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Bcl-2-like protein 10 (Bcl2-L-10) (Anti-apoptotic protein NrH) (Apoptosis regulator Bcl-B)

 B2L10_HUMAN             Reviewed;         194 AA.
Q9HD36; Q3SX80; Q52LQ9; Q8TCS9;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
28-FEB-2018, entry version 145.
RecName: Full=Bcl-2-like protein 10;
Short=Bcl2-L-10;
AltName: Full=Anti-apoptotic protein NrH;
AltName: Full=Apoptosis regulator Bcl-B;
Name=BCL2L10; Synonyms=BCLB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=11689480; DOI=10.1093/hmg/10.21.2329;
Zhang H., Holzgreve W., De Geyter C.;
"Bcl2-L-10, a novel anti-apoptotic member of the Bcl-2 family, blocks
apoptosis in the mitochondria death pathway but not in the death
receptor pathway.";
Hum. Mol. Genet. 10:2329-2339(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH BAX.
TISSUE=Liver;
PubMed=11278245; DOI=10.1074/jbc.C000871200;
Ke N., Godzik A., Reed J.C.;
"Bcl-B, a novel Bcl-2 family member that differentially binds and
regulates Bax and Bak.";
J. Biol. Chem. 276:12481-12484(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND INTERACTION WITH BCLX.
PubMed=11593390; DOI=10.1038/sj.onc.1204740;
Aouacheria A., Arnaud E., Venet S., Lalle P., Gouy M., Rigal D.,
Gillet G.;
"NrH, a human homologue of Nr-13 associates with Bcl-Xs and is an
inhibitor of apoptosis.";
Oncogene 20:5846-5855(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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 induced by
BAX but not BAK. {ECO:0000269|PubMed:11278245}.
-!- SUBUNIT: Binds to Bcl-2, Bcl-X and BAX. Interacts with APAF1.
{ECO:0000269|PubMed:11278245, ECO:0000269|PubMed:11593390}.
-!- INTERACTION:
Q07812:BAX; NbExp=2; IntAct=EBI-2126349, EBI-516580;
O43521:BCL2L11; NbExp=7; IntAct=EBI-2126349, EBI-526406;
O43521-1:BCL2L11; NbExp=2; IntAct=EBI-2126349, EBI-526416;
Q13323:BIK; NbExp=2; IntAct=EBI-2126349, EBI-700794;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11593390}.
Nucleus membrane {ECO:0000269|PubMed:11593390}.
-!- TISSUE SPECIFICITY: Widely expressed in adult tissues.
Preferentially expressed in lung, liver and kidney.
{ECO:0000269|PubMed:11593390}.
-!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG00503.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH93826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH93828.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAI04443.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAI04444.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAK48715.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF285092; AAG00503.1; ALT_INIT; mRNA.
EMBL; AF326964; AAK48715.1; ALT_INIT; mRNA.
EMBL; AJ458330; CAD30221.1; -; Genomic_DNA.
EMBL; AC023906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC093826; AAH93826.1; ALT_INIT; mRNA.
EMBL; BC093828; AAH93828.1; ALT_INIT; mRNA.
EMBL; BC104442; AAI04443.1; ALT_INIT; mRNA.
EMBL; BC104443; AAI04444.1; ALT_INIT; mRNA.
RefSeq; NP_001293097.1; NM_001306168.1.
RefSeq; NP_065129.1; NM_020396.3.
UniGene; Hs.283672; -.
PDB; 4B4S; X-ray; 1.90 A; A=2-167.
PDBsum; 4B4S; -.
ProteinModelPortal; Q9HD36; -.
SMR; Q9HD36; -.
BioGrid; 115334; 8.
IntAct; Q9HD36; 5.
MINT; Q9HD36; -.
STRING; 9606.ENSP00000260442; -.
BindingDB; Q9HD36; -.
ChEMBL; CHEMBL5988; -.
iPTMnet; Q9HD36; -.
