ID B2L11_RAT Reviewed; 196 AA.
AC O88498; O88497; Q9WUI8;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 24-JAN-2024, entry version 165.
DE RecName: Full=Bcl-2-like protein 11;
DE Short=Bcl2-L-11;
DE AltName: Full=Bcl-2-related ovarian death protein;
DE AltName: Full=Bcl2-interacting mediator of cell death;
GN Name=Bcl2l11; Synonyms=Bim, Bod;
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], FUNCTION, INTERACTION WITH BCL-2 PROTEINS, AND
RP TISSUE SPECIFICITY (ISOFORMS BOD-L; BOD-M AND BOD-S).
RC TISSUE=Ovary;
RX PubMed=9731710; DOI=10.1210/mend.12.9.0166;
RA Hsu S.Y., Lin P., Hsueh A.J.W.;
RT "BOD (Bcl-2-related ovarian death gene) is an ovarian BH3 domain-containing
RT proapoptotic Bcl-2 protein capable of dimerization with diverse
RT antiapoptotic Bcl-2 members.";
RL Mol. Endocrinol. 12:1432-1440(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BIML).
RA Chen D., Simon R.P., Chen J.;
RT "Cloning of rat bimEL and bimL, and their differential expression in
RT ischemia and normal rat brain.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH DYNLL1; TRIM2 AND YWHAZ, AND UBIQUITINATION.
RX PubMed=21478148; DOI=10.1074/jbc.m110.197707;
RA Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P.,
RA Henshall D.C., Morris K.T., Simon R.P., Meller R.;
RT "Identification of a novel Bcl-2-interacting mediator of cell death (Bim)
RT E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in
RT rapid ischemic tolerance-induced neuroprotection.";
RL J. Biol. Chem. 286:19331-19339(2011).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-83, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Induces apoptosis and anoikis. {ECO:0000269|PubMed:9731710}.
CC -!- SUBUNIT: Forms heterodimers with a number of antiapoptotic Bcl-2
CC proteins, including MCL1, BCL2, BCL2L1 isoform Bcl-X(L), BCL2A1/BFL-1,
CC and BCL2L2/BCLW. Does not heterodimerize with proapoptotic proteins
CC such as BAD, BOK or BAK (PubMed:9731710). Identified in a complex
CC containing BCL2L11, DYNLL1 and BCL2L1 isoform Bcl-X(L); BH3 integrity
CC is required for BCL2L1-binding. Interacts with YWHAZ. When
CC phosphorylated, interacts with TRIM2; this interaction is associated
CC with ubiquitination and degradation (PubMed:21478148). Interacts (via
CC BH3) with MCL1; this interaction may sequester BCL2L11 and prevent its
CC pro-apoptotic activity (PubMed:9731710). When phosphorylated, isoform
CC BimEL interacts with USP27X; this interaction leads to BCL2L11
CC deubiquitination and stabilization (By similarity). Interacts with
CC GIMAP5 (By similarity). Interacts with BCL2L10/BCL-B (By similarity).
CC {ECO:0000250|UniProtKB:O43521, ECO:0000250|UniProtKB:O54918,
CC ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:9731710}.
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC Mitochondrion {ECO:0000250}. Note=Associated with intracytoplasmic
CC membranes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=BOD-L;
CC IsoId=O88498-1; Sequence=Displayed;
CC Name=BimL;
CC IsoId=O88498-2; Sequence=VSP_000538;
CC Name=BOD-M;
CC IsoId=O88498-3; Sequence=VSP_000539;
CC Name=BOD-S;
CC IsoId=O88498-4; Sequence=VSP_018668;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: The BH3 motif is required for the interaction with Bcl-2
CC proteins and cytotoxicity. {ECO:0000250|UniProtKB:O54918}.
CC -!- PTM: Phosphorylation at Ser-65 by MAPK1/MAPK3 leads interaction with
CC TRIM2 and ubiquitination, followed by proteasomal degradation.
CC Deubiquitination catalyzed by USP27X stabilizes the protein.
CC {ECO:0000250|UniProtKB:O54918}.
CC -!- PTM: Ubiquitination by TRIM2 following phosphorylation by MAPK1/MAPK3
CC leads to proteasomal degradation (PubMed:21478148). Conversely,
CC deubiquitination catalyzed by USP27X stabilizes the protein (By
CC similarity). {ECO:0000250|UniProtKB:O54918,
CC ECO:0000269|PubMed:21478148}.
CC -!- MISCELLANEOUS: [Isoform BOD-S]: Produced by alternative initiation at
CC Met-104 of isoform BOD-L. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; AF065433; AAC23595.1; -; mRNA.
DR EMBL; AF065431; AAC23593.1; -; mRNA.
DR EMBL; AF065432; AAC23594.1; -; mRNA.
DR EMBL; AF136927; AAD26594.1; -; mRNA.
