BCL2_RAT
ID BCL2_RAT Reviewed; 236 AA.
AC P49950; Q62837; Q64032;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Apoptosis regulator Bcl-2;
GN Name=Bcl2; Synonyms=Bcl-2;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=8144041; DOI=10.1016/0378-1119(94)90561-4;
RA Sato T., Irie S., Krajewski S., Reed J.C.;
RT "Cloning and sequencing of a cDNA encoding the rat Bcl-2 protein.";
RL Gene 140:291-292(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-172.
RX PubMed=7969891; DOI=10.1016/0306-4522(94)90069-8;
RA Castren E., Ohga Y., Berzaghi M.P., Tzimagiorgis G., Thoenen H.,
RA Lindholm D.;
RT "bcl-2 messenger RNA is localized in neurons of the developing and adult
RT rat brain.";
RL Neuroscience 61:165-177(1994).
RN [4]
RP INTERACTION WITH PPIF.
RX PubMed=19228691; DOI=10.1074/jbc.m808750200;
RA Eliseev R.A., Malecki J., Lester T., Zhang Y., Humphrey J., Gunter T.E.;
RT "Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic effect.";
RL J. Biol. Chem. 284:9692-9699(2009).
CC -!- FUNCTION: Suppresses apoptosis in a variety of cell systems including
CC factor-dependent lymphohematopoietic and neural cells. Regulates cell
CC death by controlling the mitochondrial membrane permeability. Appears
CC to function in a feedback loop system with caspases. Inhibits caspase
CC activity either by preventing the release of cytochrome c from the
CC mitochondria and/or by binding to the apoptosis-activating factor
CC (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1
CC and AMBRA1 during non-starvation conditions and inhibits their
CC autophagy function. May attenuate inflammation by impairing NLRP1-
CC inflammasome activation, hence CASP1 activation and IL1B release.
CC {ECO:0000250|UniProtKB:P10415}.
CC -!- SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and Bcl-
CC X(L). Heterodimerization with BAX requires intact BH1 and BH2 motifs,
CC and is necessary for anti-apoptotic activity (By similarity). Interacts
CC with EI24 (By similarity). Also interacts with APAF1, BBC3, BCL2L1,
CC BNIPL, MRPL41 and TP53BP2. Binding to FKBP8 seems to target BCL2 to the
CC mitochondria and probably interferes with the binding of BCL2 to its
CC targets. Interacts with BAG1 in an ATP-dependent manner. Interacts with
CC RAF1 (the 'Ser-338' and 'Ser-339' phosphorylated form). Interacts (via
CC the BH4 domain) with EGLN3; the interaction prevents the formation of
CC the BAX-BCL2 complex and inhibits the anti-apoptotic activity of BCL2.
CC Interacts with G0S2; this interaction also prevents the formation of
CC the anti-apoptotic BAX-BCL2 complex. Interacts with RTL10/BOP.
CC Interacts with the SCF(FBXO10) complex. 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
CC GIMAP3/IAN4, GIMAP4/IAN1 and GIMAP5/IAN5 (By similarity). Interacts
CC with BCAP31. Interacts with IRF3; the interaction is inhibited by
CC Sendai virus infection. Interacts with BECN1; thereby inhibiting
CC autophagy in non-starvation conditions. Interacts with AMBRA1; thereby
CC inhibiting autophagy (By similarity). {ECO:0000250|UniProtKB:P10415,
CC ECO:0000250|UniProtKB:P10417}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein
CC {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single-
CC pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues, with highest
CC levels in reproductive tissues. In the adult brain, expression is
CC localized in mitral cells of the olfactory bulb, granule and pyramidal
CC neurons of hippocampus, pontine nuclei, cerebellar granule neurons, and
CC in ependymal cells. In prenatal brain, expression is higher and
CC localized in the neuroepithelium and in the cortical plate.
CC -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity and for
CC interaction with RAF1 and EGLN3. {ECO:0000250}.
CC -!- DOMAIN: BH1 and BH2 domains are required for the interaction with BAX
CC and for anti-apoptotic activity. {ECO:0000250|UniProtKB:P10415}.
CC -!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
CC interaction with NLRP1. {ECO:0000250|UniProtKB:P10415}.
CC -!- DOMAIN: The BH3 motif is required for XIAP-mediated ubiquitination and
CC subsequent induction of apoptosis. {ECO:0000250|UniProtKB:P10415}.
