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Bcl-2-like protein 11 (Bcl2-L-11) (Bcl-2-related ovarian death protein) (Bcl2-interacting mediator of cell death)

 B2L11_RAT               Reviewed;         196 AA.
O88498; O88497; Q9WUI8;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
23-MAY-2018, entry version 136.
RecName: Full=Bcl-2-like protein 11;
Short=Bcl2-L-11;
AltName: Full=Bcl-2-related ovarian death protein;
AltName: Full=Bcl2-interacting mediator of cell death;
Name=Bcl2l11; Synonyms=Bim, Bod;
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], FUNCTION, INTERACTION WITH BCL-2 PROTEINS,
AND TISSUE SPECIFICITY (ISOFORMS BOD-L; BOD-M AND BOD-S).
TISSUE=Ovary;
PubMed=9731710; DOI=10.1210/mend.12.9.0166;
Hsu S.Y., Lin P., Hsueh A.J.W.;
"BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-
containing proapoptotic Bcl-2 protein capable of dimerization with
diverse antiapoptotic Bcl-2 members.";
Mol. Endocrinol. 12:1432-1440(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIML).
Chen D., Simon R.P., Chen J.;
"Cloning of rat bimEL and bimL, and their differential expression in
ischemia and normal rat brain.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
INTERACTION WITH DYNLL1; TRIM2 AND YWHAZ, AND UBIQUITINATION.
PubMed=21478148; DOI=10.1074/jbc.M110.197707;
Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M.,
Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R.;
"Identification of a novel Bcl-2-interacting mediator of cell death
(Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and
its role in rapid ischemic tolerance-induced neuroprotection.";
J. Biol. Chem. 286:19331-19339(2011).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-83, 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: Induces apoptosis and anoikis.
{ECO:0000269|PubMed:9731710}.
-!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2
proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L),
BCL2A1/BFL-1, and BCL2L2/BCLW. Does not heterodimerize with
proapoptotic proteins such as BAD, BOK or BAK (PubMed:9731710).
Identified in a complex containing BCL2L11, DYNLL1 and BCL2L1
isoform Bcl-X(L); BH3 integrity is required for BCL2L1-binding.
Interacts with YWHAZ. When phosphorylated, interacts with TRIM2;
this interaction is associated with ubiquitination and degradation
(PubMed:21478148). Interacts (via BH3) with MCL1; this interaction
may sequester BCL2L11 and prevent its pro-apoptotic activity
(PubMed:9731710). When phosphorylated, isoform BimEL interacts
with USP27X; this interaction leads to BCL2L11 deubiquitination
and stabilization (By similarity). {ECO:0000250|UniProtKB:O54918,
ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:9731710}.
-!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic
membranes. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=4;
Name=BOD-L;
IsoId=O88498-1; Sequence=Displayed;
Name=BimL;
IsoId=O88498-2; Sequence=VSP_000538;
Name=BOD-M;
IsoId=O88498-3; Sequence=VSP_000539;
Name=BOD-S;
IsoId=O88498-4; Sequence=VSP_018668;
Note=Produced by alternative initiation at Met-104 of isoform
BOD-L.;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DOMAIN: The BH3 motif is required for the interaction with Bcl-2
proteins and cytotoxicity. {ECO:0000250|UniProtKB:O54918}.
-!- PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction
with TRIM2 and ubiquitination, followed by proteasomal
degradation. Deubiquitination catalyzed by USP27X stabilizes the
protein. {ECO:0000250|UniProtKB:O54918}.
-!- PTM: Ubiquitination by TRIM2 following phosphorylation by
MAPK1/MAPK3 leads to proteasomal degradation (PubMed:21478148).
Conversely, deubiquitination catalyzed by USP27X stabilizes the
protein (By similarity). {ECO:0000250|UniProtKB:O54918,
ECO:0000269|PubMed:21478148}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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EMBL; AF065433; AAC23595.1; -; mRNA.
EMBL; AF065431; AAC23593.1; -; mRNA.
EMBL; AF065432; AAC23594.1; -; mRNA.
EMBL; AF136927; AAD26594.1; -; mRNA.
RefSeq; NP_072134.1; NM_022612.1. [O88498-2]
RefSeq; NP_741985.1; NM_171988.2. [O88498-1]
RefSeq; NP_741986.1; NM_171989.1.
UniGene; Rn.82709; -.
ProteinModelPortal; O88498; -.
SMR; O88498; -.
BioGrid; 249128; 4.