DR RefSeq; NP_072134.1; NM_022612.1.
DR RefSeq; NP_741985.1; NM_171988.2. [O88498-1]
DR RefSeq; NP_741986.1; NM_171989.1.
DR AlphaFoldDB; O88498; -.
DR SMR; O88498; -.
DR BioGRID; 249128; 4.
DR ComplexPortal; CPX-2026; BIM:BCL-XL complex.
DR ComplexPortal; CPX-2035; BIM:BCL-2 complex.
DR ELM; O88498; -.
DR IntAct; O88498; 5.
DR STRING; 10116.ENSRNOP00000039006; -.
DR iPTMnet; O88498; -.
DR PhosphoSitePlus; O88498; -.
DR PaxDb; 10116-ENSRNOP00000039006; -.
DR GeneID; 64547; -.
DR KEGG; rno:64547; -.
DR UCSC; RGD:628774; rat. [O88498-1]
DR AGR; RGD:628774; -.
DR CTD; 10018; -.
DR RGD; 628774; Bcl2l11.
DR VEuPathDB; HostDB:ENSRNOG00000016551; -.
DR eggNOG; ENOG502S0DF; Eukaryota.
DR HOGENOM; CLU_104244_0_0_1; -.
DR InParanoid; O88498; -.
DR OrthoDB; 4327858at2759; -.
DR PhylomeDB; O88498; -.
DR Reactome; R-RNO-111446; Activation of BIM 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-193648; NRAGE signals death through JNK.
DR PRO; PR:O88498; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000016551; Expressed in thymus and 18 other cell types or tissues.
DR Genevisible; O88498; RN.
DR GO; GO:0097136; C:Bcl-2 family protein complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:1902263; P:apoptotic process involved in embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0001782; P:B cell homeostasis; ISO:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0048066; P:developmental pigmentation; ISO:RGD.
DR GO; GO:0043583; P:ear development; ISO:RGD.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0001776; P:leukocyte homeostasis; ISO:RGD.
DR GO; GO:0070227; P:lymphocyte apoptotic process; ISO:RGD.
DR GO; GO:0002260; P:lymphocyte homeostasis; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:0030879; P:mammary gland development; ISO:RGD.
DR GO; GO:0007127; P:meiosis I; IBA:GO_Central.
DR GO; GO:0002262; P:myeloid cell homeostasis; ISO:RGD.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0034263; P:positive regulation of autophagy in response to ER overload; IMP:RGD.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
DR GO; GO:2000271; P:positive regulation of fibroblast apoptotic process; ISO:RGD.
DR GO; GO:0070230; P:positive regulation of lymphocyte apoptotic process; ISO:RGD.
DR GO; GO:1902110; P:positive regulation of mitochondrial membrane permeability involved in apoptotic process; ISO:RGD.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
DR GO; GO:0070234; P:positive regulation of T cell apoptotic process; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR GO; GO:0048070; P:regulation of developmental pigmentation; ISO:RGD.
DR GO; GO:0046620; P:regulation of organ growth; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0048536; P:spleen development; ISO:RGD.
DR GO; GO:0070231; P:T cell apoptotic process; ISO:RGD.
DR GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
DR GO; GO:0070242; P:thymocyte apoptotic process; ISO:RGD.
DR GO; GO:0048538; P:thymus development; ISO:RGD.
DR GO; GO:0035148; P:tube formation; ISO:RGD.
DR InterPro; IPR014771; Apoptosis_Bim_N.
DR InterPro; IPR017288; Bcl-2-like_11.
DR InterPro; IPR015040; Bcl-x_interacting_BH3_dom.
DR PANTHER; PTHR12044:SF9; BCL-2-LIKE PROTEIN 11; 1.
DR PANTHER; PTHR12044; BCL2 INTERACTING MEDIATOR OF CELL DEATH; 1.
DR Pfam; PF08945; Bclx_interact; 1.
DR Pfam; PF06773; Bim_N; 1.
DR PIRSF; PIRSF037827; Bcl-2-like_p11; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Alternative splicing; Apoptosis; Membrane;
KW Mitochondrion; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..196
FT /note="Bcl-2-like protein 11"
FT /id="PRO_0000002814"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 90..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 146..160
FT /note="BH3"
FT MOD_RES 65
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O43521"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43521"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform BOD-S)"
FT /evidence="ECO:0000305"
FT /id="VSP_018668"
FT VAR_SEQ 42..127
FT /note="Missing (in isoform BOD-M)"
FT /evidence="ECO:0000305"
FT /id="VSP_000539"
FT VAR_SEQ 42..97
FT /note="Missing (in isoform BimL)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_000538"
FT CONFLICT 136
FT /note="E -> D (in Ref. 1; AAC23594)"
FT /evidence="ECO:0000305"
SQ 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
//
