B2L10_MOUSE
ID B2L10_MOUSE Reviewed; 191 AA.
AC Q9Z0F3; Q3ULP5; Q7TPY8;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Bcl-2-like protein 10 {ECO:0000312|MGI:MGI:1330841};
DE Short=Bcl2-L-10 {ECO:0000250|UniProtKB:Q9HD36};
DE AltName: Full=Anti-apoptotic protein Boo {ECO:0000303|PubMed:9878060};
DE AltName: Full=Apoptosis regulator Bcl-B {ECO:0000250|UniProtKB:Q9HD36};
DE AltName: Full=Bcl-2 homolog Diva {ECO:0000303|PubMed:9829980};
GN Name=Bcl2l10 {ECO:0000312|MGI:MGI:1330841};
GN Synonyms=Bcl-b {ECO:0000250|UniProtKB:Q9HD36},
GN Boo {ECO:0000303|PubMed:9878060}, Diva {ECO:0000303|PubMed:9829980};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH APAF1, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Ovary;
RX PubMed=9878060; DOI=10.1093/emboj/18.1.167;
RA Song Q.Z., Kuang Y.P., Dixit V.M., Vincenz C.;
RT "Boo, a novel negative regulator of cell death, interacts with Apaf-1.";
RL EMBO J. 18:167-178(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH APAF1, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/2;
RX PubMed=9829980; DOI=10.1074/jbc.273.49.32479;
RA Inohara N., Gourley T.S., Carrio R., Muniz M., Merino J., Garcia I.,
RA Koseki T., Hu Y., Chen S., Nunez G.;
RT "Diva, a Bcl-2 homologue that binds directly to Apaf-1 and induces BH3-
RT independent cell death.";
RL J. Biol. Chem. 273:32479-32486(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
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).
RN [7]
RP FUNCTION, INTERACTION WITH TPX2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=27753540; DOI=10.1080/15384101.2016.1243630;
RA Lee S.Y., Kim E.Y., Kim K.H., Lee K.A.;
RT "Bcl2l10, a new Tpx2 binding partner, is a master regulator of Aurora
RT kinase A in mouse oocytes.";
RL Cell Cycle 15:3296-3305(2016).
RN [8] {ECO:0007744|PDB:2KUA}
RP STRUCTURE BY NMR OF 1-165.
RX PubMed=20455273; DOI=10.1002/prot.22728;
RA Rautureau G.J., Day C.L., Hinds M.G.;
RT "The structure of Boo/Diva reveals a divergent Bcl-2 protein.";
RL Proteins 78:2181-2186(2010).
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 (PubMed:27753540). {ECO:0000250|UniProtKB:Q9HD36,
CC ECO:0000269|PubMed:27753540}.
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 and
CC BCL2L1/BCLX (By similarity). Interacts with APAF1 (PubMed:9878060,
CC PubMed:9829980). Interacts with ITPR1, ITPR2 and ITPR3; the interaction
CC with ITPR1 is increased in the presence of AHCLY1 (By similarity).
CC Interacts with AHCYL1 (By similarity). Interacts with HIP1R (via ENTH
CC and I/LWEQ domains) (By similarity). Interacts with CASP9 (By
CC similarity). Interacts with BCL2L11/BIM (By similarity). Interacts with
CC BIK (By similarity). Interacts with UBQLN4 (By similarity). Interacts
CC with NME2/NM23-H2 (PubMed:17532299). Interacts with PMAIP1/NOXA (By
CC similarity). Interacts with TPX2 (PubMed:27753540). Interacts with
CC UBQLN1; in the cytoplasm (By similarity). Interacts (via BH1 domain)
CC with BECN1 (By similarity). {ECO:0000250|UniProtKB:Q9HD36,
CC ECO:0000269|PubMed:17532299, ECO:0000269|PubMed:27753540,
CC ECO:0000269|PubMed:9829980, ECO:0000269|PubMed:9878060}.
