ID BEX3_MOUSE Reviewed; 124 AA. AC Q9WTZ9; A3KGA0; A3KGA1; Q9CWN9; Q9D0S2; Q9D1N5; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 03-AUG-2022, entry version 136. DE RecName: Full=Protein BEX3 {ECO:0000305}; DE AltName: Full=Brain-expressed X-linked protein 3 homolog {ECO:0000250|UniProtKB:Q00994}; DE AltName: Full=Nerve growth factor receptor-associated protein 1; DE AltName: Full=p75NTR-associated cell death executor; GN Name=Bex3; Synonyms=Nade, Ngfrap1; 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] (ISOFORM 1). RC STRAIN=FVB/N; RX PubMed=10072429; DOI=10.1093/hmg/8.4.611; RA Brown A.L., Kay G.F.; RT "Bex1, a gene with increased expression in parthenogenetic embryos, is a RT member of a novel gene family on the mouse X chromosome."; RL Hum. Mol. Genet. 8:611-619(1999). RN [2] RP ERRATUM OF PUBMED:10072429. RA Brown A.L., Kay G.F.; RL Hum. Mol. Genet. 8:943-943(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DEGRADATION BY THE RP PROTEASOME. RC STRAIN=BALB/cJ; RX PubMed=10764727; DOI=10.1074/jbc.c000140200; RA Mukai J., Hachiya T., Shoji-Hoshino S., Kimura M.T., Nadano D., Suvanto P., RA Hanaoka T., Li Y., Irie S., Greene L.A., Sato T.-A.; RT "NADE, a p75NTR-associated cell death executor, is involved in signal RT transduction mediated by the common neurotrophin receptor p75NTR."; RL J. Biol. Chem. 275:17566-17570(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Mammary tumor; 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 [7] RP INTERACTION WITH YWHAE. RX PubMed=11278287; DOI=10.1074/jbc.m005453200; RA Kimura M.T., Irie S., Shoji-Hoshino S., Mukai J., Nadano D., Oshimura M., RA Sato T.-A.; RT "14-3-3 is involved in p75 neurotrophin receptor-mediated signal RT transduction."; RL J. Biol. Chem. 276:17291-17300(2001). RN [8] RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH NGFR, AND MUTAGENESIS OF RP LEU-94; LEU-97 AND LEU-99. RX PubMed=11830582; DOI=10.1074/jbc.m106342200; RA Mukai J., Shoji S., Kimura M.T., Okubo S., Sano H., Suvanto P., Li Y., RA Irie S., Sato T.-A.; RT "Structure-function analysis of NADE: identification of regions that RT mediate nerve growth factor-induced apoptosis."; RL J. Biol. Chem. 277:13973-13982(2002). RN [9] RP TISSUE SPECIFICITY. RX PubMed=12935912; DOI=10.1016/s0165-3806(03)00166-4; RA Kendall S.E., Ryczko M.C., Mehan M., Verdi J.M.; RT "Characterization of NADE, NRIF and SC-1 gene expression during mouse RT neurogenesis."; RL Brain Res. Dev. Brain Res. 144:151-158(2003). RN [10] RP INTERACTION WITH DIABLO. RX PubMed=15178455; DOI=10.1016/j.bbrc.2004.05.043; RA Yoon K., Jang H.D., Lee S.Y.; RT "Direct interaction of Smac with NADE promotes TRAIL-induced apoptosis."; RL Biochem. Biophys. Res. Commun. 319:649-654(2004). RN [11] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-121. RX PubMed=15563833; DOI=10.1016/j.gene.2004.08.031; RA Kim A.-J., Lee C.-S., Schlessinger D.; RT "Bex3 associates with replicating mitochondria and is involved in possible RT growth control of F9 teratocarcinoma cells."; RL Gene 343:79-89(2004). CC -!- FUNCTION: May be a signaling adapter molecule involved in p75NTR- CC mediated apoptosis induced by NGF. Plays a role in zinc-triggered CC neuronal death. {ECO:0000269|PubMed:10764727}. CC -!- SUBUNIT: Self-associates (PubMed:11830582). Binds to the DEATH domain CC of p75NTR/NGFR (PubMed:11830582). Interacts with 14-3-3 epsilon (YWHAE) CC (PubMed:11278287). Interacts with DIABLO/SMAC (PubMed:15178455). CC {ECO:0000269|PubMed:11278287, ECO:0000269|PubMed:11830582, CC ECO:0000269|PubMed:15178455}. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the CC cytoplasm and the nucleus. Associates with replicating mitochondria. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9WTZ9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9WTZ9-2; Sequence=VSP_017744; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12935912, CC ECO:0000269|PubMed:15563833}. CC -!- DOMAIN: The nuclear export signal is required for export from the CC nucleus and the interactions with itself and p75NTR/NGFR. CC -!- PTM: Ubiquitinated (Probable). Degraded by the proteasome. CC {ECO:0000305}. CC -!