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Bcl2-associated agonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl-xL/Bcl-2-associated death promoter) (Bcl2 antagonist of cell death)

 BAD_RAT                 Reviewed;         205 AA.
O35147; O70256; Q9JHX1;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 2.
30-AUG-2017, entry version 138.
RecName: Full=Bcl2-associated agonist of cell death;
Short=BAD;
AltName: Full=Bcl-2-binding component 6;
AltName: Full=Bcl-xL/Bcl-2-associated death promoter;
AltName: Full=Bcl2 antagonist of cell death;
Name=Bad;
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], AND MUTAGENESIS OF SER-113 AND SER-137.
TISSUE=Ovary;
PubMed=9369453; DOI=10.1210/mend.11.12.0023;
Hsu S.Y., Kaipia A., Zhu L., Hsueh A.J.W.;
"Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced
apoptosis in mammalian cells by 14-3-3 isoforms and P11.";
Mol. Endocrinol. 11:1858-1867(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9535132; DOI=10.1016/S0304-3940(98)00116-5;
D'Agata V., Magro G., Travali S., Musco S., Cavallaro S.;
"Cloning and expression of the programmed cell death regulator BAD in
the rat brain.";
Neurosci. Lett. 243:137-140(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
TISSUE=Brain;
PubMed=11161472; DOI=10.1006/mcne.2000.0905;
Hamner S., Arumae U., Yu L.-Y., Sun Y.-F., Saarma M., Lindholm D.;
"Functional characterization of two splice variants of rat BAD and
their interaction with Bcl-w in sympathetic neurons.";
Mol. Cell. Neurosci. 17:97-106(2001).
[4]
INTERACTION WITH NOL3.
PubMed=17998337; DOI=10.1128/MCB.00738-07;
Li Y.Z., Lu D.Y., Tan W.Q., Wang J.X., Li P.F.;
"p53 initiates apoptosis by transcriptionally targeting the
antiapoptotic protein ARC.";
Mol. Cell. Biol. 28:564-574(2008).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-135 AND
SER-156, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Promotes cell death. Successfully competes for the
binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level
of heterodimerization of these proteins with BAX. Can reverse the
death repressor activity of Bcl-X(L), but not that of Bcl-2 (By
similarity). Appears to act as a link between growth factor
receptor signaling and the apoptotic pathways. {ECO:0000250}.
-!- SUBUNIT: Forms heterodimers with the anti-apoptotic proteins, Bcl-
X(L), Bcl-2 and Bcl-W. Also binds protein S100A10. The Ser-
113/Ser-137 phosphorylated form binds 14-3-3 proteins. Interacts
with AKT1 and PIM3 (By similarity). Interacts with HIF3A (via C-
terminus domain); the interaction reduces the binding between BAD
and BAX (By similarity). Interacts (via BH3 domain) with NOL3 (via
CARD domain); preventing the association of BAD with BCL2
(PubMed:17998337). {ECO:0000250|UniProtKB:Q61337,
ECO:0000269|PubMed:17998337}.
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm
{ECO:0000250|UniProtKB:Q61337}. Note=Colocalizes with HIF3A in the
cytoplasm. Upon phosphorylation, locates to the cytoplasm.
{ECO:0000250|UniProtKB:Q61337}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Alpha;
IsoId=O35147-1; Sequence=Displayed;
Name=Beta;
IsoId=O35147-2; Sequence=VSP_000534;
-!- TISSUE SPECIFICITY: Expressed in all tissues tested, including
brain, liver, spleen and heart. In the brain, restricted to
epithelial cells of the choroid plexus. Isoform alpha is the more
abundant form.
-!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX
for their pro-apoptotic activity and for their interaction with
anti-apoptotic members of the Bcl-2 family.
-!- PTM: Phosphorylated at one or more of Ser-113, Ser-137, Ser-156
and Ser-171 in response to survival stimuli, which blocks its pro-
apoptotic activity. Phosphorylation on Ser-137 or Ser-113 promotes
heterodimerization with 14-3-3 proteins. This interaction then
facilitates the phosphorylation at Ser-156, a site within the BH3
motif, leading to the release of Bcl-X(L) and the promotion of
cell survival. Ser-137 is the major site of AKT/PKB
phosphorylation, Ser-156 the major site of protein kinase A (CAPK)
phosphorylation.
-!- PTM: Methylation at Arg-132 and Arg-134 by PRMT1 inhibits Akt-
mediated phosphorylation at Ser-137. {ECO:0000250}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- CAUTION: The protein name 'Bcl2 antagonist of cell death' may be
misleading. The protein antagonises Bcl2-mediated repression of
cell death, hence it promotes apoptosis. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF003523; AAC53374.1; -; mRNA.
EMBL; AF031227; AAC15100.1; -; mRNA.
EMBL; AF279910; AAF91427.1; -; mRNA.
EMBL; AF279911; AAF91428.1; -; mRNA.
RefSeq; NP_073189.1; NM_022698.1. [O35147-1]
RefSeq; XP_006230958.1; XM_006230896.3. [O35147-2]
UniGene; Rn.36696; -.
ProteinModelPortal; O35147; -.
SMR; O35147; -.
BioGrid; 249177; 3.
DIP; DIP-29862N; -.
ELM; O35147; -.
