT /note="BH4"
FT MOTIF 86..100
FT /note="BH3"
FT MOTIF 129..148
FT /note="BH1"
FT MOTIF 180..195
FT /note="BH2"
FT COMPBIAS 32..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine; by PLK3"
FT /evidence="ECO:0000250|UniProtKB:Q07817"
FT MOD_RES 62
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q07817"
FT VAR_SEQ 126..188
FT /note="Missing (in isoform Bcl-X(S))"
FT /evidence="ECO:0000305"
FT /id="VSP_000517"
FT VAR_SEQ 189..233
FT /note="DTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK -> VRT
FT TPLVCPPLACVSLLCEHP (in isoform Bcl-X(beta))"
FT /evidence="ECO:0000305"
FT /id="VSP_000518"
FT VAR_SEQ 194..233
FT /note="LYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK -> GHDCGWCG
FT SAGLTLQSEVTRH (in isoform Bcl-X(delta-TM))"
FT /evidence="ECO:0000305"
FT /id="VSP_000519"
FT CONFLICT 207..209
FT /note="QER -> KEG (in Ref. 4; AAC53459)"
FT /evidence="ECO:0000305"
FT HELIX 1..20
FT /evidence="ECO:0007829|PDB:3ILC"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:4YK9"
FT HELIX 83..101
FT /evidence="ECO:0007829|PDB:3ILC"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1PQ1"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:3ILC"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1PQ1"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:3ILC"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:3ILC"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:3ILC"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:3ILC"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:3ILC"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:3ILC"
SQ SEQUENCE 233 AA; 26132 MW; 24D2AC79887E072E 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