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:0000269|PubMed:27753540}. 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 multiple embryonic tissues
CC (PubMed:9829980). Restricted to the ovary and testis in adult mice
CC (PubMed:9878060, PubMed:9829980). {ECO:0000269|PubMed:9829980,
CC ECO:0000269|PubMed:9878060}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all phases of oocyte maturation;
CC localized at the meiotic spindle and spindle poles during meiosis.
CC {ECO:0000269|PubMed:27753540}.
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; AF102501; AAD08703.1; -; mRNA.
DR EMBL; AF067660; AAC83150.1; -; mRNA.
DR EMBL; AK136172; BAE22856.1; -; mRNA.
DR EMBL; AK145385; BAE26403.1; -; mRNA.
DR EMBL; AK162127; BAE36742.1; -; mRNA.
DR EMBL; CH466522; EDL26315.1; -; Genomic_DNA.
DR EMBL; BC052690; AAH52690.1; -; mRNA.
DR CCDS; CCDS23341.1; -.
DR RefSeq; NP_038507.1; NM_013479.2.
DR PDB; 2KUA; NMR; -; A=1-165.
DR PDBsum; 2KUA; -.
DR AlphaFoldDB; Q9Z0F3; -.
DR BMRB; Q9Z0F3; -.
DR SMR; Q9Z0F3; -.
DR BioGRID; 198324; 1.
DR MINT; Q9Z0F3; -.
DR STRING; 10090.ENSMUSP00000034709; -.
DR PhosphoSitePlus; Q9Z0F3; -.
DR PaxDb; Q9Z0F3; -.
DR PRIDE; Q9Z0F3; -.
DR Antibodypedia; 24926; 240 antibodies from 36 providers.
DR DNASU; 12049; -.
DR Ensembl; ENSMUST00000034709; ENSMUSP00000034709; ENSMUSG00000032191.
DR GeneID; 12049; -.
DR KEGG; mmu:12049; -.
DR UCSC; uc012gwy.1; mouse.
DR CTD; 10017; -.
DR MGI; MGI:1330841; Bcl2l10.
DR VEuPathDB; HostDB:ENSMUSG00000032191; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT00940000164610; -.
DR HOGENOM; CLU_122207_0_0_1; -.
DR InParanoid; Q9Z0F3; -.
DR OMA; GRKMSCG; -.
DR OrthoDB; 1557685at2759; -.
DR PhylomeDB; Q9Z0F3; -.
DR TreeFam; TF334762; -.
DR BioGRID-ORCS; 12049; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Bcl2l10; mouse.
DR EvolutionaryTrace; Q9Z0F3; -.
DR PRO; PR:Q9Z0F3; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9Z0F3; protein.
DR Bgee; ENSMUSG00000032191; Expressed in secondary oocyte and 23 other tissues.
DR Genevisible; Q9Z0F3; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
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; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0089720; F:caspase binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
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; IDA:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IDA:MGI.
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; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Isopeptide bond; Membrane; Mitochondrion; Nucleus; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..191
FT /note="Bcl-2-like protein 10"
FT /id="PRO_0000143069"
FT TRANSMEM 166..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 79..98
FT /note="BH1"
FT MOTIF 144..155
FT /note="BH2"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9HD36"
FT CONFLICT 10
FT /note="E -> G (in Ref. 5; AAH52690)"
FT /evidence="ECO:0000305"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2KUA"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:2KUA"
FT HELIX 37..61
FT /evidence="ECO:0007829|PDB:2KUA"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2KUA"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:2KUA"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2KUA"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:2KUA"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:2KUA"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:2KUA"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:2KUA"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2KUA"
SQ SEQUENCE 191 AA; 22302 MW; 819014E6B2DFE411 CRC64;
MADSQDPLHE RTRRLLSDYI FFCAREPDTP EPPPTSVEAA LLRSVTRQIQ QEHQEFFSSF
CESRGNRLEL VKQMADKLLS KDQDFSWSQL VMLLAFAGTL MNQGPYMAVK QKRDLGNRVI
VTRDCCLIVN FLYNLLMGRR HRARLEALGG WDGFCRFFKN PLPLGFWRRL LIQAFLSGFF
ATAIFFIWKR L
