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Bcl-2-like protein 10 (Bcl2-L-10) (Anti-apoptotic protein Boo) (Apoptosis regulator Bcl-B) (Bcl-2 homolog Diva)

 B2L10_MOUSE             Reviewed;         191 AA.
Q9Z0F3; Q3ULP5; Q7TPY8;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
12-SEP-2018, entry version 130.
RecName: Full=Bcl-2-like protein 10;
Short=Bcl2-L-10;
AltName: Full=Anti-apoptotic protein Boo;
AltName: Full=Apoptosis regulator Bcl-B;
AltName: Full=Bcl-2 homolog Diva;
Name=Bcl2l10; Synonyms=Boo, Diva;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X DBA/2; TISSUE=Ovary;
PubMed=9878060; DOI=10.1093/emboj/18.1.167;
Song Q.Z., Kuang Y.P., Dixit V.M., Vincenz C.;
"Boo, a novel negative regulator of cell death, interacts with Apaf-
1.";
EMBO J. 18:167-178(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X DBA/2;
PubMed=9829980; DOI=10.1074/jbc.273.49.32479;
Inohara N., Gourley T.S., Carrio R., Muniz M., Merino J., Garcia I.,
Koseki T., Hu Y., Chen S., Nunez G.;
"Diva, a Bcl-2 homologue that binds directly to Apaf-1 and induces
BH3-independent cell death.";
J. Biol. Chem. 273:32479-32486(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Egg;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Promotes cell survival. Suppresses apoptosis.
-!- SUBUNIT: Binds to Bcl-2, Bcl-X and BAX. Interacts with APAF1.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Nucleus
membrane {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in multiple embryonic tissues.
Restricted to the ovary and testis in adult mice.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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EMBL; AF102501; AAD08703.1; -; mRNA.
EMBL; AF067660; AAC83150.1; -; mRNA.
EMBL; AK136172; BAE22856.1; -; mRNA.
EMBL; AK145385; BAE26403.1; -; mRNA.
EMBL; AK162127; BAE36742.1; -; mRNA.
EMBL; CH466522; EDL26315.1; -; Genomic_DNA.
EMBL; BC052690; AAH52690.1; -; mRNA.
CCDS; CCDS23341.1; -.
RefSeq; NP_038507.1; NM_013479.2.
UniGene; Mm.25988; -.
PDB; 2KUA; NMR; -; A=1-165.
PDBsum; 2KUA; -.
ProteinModelPortal; Q9Z0F3; -.
SMR; Q9Z0F3; -.
MINT; Q9Z0F3; -.
STRING; 10090.ENSMUSP00000034709; -.
PhosphoSitePlus; Q9Z0F3; -.
PaxDb; Q9Z0F3; -.
PRIDE; Q9Z0F3; -.
DNASU; 12049; -.
Ensembl; ENSMUST00000034709; ENSMUSP00000034709; ENSMUSG00000032191.
GeneID; 12049; -.
KEGG; mmu:12049; -.
UCSC; uc012gwy.1; mouse.
CTD; 10017; -.
MGI; MGI:1330841; Bcl2l10.
eggNOG; ENOG410J2PB; Eukaryota.
eggNOG; ENOG4112AS5; LUCA.
GeneTree; ENSGT00640000091607; -.
HOGENOM; HOG000059275; -.
HOVERGEN; HBG050646; -.
InParanoid; Q9Z0F3; -.
KO; K18451; -.
OMA; QAQGGWD; -.
OrthoDB; EOG091G0KGL; -.
PhylomeDB; Q9Z0F3; -.
TreeFam; TF334762; -.
EvolutionaryTrace; Q9Z0F3; -.
PRO; PR:Q9Z0F3; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032191; Expressed in 44 organ(s), highest expression level in primary oocyte.
CleanEx; MM_BCL2L10; -.
Genevisible; Q9Z0F3; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0089720; F:caspase binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR036834; Blc2-like_sf.
InterPro; IPR026298; Blc2_fam.
PANTHER; PTHR11256; PTHR11256; 1.
Pfam; PF00452; Bcl-2; 1.
SUPFAM; SSF56854; SSF56854; 1.
PROSITE; PS50062; BCL2_FAMILY; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Membrane; Mitochondrion;
Nucleus; Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 191 Bcl-2-like protein 10.
/FTId=PRO_0000143069.
TRANSMEM 166 183 Helical. {ECO:0000255}.
MOTIF 79 98 BH1.
MOTIF 144 155 BH2.
CONFLICT 10 10 E -> G (in Ref. 5; AAH52690).
{ECO:0000305}.
STRAND 3 5 {ECO:0000244|PDB:2KUA}.
HELIX 9 24 {ECO:0000244|PDB:2KUA}.
HELIX 37 61 {ECO:0000244|PDB:2KUA}.
TURN 62 64 {ECO:0000244|PDB:2KUA}.
HELIX 67 77 {ECO:0000244|PDB:2KUA}.
STRAND 81 83 {ECO:0000244|PDB:2KUA}.
HELIX 87 100 {ECO:0000244|PDB:2KUA}.
HELIX 120 136 {ECO:0000244|PDB:2KUA}.
HELIX 139 147 {ECO:0000244|PDB:2KUA}.
HELIX 150 157 {ECO:0000244|PDB:2KUA}.
STRAND 161 163 {ECO:0000244|PDB:2KUA}.
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


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