MINT; MINT-206504; -.
STRING; 10116.ENSRNOP00000061855; -.
iPTMnet; O35147; -.
PhosphoSitePlus; O35147; -.
PaxDb; O35147; -.
PRIDE; O35147; -.
Ensembl; ENSRNOT00000028712; ENSRNOP00000028712; ENSRNOG00000021147. [O35147-1]
GeneID; 64639; -.
KEGG; rno:64639; -.
UCSC; RGD:620103; rat. [O35147-1]
CTD; 572; -.
RGD; 620103; Bad.
eggNOG; ENOG410IXUQ; Eukaryota.
eggNOG; ENOG410Y2J3; LUCA.
GeneTree; ENSGT00390000010740; -.
HOGENOM; HOG000095169; -.
HOVERGEN; HBG001653; -.
InParanoid; O35147; -.
KO; K02158; -.
OMA; IQSWWDR; -.
OrthoDB; EOG091G0Z5T; -.
PhylomeDB; O35147; -.
TreeFam; TF102001; -.
Reactome; R-RNO-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-RNO-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members.
Reactome; R-RNO-193648; NRAGE signals death through JNK.
PRO; PR:O35147; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000021147; -.
Genevisible; O35147; RN.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0071889; F:14-3-3 protein binding; IDA:RGD.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0043422; F:protein kinase B binding; IPI:RGD.
GO; GO:0030346; F:protein phosphatase 2B binding; IPI:RGD.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0046031; P:ADP metabolic process; ISS:UniProtKB.
GO; GO:0046034; P:ATP metabolic process; ISS:UniProtKB.
GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IEA:Ensembl.
GO; GO:0071247; P:cellular response to chromate; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071396; P:cellular response to lipid; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071316; P:cellular response to nicotine; ISS:UniProtKB.
GO; GO:0021987; P:cerebral cortex development; IEP:RGD.
GO; GO:0019221; P:cytokine-mediated signaling pathway; 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:0006007; P:glucose catabolic process; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0045918; P:negative regulation of cytolysis; IEA:Ensembl.
GO; GO:0046931; P:pore complex assembly; ISS:UniProtKB.
GO; GO:0060139; P:positive regulation of apoptotic process by virus; IEA:Ensembl.
GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0033133; P:positive regulation of glucokinase activity; ISS:UniProtKB.
GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:1902220; P:positive regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISS:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; IDA:RGD.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
GO; GO:2000078; P:positive regulation of type B pancreatic cell development; ISS:UniProtKB.
GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:UniProtKB.
GO; GO:0001836; P:release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0034201; P:response to oleic acid; 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:0032570; P:response to progesterone; IEP:RGD.
GO; GO:0033574; P:response to testosterone; IEP:RGD.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
GO; GO:0019050; P:suppression by virus of host apoptotic process; IEA:Ensembl.
GO; GO:0044342; P:type B pancreatic cell proliferation; ISS:UniProtKB.
InterPro; IPR018868; BAD.
PANTHER; PTHR28540; PTHR28540; 1.
Pfam; PF10514; Bcl-2_BAD; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome; Cytoplasm;
Membrane; Methylation; Mitochondrion; Mitochondrion outer membrane;
Phosphoprotein; Reference proteome.
CHAIN 1 205 Bcl2-associated agonist of cell death.
/FTId=PRO_0000143105.
MOTIF 148 162 BH3.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:Q92934}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000250|UniProtKB:Q92934}.
MOD_RES 132 132 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:Q92934}.
MOD_RES 134 134 Asymmetric dimethylarginine; by PRMT1.
{ECO:0000250|UniProtKB:Q92934}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 137 137 Phosphoserine; by PKA, PKB, PAK1,
RPS6KA1, RPS6KB1 and PKC/PRKCQ.
{ECO:0000250|UniProtKB:Q61337}.
MOD_RES 156 156 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000250|UniProtKB:Q92934}.
VAR_SEQ 166 205 LPRPKSAGTATQMRQSASWTRIIQSWWDRNLGKGGSTPSQ
-> EELTYSVEFLPVRAIAMEGWPLLWSFQSFPHTLPPTPP
EVAMFPLRYWTALRRLC (in isoform Beta).
{ECO:0000303|PubMed:11161472}.
/FTId=VSP_000534.
MUTAGEN 113 113 S->A: No effect on heterodimerization
with 14-3-3 proteins.
{ECO:0000269|PubMed:9369453}.
MUTAGEN 137 137 S->A: No heterodimerization with 14-3-3
proteins. No effect on heterodimerization
with BCL2 nor with protein P11.
{ECO:0000269|PubMed:9369453}.
CONFLICT 29 34 SDAGGR -> ERRGRK (in Ref. 1; AAC53374).
{ECO:0000305}.
SEQUENCE 205 AA; 22228 MW; 7AFA71DAE9CF4A81 CRC64;
MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE PSEQEDASTT
DRGLGPSLTE DQPGPYLAPG LLGSIVQQQP GQAANNSHHG GAGTMETRSR HSSYPAGTEE
DEGMEEELSP FRGRSRSAPP NLWAAQRYGR ELRRMSDEFE GSFKGLPRPK SAGTATQMRQ
SASWTRIIQS WWDRNLGKGG STPSQ


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