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Apoptosis regulator Bcl-2

 BCL2_CRIGR              Reviewed;         236 AA.
Q9JJV8;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 103.
RecName: Full=Apoptosis regulator Bcl-2;
Name=BCL2;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=10973819; DOI=10.1006/bbrc.2000.3386;
Tomicic M.T., Christmann M., Kaina B.;
"Cloning and functional analysis of cDNA encoding the hamster Bcl-2
protein.";
Biochem. Biophys. Res. Commun. 275:899-903(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CLEAVAGE BY CASPASES.
PubMed=11181062; DOI=10.1006/bbrc.2001.4367;
Tomicic M.T., Kaina B.;
"Hamster Bcl-2 protein is cleaved in vitro and in cells by caspase-9
and caspase-3.";
Biochem. Biophys. Res. Commun. 281:404-408(2001).
-!- FUNCTION: Suppresses apoptosis in a variety of cell systems
including factor-dependent lymphohematopoietic and neural cells.
Regulates cell death by controlling the mitochondrial membrane
permeability. Appears to function in a feedback loop system with
caspases. Inhibits caspase activity either by preventing the
release of cytochrome c from the mitochondria and/or by binding to
the apoptosis-activating factor (APAF-1) (By similarity). May
attenuate inflammation by impairing NLRP1-inflammasome activation,
hence CASP1 activation and IL1B release (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P10415}.
-!- SUBUNIT: Forms homodimers, and heterodimers with BAX, BAD, BAK and
Bcl-X(L). Heterodimerization with BAX requires intact BH1 and BH2
motifs, and is necessary for anti-apoptotic activity (By
similarity). Also interacts with APAF1, BBC3, BCL2L1, BNIPL, EI24,
MRPL41 and TP53BP2. Binding to FKBP8 seems to target BCL2 to the
mitochondria and probably interferes with the binding of BCL2 to
its targets. Interacts with BAG1 in an ATP-dependent manner.
Interacts with RAF1 (the 'Ser-338' and 'Ser-339' phosphorylated
form). Interacts (via the BH4 domain) with EGLN3; the interaction
prevents the formation of the BAX-BCL2 complex and inhibits the
anti-apoptotic activity of BCL2 (By similarity). Interacts with
G0S2; this interaction also prevents the formation of the anti-
apoptotic BAX-BCL2 complex (By similarity). Interacts with BOP (By
similarity). Interacts with the SCF(FBXO10) complex (By
similarity). Interacts (via the loop between motifs BH4 and BH3)
with NLRP1 (via LRR repeats) (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P10415}.
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
membrane protein. Nucleus membrane; Single-pass membrane protein.
Endoplasmic reticulum membrane; Single-pass membrane protein.
-!- DOMAIN: The BH4 motif is required for anti-apoptotic activity and
for interaction with RAF1 and EGLN3. {ECO:0000250}.
-!- DOMAIN: BH1 and BH2 domains are required for the interaction with
BAX and for anti-apoptotic activity.
{ECO:0000250|UniProtKB:P10415}.
-!- DOMAIN: The loop between motifs BH4 and BH3 is required for the
interaction with NLRP1. {ECO:0000250|UniProtKB:P10415}.
-!- PTM: Phosphorylation/dephosphorylation on Ser-70 regulates anti-
apoptotic activity. Growth factor-stimulated phosphorylation on
Ser-70 by PKC is required for the anti-apoptosis activity and
occurs during the G2/M phase of the cell cycle (By similarity). In
the absence of growth factors, BCL2 appears to be phosphorylated
by other protein kinases such as ERKs and stress-activated kinases
(By similarity). Phosphorylated by MAPK8/JNK1 at Thr-69, Ser-70
and Ser-84, wich stimulates starvation-induced autophagy (By
similarity). Dephosphorylated by protein phosphatase 2A (PP2A) (By
similarity). {ECO:0000250}.
-!- PTM: Proteolytically cleaved by caspases during apoptosis. The
cleaved protein, lacking the BH4 motif, has pro-apoptotic
activity, causes the release of cytochrome c into the cytosol
promoting further caspase activity. {ECO:0000269|PubMed:11181062}.
-!- PTM: Monoubiquitinated by PRKN, leading to increase its stability.
Ubiquitinated by SCF(FBXO10), leading to its degradation by the
proteasome. {ECO:0000250}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ271720; CAB92245.1; -; mRNA.
PIR; JC7383; JC7383.
ProteinModelPortal; Q9JJV8; -.
IntAct; Q9JJV8; 1.
Ensembl; ENSCGRT00001031574; ENSCGRP00001027327; ENSCGRG00001024362.
HOVERGEN; HBG004472; -.
PMAP-CutDB; Q9JJV8; -.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0046930; C:pore complex; IEA:Ensembl.
GO; GO:0051434; F:BH3 domain binding; IEA:Ensembl.
GO; GO:0015267; F:channel activity; IEA:Ensembl.
GO; GO:0016248; F:channel inhibitor activity; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0051721; F:protein phosphatase 2A binding; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
GO; GO:0031103; P:axon regeneration; IEA:Ensembl.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0002326; P:B cell lineage commitment; IEA:Ensembl.
GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0001662; P:behavioral fear response; IEA:Ensembl.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0043375; P:CD8-positive, alpha-beta T cell lineage commitment; IEA:Ensembl.