CC -!- PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-
CC apoptotic activity. Growth factor-stimulated phosphorylation on Ser-70
CC by PKC is required for the anti-apoptosis activity and occurs during
CC the G2/M phase of the cell cycle. In the absence of growth factors,
CC BCL2 appears to be phosphorylated by other protein kinases such as ERKs
CC and stress-activated kinases. Phosphorylated by MAPK8/JNK1 at Thr-69,
CC Ser-70 and Ser-84, wich stimulates starvation-induced autophagy (By
CC similarity). Dephosphorylated by protein phosphatase 2A (PP2A) (By
CC similarity). {ECO:0000250|UniProtKB:P10415,
CC ECO:0000250|UniProtKB:P10417}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved
CC protein, lacking the BH4 motif, has pro-apoptotic activity, causes the
CC release of cytochrome c into the cytosol promoting further caspase
CC activity (By similarity). {ECO:0000250|UniProtKB:P10415}.
CC -!- PTM: Monoubiquitinated by PRKN, leading to an increase in its
CC stability. Ubiquitinated by SCF(FBXO10), leading to its degradation by
CC the proteasome. {ECO:0000250|UniProtKB:P10415}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; L14680; AAA53662.1; -; mRNA.
DR EMBL; U34964; AAA77687.1; -; mRNA.
DR EMBL; S74122; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; I53744; I53744.
DR PIR; I67432; I67432.
DR RefSeq; NP_058689.1; NM_016993.1.
DR AlphaFoldDB; P49950; -.
DR SMR; P49950; -.
DR BioGRID; 246412; 1.
DR ComplexPortal; CPX-2018; BCL-2 dimer.
DR ComplexPortal; CPX-2020; BAD:BCL-2 complex.
DR ComplexPortal; CPX-2023; BID:BCL-2 complex.
DR ComplexPortal; CPX-2028; PUMA:BCL-2 complex.
DR ComplexPortal; CPX-2035; BIM:BCL-2 complex.
DR DIP; DIP-30849N; -.
DR IntAct; P49950; 3.
DR STRING; 10116.ENSRNOP00000003768; -.
DR iPTMnet; P49950; -.
DR PhosphoSitePlus; P49950; -.
DR PaxDb; P49950; -.
DR GeneID; 24224; -.
DR KEGG; rno:24224; -.
DR UCSC; RGD:2199; rat.
DR CTD; 596; -.
DR RGD; 2199; Bcl2.
DR eggNOG; KOG4728; Eukaryota.
DR InParanoid; P49950; -.
DR OrthoDB; 1218929at2759; -.
DR PhylomeDB; P49950; -.
DR Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
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 PRO; PR:P49950; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0030061; C:mitochondrial crista; IDA:CACAO.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0043209; C:myelin sheath; ISO:RGD.
DR GO; GO:0031965; C:nuclear membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0046930; C:pore complex; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0051400; F:BH domain binding; IPI:RGD.
DR GO; GO:0051434; F:BH3 domain binding; ISO:RGD.
DR GO; GO:0015267; F:channel activity; ISO:RGD.
DR GO; GO:0016248; F:channel inhibitor activity; ISO:RGD.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; ISO:RGD.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEP:RGD.
DR GO; GO:0031103; P:axon regeneration; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR GO; GO:0001782; P:B cell homeostasis; ISO:RGD.
DR GO; GO:0002326; P:B cell lineage commitment; ISO:RGD.
DR GO; GO:0042100; P:B cell proliferation; ISO:RGD.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0001662; P:behavioral fear response; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0043375; P:CD8-positive, alpha-beta T cell lineage commitment; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
DR GO; GO:1902618; P:cellular response to fluoride; IEP:RGD.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
DR GO; GO:0021747; P:cochlear nucleus development; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0048066; P:developmental pigmentation; ISO:RGD.
DR GO; GO:0048546; P:digestive tract morphogenesis; ISO:RGD.
DR GO; GO:0043583; P:ear development; ISO:RGD.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISO:RGD.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0048041; P:focal adhesion assembly; ISO:RGD.
DR GO; GO:0022612; P:gland morphogenesis; ISO:RGD.
DR GO; GO:0034349; P:glial cell apoptotic process; IEP:RGD.
DR GO; GO:0032835; P:glomerulus development; ISO:RGD.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
DR GO; GO:0002520; P:immune system development; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0001776; P:leukocyte homeostasis; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0002260; P:lymphocyte homeostasis; ISO:RGD.
