B2CL1_RAT
ID B2CL1_RAT Reviewed; 233 AA.
AC P53563; P70613; P70614; Q52KS0; Q62678; Q62836; Q64087; Q64128;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Bcl-2-like protein 1;
DE Short=Bcl2-L-1;
DE AltName: Full=Apoptosis regulator Bcl-X;
GN Name=Bcl2l1; Synonyms=Bclx, Blc2l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS BCL-X(L) AND BCL-X(S)).
RC TISSUE=Brain;
RA Michaelidis T.M.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM BCL-X(L)).
RC TISSUE=Brain;
RA Wesselingh S.L., David G.L., Choi S., Veliuona M., Hardwick J.M.;
RT "Cloning and expression of rat bcl-x in cultured neurons.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)), AND
RP FUNCTION.
RC TISSUE=Thymus;
RX PubMed=8662675; DOI=10.1074/jbc.271.22.13258;
RA Shiraiwa N., Inohara N., Okada S., Yuzaki M., Shoji S., Ohta S.;
RT "An additional form of rat Bcl-x, Bcl-xbeta, generated by an unspliced RNA,
RT promotes apoptosis in promyeloid cells.";
RL J. Biol. Chem. 271:13258-13265(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(S)), AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Ovary;
RX PubMed=7828536; DOI=10.1210/endo.136.1.7828536;
RA Tilly J.L., Tilly K.I., Kenton M.L., Johnson A.L.;
RT "Expression of members of the Bcl-2 gene family in the immature rat ovary:
RT equine chorionic gonadotropin-mediated inhibition of granulosa cell
RT apoptosis is associated with decreased Bax and constitutive Bcl-2 and Bcl-
RT xlong messenger ribonucleic acid levels.";
RL Endocrinology 136:232-241(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BCL-X(L)).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION IN SYNAPTIC VESICLE REGULATION, AND INTERACTION WITH DNM1L.
RX PubMed=18250306; DOI=10.1073/pnas.0711647105;
RA Li H., Chen Y., Jones A.F., Sanger R.H., Collis L.P., Flannery R.,
RA McNay E.C., Yu T., Schwarzenbacher R., Bossy B., Bossy-Wetzel E.,
RA Bennett M.V., Pypaert M., Hickman J.A., Smith P.J., Hardwick J.M.,
RA Jonas E.A.;
RT "Bcl-xL induces Drp1-dependent synapse formation in cultured hippocampal
RT neurons.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2169-2174(2008).
RN [7]
RP FUNCTION IN SYNAPTIC VESICLE REGULATION, INTERACTION WITH ATP5F1A AND
RP ATP5F1B, AND SUBCELLULAR LOCATION.
RX PubMed=21926988; DOI=10.1038/ncb2330;
RA Alavian K.N., Li H., Collis L., Bonanni L., Zeng L., Sacchetti S.,
RA Lazrove E., Nabili P., Flaherty B., Graham M., Chen Y., Messerli S.M.,
RA Mariggio M.A., Rahner C., McNay E., Shore G.C., Smith P.J., Hardwick J.M.,
RA Jonas E.A.;
RT "Bcl-xL regulates metabolic efficiency of neurons through interaction with
RT the mitochondrial F1FO ATP synthase.";
RL Nat. Cell Biol. 13:1224-1233(2011).
RN [8]
RP FUNCTION IN SYNAPTIC VESICLE REGULATION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH CLTA; DNM1L AND MFF.
RX PubMed=23792689; DOI=10.1038/ncb2791;
RA Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P.,
RA Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S.,
RA Morrison R.S., Jonas E.A.;
RT "A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during
RT endocytosis.";
RL Nat. Cell Biol. 15:773-785(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9346936; DOI=10.1074/jbc.272.44.27886;
RA Aritomi M., Kunishima N., Inohara N., Ishibashi Y., Ohta S., Morikawa K.;
RT "Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-
RT 2 protein family.";
RL J. Biol. Chem. 272:27886-27892(1997).
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.
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. May attenuate inflammation
CC impairing NLRP1-inflammasome activation, hence CASP1 activation and
CC IL1B release (By similarity). {ECO:0000250|UniProtKB:Q07817,
CC ECO:0000269|PubMed:18250306, ECO:0000269|PubMed:21926988,
CC ECO:0000269|PubMed:23792689, ECO:0000269|PubMed:7828536,
CC ECO:0000269|PubMed:8662675}.
CC -!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis.
