ID B2L10_HUMAN Reviewed; 204 AA. AC Q9HD36; Q3SX80; Q52LQ9; Q8TCS9; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 08-MAY-2019, sequence version 3. DT 07-APR-2021, entry version 166. DE RecName: Full=Bcl-2-like protein 10; DE Short=Bcl2-L-10; DE AltName: Full=Anti-apoptotic protein NrH; DE AltName: Full=Apoptosis regulator Bcl-B; GN Name=BCL2L10; Synonyms=BCLB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Ovary; RX PubMed=11689480; DOI=10.1093/hmg/10.21.2329; RA Zhang H., Holzgreve W., De Geyter C.; RT "Bcl2-L-10, a novel anti-apoptotic member of the Bcl-2 family, blocks RT apoptosis in the mitochondria death pathway but not in the death receptor RT pathway."; RL Hum. Mol. Genet. 10:2329-2339(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH BAX; BCL2 AND RP BCL2L1. RC TISSUE=Liver; RX PubMed=11278245; DOI=10.1074/jbc.c000871200; RA Ke N., Godzik A., Reed J.C.; RT "Bcl-B, a novel Bcl-2 family member that differentially binds and regulates RT Bax and Bak."; RL J. Biol. Chem. 276:12481-12484(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-204, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND INTERACTION WITH BCL2L1. RX PubMed=11593390; DOI=10.1038/sj.onc.1204740; RA Aouacheria A., Arnaud E., Venet S., Lalle P., Gouy M., Rigal D., Gillet G.; RT "NrH, a human homologue of Nr-13 associates with Bcl-Xs and is an inhibitor RT of apoptosis."; RL Oncogene 20:5846-5855(2001). RN [6] RP FUNCTION, INTERACTION WITH AHCYL1; ITPR1; ITPR2 AND ITPR3, AND SUBCELLULAR RP LOCATION. RX PubMed=27995898; DOI=10.7554/elife.19896; RA Bonneau B., Ando H., Kawaai K., Hirose M., Takahashi-Iwanaga H., RA Mikoshiba K.; RT "IRBIT controls apoptosis by interacting with the Bcl-2 homolog, Bcl2l10, RT and by promoting ER-mitochondria contact."; RL Elife 5:e19896-e19896(2016). CC -!- FUNCTION: Promotes cell survival by suppressing apoptosis induced by CC BAX but not BAK (PubMed:11689480, PubMed:11278245). Increases binding CC of AHCYL1/IRBIT to ITPR1 (PubMed:27995898). Reduces ITPR1-mediated CC calcium release from the endoplasmic reticulum cooperatively with CC AHCYL1/IRBIT under normal cellular conditions (PubMed:27995898). Under CC apoptotic stress conditions, dissociates from ITPR1 and is displaced CC from mitochondria-associated endoplasmic reticulum membranes, leading CC to increased Ca(2+) transfer to mitochondria which promotes apoptosis CC (PubMed:27995898). {ECO:0000269|PubMed:11278245, CC ECO:0000269|PubMed:11689480, ECO:0000269|PubMed:27995898}. CC -!- SUBUNIT: Interacts with BCL2, BCL2L1/BCLX and BAX (PubMed:11278245, CC PubMed:11593390). Interacts with APAF1 (By similarity). Interacts with CC ITPR1, ITPR2 and ITPR3; the interaction with ITPR1 is increased in the CC presence of AHCLY1 (PubMed:27995898). Interacts with AHCYL1 CC (PubMed:27995898). {ECO:0000250|UniProtKB:Q9Z0F3, CC ECO:0000269|PubMed:11278245, ECO:0000269|PubMed:11593390, CC ECO:0000269|PubMed:27995898}. CC -!- INTERACTION: CC Q9HD36; O43865: AHCYL1; NbExp=4; IntAct=EBI-2126349, EBI-2371423; CC Q9HD36; Q07812: BAX; NbExp=2; IntAct=EBI-2126349, EBI-516580; CC Q9HD36; O43521: BCL2L11; NbExp=10; IntAct=EBI-2126349, EBI-526406; CC Q9HD36; O43521-1: BCL2L11; NbExp=2; IntAct=EBI-2126349, EBI-526416; CC Q9HD36; Q13323: BIK; NbExp=8; IntAct=EBI-2126349, EBI-700794; CC Q9HD36; Q96LC9: BMF; NbExp=3; IntAct=EBI-2126349, EBI-3919268; CC Q9HD36; Q14643: ITPR1; NbExp=7; IntAct=EBI-2126349, EBI-465548; CC Q9HD36; Q99735: MGST2; NbExp=3; IntAct=EBI-2126349, EBI-11324706; CC Q9HD36; Q5PRF9: SAMD4B; NbExp=3; IntAct=EBI-2126349, EBI-1047489; CC Q9HD36; Q86VY9: TMEM200A; NbExp=3; IntAct=EBI-2126349, EBI-11732844; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11593390}. CC Nucleus membrane {ECO:0000269|PubMed:11593390}. Endoplasmic reticulum CC {ECO:0000269|PubMed:27995898}. Note=Localizes to mitochondria- CC associated endoplasmic reticulum membranes (MAMs) (PubMed:27995898). CC Localization to MAMs is greatly reduced under apoptotic stress CC conditions (PubMed:27995898). {ECO:0000269|PubMed:27995898}. CC -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Preferentially CC expressed in lung, liver and kidney. {ECO:0000269|PubMed:11593390}. CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator. CC {ECO:0000305|PubMed:11593390}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF285092; AAG00503.1; -; mRNA. DR