- MISCELLANEOUS: Binds transition metals. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB23350.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305}; 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; AF097440; AAD24431.1; -; mRNA. DR EMBL; AF187066; AAF75131.1; -; mRNA. DR EMBL; AK003294; BAB22697.1; -; mRNA. DR EMBL; AK004531; BAB23350.1; ALT_SEQ; mRNA. DR EMBL; AK010500; BAB26986.1; -; mRNA. DR EMBL; AL671493; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC027815; AAH27815.1; -; mRNA. DR CCDS; CCDS30419.1; -. [Q9WTZ9-1] DR CCDS; CCDS53194.1; -. [Q9WTZ9-2] DR RefSeq; NP_001103703.1; NM_001110233.1. [Q9WTZ9-1] DR RefSeq; NP_001103704.1; NM_001110234.1. [Q9WTZ9-2] DR RefSeq; NP_033880.1; NM_009750.2. [Q9WTZ9-1] DR AlphaFoldDB; Q9WTZ9; -. DR BioGRID; 198339; 9. DR STRING; 10090.ENSMUSP00000063039; -. DR PhosphoSitePlus; Q9WTZ9; -. DR PaxDb; Q9WTZ9; -. DR PRIDE; Q9WTZ9; -. DR Antibodypedia; 540; 265 antibodies from 36 providers. DR DNASU; 12070; -. DR Ensembl; ENSMUST00000053540; ENSMUSP00000063039; ENSMUSG00000046432. [Q9WTZ9-1] DR Ensembl; ENSMUST00000113112; ENSMUSP00000108737; ENSMUSG00000046432. [Q9WTZ9-2] DR Ensembl; ENSMUST00000113113; ENSMUSP00000108738; ENSMUSG00000046432. [Q9WTZ9-1] DR Ensembl; ENSMUST00000178632; ENSMUSP00000136952; ENSMUSG00000046432. [Q9WTZ9-1] DR GeneID; 12070; -. DR KEGG; mmu:12070; -. DR UCSC; uc009uik.2; mouse. [Q9WTZ9-1] DR CTD; 27018; -. DR MGI; MGI:1338016; Bex3. DR VEuPathDB; HostDB:ENSMUSG00000046432; -. DR eggNOG; ENOG502TF4N; Eukaryota. DR GeneTree; ENSGT00940000153412; -. DR HOGENOM; CLU_123122_0_0_1; -. DR InParanoid; Q9WTZ9; -. DR OMA; PMQNREE; -. DR OrthoDB; 1577482at2759; -. DR PhylomeDB; Q9WTZ9; -. DR TreeFam; TF337909; -. DR Reactome; R-MMU-205025; NADE modulates death signalling. DR BioGRID-ORCS; 12070; 2 hits in 71 CRISPR screens. DR ChiTaRS; Ngfrap1; mouse. DR PRO; PR:Q9WTZ9; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; Q9WTZ9; protein. DR Bgee; ENSMUSG00000046432; Expressed in yolk sac and 245 other tissues. DR Genevisible; Q9WTZ9; MM. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005123; F:death receptor binding; IPI:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005163; F:nerve growth factor receptor binding; ISO:MGI. DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IPI:MGI. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR InterPro; IPR007623; BEX. DR InterPro; IPR021156; TF_A-like/BEX. DR PANTHER; PTHR19430; PTHR19430; 1. DR Pfam; PF04538; BEX; 1. DR PIRSF; PIRSF008633; BEX; 1. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Cytoplasm; Metal-binding; Nucleus; KW Reference proteome; Ubl conjugation. FT CHAIN 1..124 FT /note="Protein BEX3" FT /id="PRO_0000229781" FT REGION 1..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 81..124 FT /note="Interaction with 14-3-3 epsilon" FT REGION 81..106 FT /note="Interaction with p75NTR/NGFR" FT /evidence="ECO:0000269|PubMed:11830582" FT MOTIF 90..100 FT /note="Nuclear export signal" FT VAR_SEQ 1..10 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_017744" FT MUTAGEN 94 FT /note="L->A: Abolishes nuclear export and interactions with FT itself and p75NTR/NGFR; when associated with A-97 and A- FT 99." FT /evidence="ECO:0000269|PubMed:11830582" FT MUTAGEN 97 FT /note="L->A: Abolishes nuclear export and interactions with FT itself and p75NTR/NGFR; when associated with A-97 and A- FT 99." FT /evidence="ECO:0000269|PubMed:11830582" FT MUTAGEN 99 FT /note="L->A: Abolishes nuclear export and interactions with FT itself and p75NTR/NGFR; when associated with A-94 and A- FT 97." FT /evidence="ECO:0000269|PubMed:11830582" FT MUTAGEN 121 FT /note="C->A: Abolishes localization with replicating FT mitochondria." FT /evidence="ECO:0000269|PubMed:15563833" FT CONFLICT 17 FT /note="N -> D (in Ref. 4; BAB26986)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="M -> I (in Ref. 4; BAB22697)" FT /evidence="ECO:0000305" SQ SEQUENCE 124 AA; 14542 MW; 3CCCD4F05E66F461 CRC64; MANVHQENEE MEQPLQNGQE DRPVGGGEGH QPAANNNNNN HNHNHNHHRR GQARRLAPNF RWAIPNRQMN DGLGGDGDDM EMFMEEMREI RRKLRELQLR NCLRILMGEL SNHHDHHDEF CLMP //