CC -!- SUBUNIT: Homodimer. Interacts with BCL2L11 (By similarity). Interacts
CC with BAD. Interacts with PGAM5. Interacts with HEBP2. Interacts with
CC p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with
CC p53/TP53. Interacts with ATP5F1A and ATP5F1B; the interactions mediate
CC the association of isoform Bcl-X(L) with the mitochondrial membrane ATP
CC synthase F(1)F(0) ATP synthase (PubMed:21926988). Interacts with VDAC1
CC (By similarity). Interacts with BCL2L11 (via BH3) (By similarity).
CC Interacts with RNF183 (By similarity). Interacts with GIMAP3/IAN4 and
CC GIMAP5/IAN5 (By similarity). Interacts with GIMAP5 and HSPA8/HSC70; the
CC interaction between HSPA8 and BCL2L1 is impaired in the absence of
CC GIMAP5 (By similarity). Interacts with isoform 4 of CLU; this
CC interaction releases and activates BAX and promotes cell death (By
CC similarity). {ECO:0000250|UniProtKB:Q07817,
CC ECO:0000250|UniProtKB:Q64373, ECO:0000269|PubMed:21926988}.
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 (PubMed:18250306, PubMed:23792689). Interacts (via the
CC loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not
CC with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (By similarity). Interacts
CC with BECN1 (By similarity). {ECO:0000250|UniProtKB:Q07817,
CC ECO:0000269|PubMed:18250306, ECO:0000269|PubMed:23792689}.
CC -!- INTERACTION:
CC P53563-1; P08081: Clta; NbExp=2; IntAct=EBI-287204, EBI-916140;
CC P53563-1; O35303: Dnm1l; NbExp=4; IntAct=EBI-287204, EBI-1767447;
CC -!- SUBCELLULAR LOCATION: [Isoform Bcl-X(L)]: Mitochondrion inner membrane.
CC Mitochondrion outer membrane. Mitochondrion matrix. Cytoplasmic
CC vesicle, secretory vesicle, synaptic vesicle membrane. Cytoplasm,
CC cytosol. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Nucleus membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC Note=Localizes to the centrosome when phosphorylated at Ser-49 (By
CC similarity). After neuronal stimulation, translocates from cytosol to
CC synaptic vesicle and mitochondrion membrane in a calmodulin-dependent
CC manner. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Bcl-X(L); Synonyms=Bcl-xL;
CC IsoId=P53563-1; Sequence=Displayed;
CC Name=Bcl-X(S); Synonyms=Bcl-xS;
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 ovary,
CC the predominant form is Bcl-X(L), with a small but detectable level of
CC Bcl-X(S).
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 (By
CC similarity). {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC60701.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC60702.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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 PIR; I67431; I67431.
DR PIR; I67435; I67435.
DR PIR; S51761; S51761.
DR RefSeq; NP_001028842.1; NM_001033670.1. [P53563-1]
DR RefSeq; NP_001028843.1; NM_001033671.1. [P53563-2]
DR RefSeq; NP_113723.2; NM_031535.2.
DR RefSeq; XP_006235327.1; XM_006235265.3. [P53563-1]
DR PDB; 1AF3; X-ray; 2.50 A; A=1-196.
DR PDB; 4QNQ; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-233.
DR PDBsum; 1AF3; -.
DR PDBsum; 4QNQ; -.
DR AlphaFoldDB; P53563; -.
DR BMRB; P53563; -.
DR SMR; P53563; -.
DR BioGRID; 246998; 5.
DR ComplexPortal; CPX-2022; BAD:BCL-XL complex. [P53563-1]
DR ComplexPortal; CPX-2026; BIM:BCL-XL complex. [P53563-1]
DR ComplexPortal; CPX-2030; PUMA:BCL-XL complex. [P53563-1]
DR ComplexPortal; CPX-2038; BID:BCL-XL complex. [P53563-1]
DR ComplexPortal; CPX-300; BCL-XL complex. [P53563-1]
DR CORUM; P53563; -.
DR DIP; DIP-29698N; -.
DR IntAct; P53563; 5.
DR STRING; 10116.ENSRNOP00000043542; -.
DR ChEMBL; CHEMBL1075182; -.
DR iPTMnet; P53563; -.
DR PhosphoSitePlus; P53563; -.
DR SwissPalm; P53563; -.
DR jPOST; P53563; -.
DR PaxDb; P53563; -.