PhosphoSitePlus; Q9HD36; -.
DMDM; 23396469; -.
PaxDb; Q9HD36; -.
PeptideAtlas; Q9HD36; -.
PRIDE; Q9HD36; -.
Ensembl; ENST00000260442; ENSP00000260442; ENSG00000137875.
GeneID; 10017; -.
KEGG; hsa:10017; -.
UCSC; uc002abq.4; human.
CTD; 10017; -.
DisGeNET; 10017; -.
EuPathDB; HostDB:ENSG00000137875.4; -.
GeneCards; BCL2L10; -.
HGNC; HGNC:993; BCL2L10.
MIM; 606910; gene.
neXtProt; NX_Q9HD36; -.
PharmGKB; PA25304; -.
eggNOG; ENOG410J2PB; Eukaryota.
eggNOG; ENOG4112AS5; LUCA.
HOGENOM; HOG000059275; -.
HOVERGEN; HBG050646; -.
InParanoid; Q9HD36; -.
KO; K18451; -.
PhylomeDB; Q9HD36; -.
TreeFam; TF334762; -.
GeneWiki; BCL2L10; -.
GenomeRNAi; 10017; -.
PRO; PR:Q9HD36; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000137875; -.
CleanEx; HS_BCL2L10; -.
ExpressionAtlas; Q9HD36; baseline and differential.
Genevisible; Q9HD36; HS.
GO; GO:0005829; C:cytosol; IDA:HGNC.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:HGNC.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0089720; F:caspase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:ProtInc.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0007292; P:female gamete generation; TAS:ProtInc.
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; IDA:HGNC.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
Gene3D; 1.10.437.10; -; 1.
InterPro; IPR002475; Bcl2-like.
InterPro; IPR020717; Bcl2_BH1_motif_CS.
InterPro; IPR020726; Bcl2_BH2_motif_CS.
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.
PROSITE; PS01080; BH1; 1.
PROSITE; PS01258; BH2; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Membrane; Mitochondrion;
Nucleus; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 194 Bcl-2-like protein 10.
/FTId=PRO_0000143068.
TRANSMEM 173 190 Helical. {ECO:0000255}.
MOTIF 76 95 BH1.
MOTIF 146 157 BH2.
VARIANT 11 11 L -> R (in dbSNP:rs2231292).
/FTId=VAR_047113.
CONFLICT 42 42 A -> V (in Ref. 5; AAI04444).
{ECO:0000305}.
CONFLICT 45 45 R -> W (in Ref. 5; AAI04444).
{ECO:0000305}.
HELIX 4 20 {ECO:0000244|PDB:4B4S}.
HELIX 34 49 {ECO:0000244|PDB:4B4S}.
HELIX 51 55 {ECO:0000244|PDB:4B4S}.
TURN 56 59 {ECO:0000244|PDB:4B4S}.
HELIX 64 77 {ECO:0000244|PDB:4B4S}.
HELIX 84 98 {ECO:0000244|PDB:4B4S}.
HELIX 102 105 {ECO:0000244|PDB:4B4S}.
HELIX 123 141 {ECO:0000244|PDB:4B4S}.
HELIX 144 149 {ECO:0000244|PDB:4B4S}.
HELIX 152 160 {ECO:0000244|PDB:4B4S}.
SEQUENCE 194 AA; 21973 MW; 86F9F1A39377755F CRC64;
MADPLRERTE LLLADYLGYC AREPGTPEPA PSTPEAAVLR SAAARLRQIH RSFFSAYLGY
PGNRFELVAL MADSVLSDSP GPTWGRVVTL VTFAGTLLER GPLVTARWKK WGFQPRLKEQ
EGDVARDCQR LVALLSSRLM GQHRAWLQAQ GGWDGFCHFF RTPFPLAFWR KQLVQAFLSC
LLTTAFIYLW TRLL


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