ELM; O88498; -.
IntAct; O88498; 5.
STRING; 10116.ENSRNOP00000039006; -.
iPTMnet; O88498; -.
PhosphoSitePlus; O88498; -.
PaxDb; O88498; -.
PRIDE; O88498; -.
Ensembl; ENSRNOT00000022596; ENSRNOP00000022596; ENSRNOG00000016551. [O88498-2]
Ensembl; ENSRNOT00000051069; ENSRNOP00000039006; ENSRNOG00000016551. [O88498-1]
GeneID; 64547; -.
KEGG; rno:64547; -.
UCSC; RGD:628774; rat. [O88498-1]
CTD; 10018; -.
RGD; 628774; Bcl2l11.
eggNOG; ENOG410IZKS; Eukaryota.
eggNOG; ENOG410Y8GB; LUCA.
GeneTree; ENSGT00390000003178; -.
InParanoid; O88498; -.
KO; K16341; -.
OMA; AEDHPQM; -.
OrthoDB; EOG091G0XD3; -.
PhylomeDB; O88498; -.
Reactome; R-RNO-111446; Activation of BIM 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:O88498; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000016551; -.
Genevisible; O88498; RN.
GO; GO:0097136; C:Bcl-2 family protein complex; IEA:Ensembl.
GO; GO:0005868; C:cytoplasmic dynein complex; IEA:Ensembl.
GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0001783; P:B cell apoptotic process; IEA:Ensembl.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0007160; P:cell-matrix adhesion; IEA:Ensembl.
GO; GO:0060154; P:cellular process regulating host cell cycle in response to virus; IEA:Ensembl.
GO; GO:0048066; P:developmental pigmentation; IEA:Ensembl.
GO; GO:0043583; P:ear development; IEA:Ensembl.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
GO; GO:0060139; P:positive regulation of apoptotic process by virus; IEA:Ensembl.
GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
GO; GO:0010942; P:positive regulation of cell death; IDA:RGD.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; IEA:Ensembl.
GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0032464; P:positive regulation of protein homooligomerization; IEA:Ensembl.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; IEA:Ensembl.
GO; GO:0048563; P:post-embryonic animal organ morphogenesis; IEA:Ensembl.
GO; GO:0048070; P:regulation of developmental pigmentation; IEA:Ensembl.
GO; GO:0046620; P:regulation of organ growth; IEA:Ensembl.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0048536; P:spleen development; IEA:Ensembl.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
GO; GO:0048538; P:thymus development; IEA:Ensembl.
GO; GO:0035148; P:tube formation; IEA:Ensembl.
InterPro; IPR014771; Apoptosis_Bim_N.
InterPro; IPR017288; Bcl-2-like_11.
InterPro; IPR015040; Bcl-x_interacting_BH3_dom.
Pfam; PF08945; Bclx_interact; 1.
Pfam; PF06773; Bim_N; 1.
PIRSF; PIRSF037827; Bcl-2-like_p11; 1.
1: Evidence at protein level;
Alternative initiation; Alternative splicing; Apoptosis;
Complete proteome; Membrane; Mitochondrion; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 196 Bcl-2-like protein 11.
/FTId=PRO_0000002814.
MOTIF 146 160 BH3.
MOD_RES 65 65 Phosphoserine; by MAPK.
{ECO:0000250|UniProtKB:O43521}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000250|UniProtKB:O43521}.
VAR_SEQ 1 103 Missing (in isoform BOD-S).
{ECO:0000305}.
/FTId=VSP_018668.
VAR_SEQ 42 127 Missing (in isoform BOD-M).
{ECO:0000305}.
/FTId=VSP_000539.
VAR_SEQ 42 97 Missing (in isoform BimL).
{ECO:0000303|Ref.2}.
/FTId=VSP_000538.
CONFLICT 136 136 E -> D (in Ref. 1; AAC23594).
{ECO:0000305}.
SEQUENCE 196 AA; 22056 MW; B4D2146F9C0B37A0 CRC64;
MAKQPSDVNS ECDREGGQLQ PAERPPQLRP GAPTSLQTES QGNPDGEGDR CPHGSPQGPL
APPASPGPFA TRSPLFIFVR RSSLLSRSSS GYFSFDTDRS PAPMSCDKST QTPSPPCQAF
NHYLSAMASI RQSQEEPEDL RPEIRIAQEL RRIGDEFNET YTRRAFANDY REAEDHPQMV
ILQLLRFIFR LVWRRH


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