DR PRIDE; P53563; -.
DR Ensembl; ENSRNOT00000010762; ENSRNOP00000010762; ENSRNOG00000007946. [P53563-1]
DR GeneID; 24888; -.
DR KEGG; rno:24888; -.
DR UCSC; RGD:2200; rat. [P53563-1]
DR CTD; 598; -.
DR RGD; 2200; Bcl2l1.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244953; -.
DR HOGENOM; CLU_085401_0_1_1; -.
DR InParanoid; P53563; -.
DR OMA; SPNRTDG; -.
DR OrthoDB; 1218929at2759; -.
DR PhylomeDB; P53563; -.
DR Reactome; R-RNO-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
DR Reactome; R-RNO-844455; The NLRP1 inflammasome.
DR Reactome; R-RNO-9648002; RAS processing.
DR EvolutionaryTrace; P53563; -.
DR PRO; PR:P53563; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000007946; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; P53563; baseline and differential.
DR Genevisible; P53563; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0097136; C:Bcl-2 family protein complex; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IDA:CAFA.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051400; F:BH domain binding; IPI:RGD.
DR GO; GO:0051434; F:BH3 domain binding; ISO:RGD.
DR GO; GO:0030276; F:clathrin binding; IPI:CAFA.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:RGD.
DR GO; GO:0051020; F:GTPase binding; IPI:CAFA.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:RGD.
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:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006915; P:apoptotic process; IEP:RGD.
DR GO; GO:0071839; P:apoptotic process in bone marrow cell; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0071312; P:cellular response to alkaloid; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:1905218; P:cellular response to astaxanthin; IEP:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; IEP:RGD.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD.
DR GO; GO:0036018; P:cellular response to erythropoietin; IEP:RGD.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISO:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:1990646; P:cellular response to prolactin; IEP:RGD.
DR GO; GO:1904579; P:cellular response to thapsigargin; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0009566; P:fertilization; ISO:RGD.
DR GO; GO:0007281; P:germ cell development; ISO:RGD.
DR GO; GO:0097284; P:hepatocyte apoptotic process; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
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:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IMP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:CAFA.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IMP:CAFA.
DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:CAFA.
DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IMP:CAFA.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; ISO:RGD.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; IMP:CAFA.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISO:RGD.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0046898; P:response to cycloheximide; ISO:RGD.
DR GO; GO:0034097; P:response to cytokine; ISO:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
DR GO; GO:0036017; P:response to erythropoietin; IEP: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:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IDA:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009314; P:response to radiation; ISO:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP:CAFA.
DR CDD; cd06845; Bcl-2_like; 1.
DR DisProt; DP00449; -.
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; Endocytosis; 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_0000143065"
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_000520"
FT VAR_SEQ 189..233
FT /note="DTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK -> VRT
FT TPLVCPPLVCLSSVEIPNCPFWSPGMVVEDIDYSGDIPGLL (in isoform Bcl-
FT X(beta))"
FT /evidence="ECO:0000305"
FT /id="VSP_000521"
FT CONFLICT 6
FT /note="R -> Q (in Ref. 1; CAA57886/CAA57887)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="F -> S (in Ref. 2; AAA19257)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="A -> E (in Ref. 2; AAA19257)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="I -> L (in Ref. 4; AAA77686/AAC60701/AAC60702)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="A -> V (in Ref. 4; AAA77686/AAC60701/AAC60702)"
FT /evidence="ECO:0000305"
FT CONFLICT 143..144
FT /note="FF -> SS (in Ref. 4; AAA77686/AAC60701)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> T (in Ref. 4; AAA77686/AAC60701/AAC60702)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="A -> P (in Ref. 4; AAA77686/AAC60701/AAC60702)"
FT /evidence="ECO:0000305"
FT HELIX 2..19
FT /evidence="ECO:0007829|PDB:4QNQ"
FT TURN 25..28
FT /evidence="ECO:0007829|PDB:1AF3"
FT HELIX 82..100
FT /evidence="ECO:0007829|PDB:4QNQ"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:4QNQ"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:4QNQ"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:4QNQ"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4QNQ"
FT HELIX 137..156
FT /evidence="ECO:0007829|PDB:4QNQ"
FT HELIX 162..177
FT /evidence="ECO:0007829|PDB:4QNQ"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:4QNQ"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:4QNQ"
SQ SEQUENCE 233 AA; 26158 MW; 2B62B6C63864BC8F 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
