B2L10_RAT
ID B2L10_RAT Reviewed; 185 AA.
AC Q99M66;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Bcl-2-like protein 10 {ECO:0000312|RGD:621015};
DE Short=Bcl2-L-10 {ECO:0000250|UniProtKB:Q9HD36};
DE AltName: Full=Anti-apoptotic protein Boo {ECO:0000250|UniProtKB:Q9Z0F3};
DE AltName: Full=Apoptosis regulator Bcl-B {ECO:0000250|UniProtKB:Q9HD36};
GN Name=Bcl2l10 {ECO:0000303|PubMed:17532299};
GN Synonyms=Bcl-b {ECO:0000250|UniProtKB:Q9HD36},
GN Boo {ECO:0000250|UniProtKB:Q9Z0F3}, Diva {ECO:0000250|UniProtKB:Q9Z0F3};
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=12787069; DOI=10.1046/j.1471-4159.2003.01795.x;
RA Itoh T., Itoh A., Pleasure D.;
RT "Bcl-2-related protein family gene expression during oligodendroglial
RT differentiation.";
RL J. Neurochem. 85:1500-1512(2003).
RN [2]
RP INTERACTION WITH NME2.
RX PubMed=17532299; DOI=10.1016/j.bbrc.2007.05.090;
RA Kang Y., Lee D.C., Han J., Yoon S., Won M., Yeom J.H., Seong M.J., Ko J.J.,
RA Lee K.A., Lee K., Bae J.;
RT "NM23-H2 involves in negative regulation of Diva and Bcl2L10 in apoptosis
RT signaling.";
RL Biochem. Biophys. Res. Commun. 359:76-82(2007).
CC -!- FUNCTION: Promotes cell survival by suppressing apoptosis induced by
CC BAX but not BAK (By similarity). Increases binding of AHCYL1/IRBIT to
CC ITPR1 (By similarity). Reduces ITPR1-mediated calcium release from the
CC endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal
CC cellular conditions (By similarity). Under apoptotic stress conditions,
CC dissociates from ITPR1 and is displaced from mitochondria-associated
CC endoplasmic reticulum membranes, leading to increased Ca(2+) transfer
CC to mitochondria which promotes apoptosis (By similarity). Required for
CC the correct formation of the microtubule organizing center during
CC oocyte cell division, potentially via regulation of protein abundance
CC and localization of other microtubule organizing center components such
CC as AURKA and TPX2 (By similarity). {ECO:0000250|UniProtKB:Q9HD36,
CC ECO:0000250|UniProtKB:Q9Z0F3}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q9HD36};
CC -!- SUBUNIT: Interacts with BAX (By similarity). Interacts with BCL2,
CC BCL2L1/BCLX (By similarity). Interacts with APAF1 (By similarity).
CC Interacts with ITPR1, ITPR2 and ITPR3; the interaction with ITPR1 is
CC increased in the presence of AHCLY1 (By similarity). Interacts with
CC AHCYL1 (By similarity). Interacts with HIP1R (via ENTH and I/LWEQ
CC domains) (By similarity). Interacts with CASP9 (By similarity).
CC Interacts with BCL2L11/BIM (By similarity). Interacts with BIK (By
CC similarity). Interacts with UBQLN4 (By similarity). Interacts with
CC NME2/NM23-H2 (PubMed:17532299). Interacts with and PMAIP1/NOXA (By
CC similarity). Interacts with TPX2 (By similarity). Interacts with
CC UBQLN1; in the cytoplasm (By similarity). Interacts (via BH1 domain)
CC with BECN1 (By similarity). {ECO:0000250|UniProtKB:Q9HD36,
CC ECO:0000250|UniProtKB:Q9Z0F3, ECO:0000269|PubMed:17532299}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9HD36}.
CC Nucleus membrane {ECO:0000250|UniProtKB:Q9HD36}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9HD36}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:Q9Z0F3}. Note=Localizes to mitochondria-
CC associated endoplasmic reticulum membranes (MAMs) (By similarity).
CC Localization to MAMs is greatly reduced under apoptotic stress
CC conditions (By similarity). {ECO:0000250|UniProtKB:Q9HD36}.
CC -!- TISSUE SPECIFICITY: Expressed in oligodendroglial lineage cells.
CC {ECO:0000269|PubMed:12787069}.
CC -!- PTM: Monoubiquitinated by UBQLN1; results in stabilization of BCL2L10
CC protein abundance and in relocalization from mitochondria to cytoplasm.
CC {ECO:0000250|UniProtKB:Q9HD36}.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; AY029163; AAK31792.1; -; mRNA.
DR RefSeq; NP_446185.1; NM_053733.1.
DR AlphaFoldDB; Q99M66; -.
DR SMR; Q99M66; -.
DR STRING; 10116.ENSRNOP00000012409; -.
DR PaxDb; Q99M66; -.
DR Ensembl; ENSRNOT00000012409; ENSRNOP00000012409; ENSRNOG00000009308.
DR GeneID; 114552; -.
DR KEGG; rno:114552; -.
DR UCSC; RGD:621015; rat.
DR CTD; 10017; -.
DR RGD; 621015; Bcl2l10.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_122207_0_0_1; -.
DR InParanoid; Q99M66; -.
DR OMA; GRKMSCG; -.
DR OrthoDB; 1557685at2759; -.
DR PhylomeDB; Q99M66; -.
DR TreeFam; TF334762; -.
DR PRO; PR:Q99M66; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000009308; Expressed in ovary and 3 other tissues.
DR Genevisible; Q99M66; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0089720; F:caspase binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01258; BH2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Membrane;
KW Mitochondrion; Nucleus; Reference proteome; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..185
FT /note="Bcl-2-like protein 10"
FT /id="PRO_0000378194"
FT TRANSMEM 160..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 76..95
FT /note="BH1"
FT MOTIF 138..149
FT /note="BH2"
SQ SEQUENCE 185 AA; 21859 MW; 2EB9B94C8EC106A2 CRC64;
MGDPLQDRTR RLLTDYILFC ARAPNTPEPL PTSVEAALLR SVTSQIQQEH QDLFNSFRDY
QGNRLELVTQ MADELLSNDQ EFNWGRLVML LAFVGTLMNQ DRTVKRRRDQ RNRLLLERDC
YLIVSLLYNR LTGRHRSWLE AHGGWDGFCQ FFKNPLPPGF WRRLLIRAIL SCFFATAIFY
IWKCL
