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Apoptosis regulator Bcl-2

 BCL2_RAT                Reviewed;         236 AA.
P49950; Q62837; Q64032;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
07-NOV-2018, entry version 146.
RecName: Full=Apoptosis regulator Bcl-2;
Name=Bcl2; Synonyms=Bcl-2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8144041; DOI=10.1016/0378-1119(94)90561-4;
Sato T., Irie S., Krajewski S., Reed J.C.;
"Cloning and sequencing of a cDNA encoding the rat Bcl-2 protein.";
Gene 140:291-292(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Ovary;
PubMed=7828536; DOI=10.1210/endo.136.1.7828536;
Tilly J.L., Tilly K.I., Kenton M.L., Johnson A.L.;
"Expression of members of the Bcl-2 gene family in the immature rat
ovary: equine chorionic gonadotropin-mediated inhibition of granulosa
cell apoptosis is associated with decreased Bax and constitutive Bcl-2
and Bcl-xlong messenger ribonucleic acid levels.";
Endocrinology 136:232-241(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 19-172.
PubMed=7969891; DOI=10.1016/0306-4522(94)90069-8;
Castren E., Ohga Y., Berzaghi M.P., Tzimagiorgis G., Thoenen H.,
Lindholm D.;
"bcl-2 messenger RNA is localized in neurons of the developing and
adult rat brain.";
Neuroscience 61:165-177(1994).
[4]
INTERACTION WITH PPIF.
PubMed=19228691; DOI=10.1074/jbc.M808750200;
Eliseev R.A., Malecki J., Lester T., Zhang Y., Humphrey J.,
Gunter T.E.;
"Cyclophilin D interacts with Bcl2 and exerts an anti-apoptotic
effect.";
J. Biol. Chem. 284:9692-9699(2009).
-!- 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). May attenuate
inflammation by impairing NLRP1-inflammasome activation, hence
CASP1 activation and IL1B release (By similarity).
{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. Also
interacts with APAF1, BBC3, BCL2L1, BNIPL, EI24, FKBP8, MRPL41,
and TP53BP2. 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.
-!- TISSUE SPECIFICITY: Expressed in a variety of tissues, with
highest levels in reproductive tissues. In the adult brain,
expression is localized in mitral cells of the olfactory bulb,
granule and pyramidal neurons of hippocampus, pontine nuclei,
cerebellar granule neurons, and in ependymal cells. In prenatal
brain, expression is higher and localized in the neuroepithelium
and in the cortical plate.
-!- 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. In the absence of
growth factors, BCL2 appears to be phosphorylated by other protein
kinases such as ERKs and stress-activated kinases. 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 (By similarity). {ECO:0000250}.
-!- 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; L14680; AAA53662.1; -; mRNA.
EMBL; U34964; AAA77687.1; -; mRNA.
EMBL; S74122; -; NOT_ANNOTATED_CDS; mRNA.
PIR; I53744; I53744.
PIR; I67432; I67432.
RefSeq; NP_058689.1; NM_016993.1.
UniGene; Rn.9996; -.
ProteinModelPortal; P49950; -.
SMR; P49950; -.
BioGrid; 246412; 1.
ComplexPortal; CPX-2018; BCL-2 dimer.
ComplexPortal; CPX-2020; BAD:BCL-2 complex.
ComplexPortal; CPX-2023; BID:BCL-2 complex.
ComplexPortal; CPX-2028; PUMA:BCL-2 complex.
ComplexPortal; CPX-2035; BIM:BCL-2 complex.
DIP; DIP-30849N; -.
IntAct; P49950; 3.
STRING; 10116.ENSRNOP00000003768; -.
iPTMnet; P49950; -.
PhosphoSitePlus; P49950; -.
PaxDb; P49950; -.
PRIDE; P49950; -.
GeneID; 24224; -.
KEGG; rno:24224; -.
UCSC; RGD:2199; rat.
CTD; 596; -.
RGD; 2199; Bcl2.
eggNOG; KOG4728; Eukaryota.
eggNOG; ENOG41123S0; LUCA.
HOGENOM; HOG000056452; -.
HOVERGEN; HBG004472; -.
InParanoid; P49950; -.
KO; K02161; -.
PhylomeDB; P49950; -.
PRO; PR:P49950; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0051400; F:BH domain binding; IPI:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IEP:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:1902618; P:cellular response to fluoride; IEP:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0034349; P:glial cell apoptotic process; IEP:RGD.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
GO; GO:0097421; P:liver regeneration; IEP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IMP:BHF-UCL.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
GO; GO:0001541; P:ovarian follicle development; IEP:RGD.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:HGNC.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:HGNC.
GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:HGNC.
GO; GO:0010044; P:response to aluminum ion; IEP:RGD.
GO; GO:1904645; P:response to amyloid-beta; IEP:RGD.
GO; GO:0031000; P:response to caffeine; IEP:RGD.
GO; GO:0051591; P:response to cAMP; IEP:RGD.
GO; GO:0046688; P:response to copper ion; IEP:RGD.
GO; GO:0051412; P:response to corticosterone; IEP:RGD.
GO; GO:0034097; P:response to cytokine; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0036017; P:response to erythropoietin; IEP:RGD.
GO; GO:0043627; P:response to estrogen; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IDA:RGD.
GO; GO:0051593; P:response to folic acid; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
GO; GO:0034284; P:response to monosaccharide; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0080184; P:response to phenylpropanoid; IEP:RGD.
GO; GO:0033197; P:response to vitamin E; IEP:RGD.
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; Complete proteome; Endoplasmic reticulum; Membrane;
Mitochondrion; Mitochondrion outer membrane; Nucleus; Phosphoprotein;
Reference proteome; Transmembrane; Transmembrane helix;
Ubl conjugation.
CHAIN 1 236 Apoptosis regulator Bcl-2.
/FTId=PRO_0000143050.
TRANSMEM 209 230 Helical. {ECO:0000255}.
MOTIF 10 30 BH4.
MOTIF 90 104 BH3.
MOTIF 133 152 BH1.
MOTIF 184 199 BH2.
SITE 34 35 Cleavage; by caspases. {ECO:0000250}.
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}.
CONFLICT 42 42 A -> R (in Ref. 2; AAA77687).
{ECO:0000305}.
CONFLICT 157 157 E -> G (in Ref. 1; AAA53662).
{ECO:0000305}.
CONFLICT 164 164 S -> Y (in Ref. 2; AAA77687).
{ECO:0000305}.
CONFLICT 212 212 L -> Q (in Ref. 2; AAA77687).
{ECO:0000305}.
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


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