GO; GO:0007569; P:cell aging; IEA:Ensembl.
GO; GO:0016049; P:cell growth; IEA:Ensembl.
GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
GO; GO:0021747; P:cochlear nucleus development; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0043583; P:ear development; IEA:Ensembl.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0048041; P:focal adhesion assembly; IEA:Ensembl.
GO; GO:0022612; P:gland morphogenesis; IEA:Ensembl.
GO; GO:0032835; P:glomerulus development; IEA:Ensembl.
GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IEA:Ensembl.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0006582; P:melanin metabolic process; IEA:Ensembl.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0014031; P:mesenchymal cell development; IEA:Ensembl.
GO; GO:0001656; P:metanephros development; IEA:Ensembl.
GO; GO:2000811; P:negative regulation of anoikis; IEA:Ensembl.
GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
GO; GO:0010523; P:negative regulation of calcium ion transport into cytosol; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IEA:Ensembl.
GO; GO:0032848; P:negative regulation of cellular pH reduction; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IEA:Ensembl.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
GO; GO:0033689; P:negative regulation of osteoblast proliferation; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0046671; P:negative regulation of retinal cell programmed cell death; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0048599; P:oocyte development; IEA:Ensembl.
GO; GO:0035265; P:organ growth; IEA:Ensembl.
GO; GO:0001503; P:ossification; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0048753; P:pigment granule organization; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0043085; P:positive regulation of catalytic activity; IEA:Ensembl.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0045636; P:positive regulation of melanocyte differentiation; IEA:Ensembl.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0014042; P:positive regulation of neuron maturation; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IEA:Ensembl.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0001952; P:regulation of cell-matrix adhesion; IEA:Ensembl.
GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
GO; GO:0010559; P:regulation of glycoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IEA:Ensembl.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Ensembl.
GO; GO:0006808; P:regulation of nitrogen utilization; IEA:Ensembl.
GO; GO:0043497; P:regulation of protein heterodimerization activity; IEA:Ensembl.
GO; GO:0043496; P:regulation of protein homodimerization activity; IEA:Ensembl.
GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
GO; GO:0045069; P:regulation of viral genome replication; IEA:Ensembl.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:0003014; P:renal system process; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0010332; P:response to gamma radiation; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0010039; P:response to iron ion; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0010224; P:response to UV-B; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR013278; Apop_reg_Bcl2.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR004725; Bcl2/BclX.
InterPro; IPR020717; Bcl2_BH1_motif_CS.
InterPro; IPR020726; Bcl2_BH2_motif_CS.
InterPro; IPR020728; Bcl2_BH3_motif_CS.
InterPro; IPR003093; Bcl2_BH4.
InterPro; IPR020731; Bcl2_BH4_motif_CS.
InterPro; IPR036834; Blc2-like_sf.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
PANTHER; PTHR11256:SF11; PTHR11256:SF11; 1.
Pfam; PF00452; Bcl-2; 1.
Pfam; PF02180; BH4; 1.
PRINTS; PR01863; APOPREGBCL2.
PRINTS; PR01862; BCL2FAMILY.
SMART; SM00265; BH4; 1.
SUPFAM; SSF56854; SSF56854; 1.
TIGRFAMs; TIGR00865; bcl-2; 1.
PROSITE; PS50062; BCL2_FAMILY; 1.
PROSITE; PS01080; BH1; 1.
PROSITE; PS01258; BH2; 1.
PROSITE; PS01259; BH3; 1.
PROSITE; PS01260; BH4_1; 1.
PROSITE; PS50063; BH4_2; 1.
1: Evidence at protein level;
Apoptosis; Endoplasmic reticulum; Membrane; Mitochondrion;
Mitochondrion outer membrane; Nucleus; Phosphoprotein; Transmembrane;
Transmembrane helix; Ubl conjugation.
CHAIN 1 236 Apoptosis regulator Bcl-2.
/FTId=PRO_0000143047.
TRANSMEM 209 230 Helical. {ECO:0000255}.
MOTIF 10 30 BH4.
MOTIF 90 104 BH3.
MOTIF 133 152 BH1.
MOTIF 184 199 BH2.
SITE 64 65 Cleavage; by caspase-3 and caspase-9.
MOD_RES 69 69 Phosphothreonine; by MAPK8.
{ECO:0000250|UniProtKB:P10415}.
MOD_RES 70 70 Phosphoserine; by MAPK8 and PKC.
{ECO:0000250|UniProtKB:P10415}.
MOD_RES 84 84 Phosphoserine; by MAPK8.
{ECO:0000250|UniProtKB:P10415}.
SEQUENCE 236 AA; 26491 MW; BECADF1EF3337228 CRC64;
MAQAGRTGYD NREIVMKYIH YKLSQRGYEW DVGDVDAAPL GAAPTPGIFS FQPESNPTPA
VHRDMAARTS PLRPIVATTG PTLSPVPPVV HLTLRRAGDD FSRRYRRDFA EMSSQLHLTP
FTARGRFATV VEELFRDGVN WGRIVAFFEF GGVMCVESVN REMSPLVDNI ALWMTEYLNR
HLHTWIQDNG GWDAFVELYG PSVRPLFDFS WLSLKTLLSL ALVGACITLG TYLGHK


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