DR GO; GO:0002320; P:lymphoid progenitor cell differentiation; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0006582; P:melanin metabolic process; ISO:RGD.
DR GO; GO:0030318; P:melanocyte differentiation; ISO:RGD.
DR GO; GO:0014031; P:mesenchymal cell development; ISO:RGD.
DR GO; GO:0001656; P:metanephros development; ISO:RGD.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; ISO:RGD.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0032848; P:negative regulation of cellular pH reduction; ISO:RGD.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISO:RGD.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0030279; P:negative regulation of ossification; ISO:RGD.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISO:RGD.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0046671; P:negative regulation of retinal cell programmed cell death; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
DR GO; GO:0048599; P:oocyte development; ISO:RGD.
DR GO; GO:0035265; P:organ growth; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0048753; P:pigment granule organization; ISO:RGD.
DR GO; GO:0043473; P:pigmentation; ISO:RGD.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:RGD.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0048087; P:positive regulation of developmental pigmentation; ISO:RGD.
DR GO; GO:0045636; P:positive regulation of melanocyte differentiation; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0014042; P:positive regulation of neuron maturation; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; ISO:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; ISO:RGD.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0050790; P:regulation of catalytic activity; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0001952; P:regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0048070; P:regulation of developmental pigmentation; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0010559; P:regulation of glycoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0040008; P:regulation of growth; ISO:RGD.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:HGNC-UCL.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:HGNC-UCL.
DR GO; GO:0006808; P:regulation of nitrogen utilization; ISO:RGD.
DR GO; GO:0043067; P:regulation of programmed cell death; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; ISO:RGD.
DR GO; GO:0045069; P:regulation of viral genome replication; ISO:RGD.
DR GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:HGNC-UCL.
DR GO; GO:0003014; P:renal system process; ISO:RGD.
DR GO; GO:0010044; P:response to aluminum ion; IEP:RGD.
DR GO; GO:1904645; P:response to amyloid-beta; IEP:RGD.
DR GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP: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:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0051593; P:response to folic acid; IEP:RGD.
DR GO; GO:0010332; P:response to gamma radiation; ISO:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; ISO:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO: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:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0010039; P:response to iron ion; ISO:RGD.
DR GO; GO:0002931; P:response to ischemia; ISO:RGD.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
DR GO; GO:0034284; P:response to monosaccharide; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0080184; P:response to phenylpropanoid; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; ISO:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR GO; GO:0010224; P:response to UV-B; ISO:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0048536; P:spleen development; ISO:RGD.
DR GO; GO:0030217; P:T cell differentiation; ISO:RGD.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
DR GO; GO:0002360; P:T cell lineage commitment; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR013278; Apop_reg_Bcl2.
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:SF11; PTHR11256:SF11; 1.
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 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 Apoptosis; Cytoplasm; Endoplasmic reticulum; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..236
FT /note="Apoptosis regulator Bcl-2"
FT /id="PRO_0000143050"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 10..30
FT /note="BH4"
FT MOTIF 90..104
FT /note="BH3"
FT MOTIF 133..152
FT /note="BH1"
FT MOTIF 184..199
FT /note="BH2"
FT SITE 34..35
FT /note="Cleavage; by caspases"
FT /evidence="ECO:0000250"
FT MOD_RES 69
FT /note="Phosphothreonine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P10415"
FT MOD_RES 70
FT /note="Phosphoserine; by MAPK8 and PKC"
FT /evidence="ECO:0000250|UniProtKB:P10415"
FT MOD_RES 84
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000250|UniProtKB:P10415"
FT CONFLICT 42
FT /note="A -> R (in Ref. 2; AAA77687)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="E -> G (in Ref. 1; AAA53662)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="S -> Y (in Ref. 2; AAA77687)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="L -> Q (in Ref. 2; AAA77687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 26622 MW; E7688CB9071A872A CRC64;
MAQAGRTGYD NREIVMKYIH YKLSQRGYEW DTGDEDSAPL RAAPTPGIFS FQPESNRTPA
VHRDTAARTS PLRPLVANAG PALSPVPPVV HLTLRRAGDD FSRRYRRDFA EMSSQLHLTP
FTARGRFATV VEELFRDGVN WGRIVAFFEF GGVMCVESVN REMSPLVDNI ALWMTEYLNR
HLHTWIQDNG GWDAFVELYG PSMRPLFDFS WLSLKTLLSL ALVGACITLG AYLGHK