EMBL; AF326964; AAK48715.1; -; mRNA. DR EMBL; AC023906; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC093826; AAH93826.1; -; mRNA. DR EMBL; BC093828; AAH93828.1; -; mRNA. DR EMBL; BC104442; AAI04443.1; -; mRNA. DR EMBL; BC104443; AAI04444.1; -; mRNA. DR EMBL; AJ458330; CAD30221.1; -; Genomic_DNA. DR CCDS; CCDS10148.1; -. DR RefSeq; NP_001293097.1; NM_001306168.1. DR RefSeq; NP_065129.1; NM_020396.3. DR PDB; 4B4S; X-ray; 1.90 A; A=12-177. DR PDBsum; 4B4S; -. DR SMR; Q9HD36; -. DR BioGRID; 115334; 14. DR IntAct; Q9HD36; 13. DR MINT; Q9HD36; -. DR STRING; 9606.ENSP00000260442; -. DR ChEMBL; CHEMBL5988; -. DR iPTMnet; Q9HD36; -. DR PhosphoSitePlus; Q9HD36; -. DR BioMuta; BCL2L10; -. DR DMDM; 23396469; -. DR MassIVE; Q9HD36; -. DR PaxDb; Q9HD36; -. DR PeptideAtlas; Q9HD36; -. DR PRIDE; Q9HD36; -. DR ProteomicsDB; 81824; -. DR Antibodypedia; 24926; 230 antibodies. DR Ensembl; ENST00000260442; ENSP00000260442; ENSG00000137875. DR GeneID; 10017; -. DR KEGG; hsa:10017; -. DR UCSC; uc002abq.4; human. DR CTD; 10017; -. DR DisGeNET; 10017; -. DR GeneCards; BCL2L10; -. DR HGNC; HGNC:993; BCL2L10. DR HPA; ENSG00000137875; Tissue enhanced (liver). DR MIM; 606910; gene. DR neXtProt; NX_Q9HD36; -. DR OpenTargets; ENSG00000137875; -. DR PharmGKB; PA25304; -. DR VEuPathDB; HostDB:ENSG00000137875.4; -. DR eggNOG; KOG4728; Eukaryota. DR GeneTree; ENSGT00940000164610; -. DR HOGENOM; CLU_122207_0_0_1; -. DR InParanoid; Q9HD36; -. DR OMA; LGYPGNR; -. DR OrthoDB; 1193942at2759; -. DR PhylomeDB; Q9HD36; -. DR TreeFam; TF334762; -. DR PathwayCommons; Q9HD36; -. DR BioGRID-ORCS; 10017; 5 hits in 987 CRISPR screens. DR GeneWiki; BCL2L10; -. DR GenomeRNAi; 10017; -. DR Pharos; Q9HD36; Tchem. DR PRO; PR:Q9HD36; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q9HD36; protein. DR Bgee; ENSG00000137875; Expressed in right lobe of liver and 86 other tissues. DR ExpressionAtlas; Q9HD36; baseline and differential. DR Genevisible; Q9HD36; HS. DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0089720; F:caspase binding; IPI:ParkinsonsUK-UCL. 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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:ProtInc. DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB. DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central. DR GO; GO:0007292; P:female gamete generation; TAS:ProtInc. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:HGNC-UCL. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central. DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc. DR CDD; cd06845; Bcl-2_like; 1. DR Gene3D; 1.10.437.10; -; 1. DR InterPro; IPR002475; Bcl2-like. DR InterPro; IPR020717; Bcl2_BH1_motif_CS. DR InterPro; IPR020726; Bcl2_BH2_motif_CS. DR InterPro; IPR036834; Blc2-like_sf. DR InterPro; IPR026298; Blc2_fam. 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; PS01080; BH1; 1. DR PROSITE; PS01258; BH2; 1. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; Endoplasmic reticulum; Membrane; Mitochondrion; KW Nucleus; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..204 FT /note="Bcl-2-like protein 10" FT /id="PRO_0000143068" FT TRANSMEM 183..200 FT /note="Helical" FT /evidence="ECO:0000255" FT MOTIF 86..105 FT /note="BH1" FT MOTIF 156..167 FT /note="BH2" FT VARIANT 21 FT /note="L -> R (in dbSNP:rs2231292)" FT /id="VAR_047113" FT CONFLICT 52 FT /note="A -> V (in Ref. 4; AAI04444)" FT /evidence="ECO:0000305" FT CONFLICT 55 FT /note="R -> W (in Ref. 4; AAI04444)" FT /evidence="ECO:0000305" FT HELIX 14..30 FT /evidence="ECO:0007744|PDB:4B4S" FT HELIX 44..59 FT /evidence="ECO:0007744|PDB:4B4S" FT HELIX 61..65 FT /evidence="ECO:0007744|PDB:4B4S" FT TURN 66..69 FT /evidence="ECO:0007744|PDB:4B4S" FT HELIX 74..87 FT /evidence="ECO:0007744|PDB:4B4S" FT HELIX 94..108 FT /evidence="ECO:0007744|PDB:4B4S" FT HELIX 112..115 FT /evidence="ECO:0007744|PDB:4B4S" FT HELIX 133..151 FT /evidence="ECO:0007744|PDB:4B4S" FT HELIX 154..159 FT /evidence="ECO:0007744|PDB:4B4S" FT HELIX 162..170 FT /evidence="ECO:0007744|PDB:4B4S" SQ SEQUENCE 204 AA; 23204 MW; 4B46B2DC472475CB CRC64; MVDQLRERTT MADPLRERTE LLLADYLGYC AREPGTPEPA PSTPEAAVLR SAAARLRQIH RSFFSAYLGY PGNRFELVAL MADSVLSDSP GPTWGRVVTL VTFAGTLLER GPLVTARWKK WGFQPRLKEQ EGDVARDCQR LVALLSSRLM GQHRAWLQAQ GGWDGFCHFF RTPFPLAFWR KQLVQAFLSC LLTTAFIYLW TRLL //