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 07-SEP-2016, entry version 106. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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 RT a member of a novel gene family on the mouse X chromosome."; RL Hum. Mol. Genet. 8:611-619(1999). RN [2] RP ERRATUM. 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 RP THE 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., RA Suvanto P., 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the 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 RT project: 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., RA Oshimura M., 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 RP OF 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 RT 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 RT possible 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 CC domain of p75NTR/NGFR (PubMed:11830582). Interacts with 14-3-3 CC epsilon (YWHAE) (PubMed:11278287). Interacts with DIABLO/SMAC CC (PubMed:15178455). {ECO:0000269|PubMed:11278287, CC ECO:0000269|PubMed:11830582, ECO:0000269|PubMed:15178455}. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between CC the cytoplasm and the nucleus. Associates with replicating CC 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. CC {ECO:0000269|PubMed:12935912, 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; Positions=125; Note=Translated as stop.; 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; CAM45862.1; -; Genomic_DNA. DR EMBL; AL671493; CAM45863.1; -; 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 UniGene; Mm.90787; -. DR BioGrid; 198339; 3. DR MINT; MINT-128772; -. DR STRING; 10090.ENSMUSP00000063039; -. DR PaxDb; Q9WTZ9; -. DR PRIDE; Q9WTZ9; -. 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; 12070; -. DR MGI; MGI:1338016; Ngfrap1. DR eggNOG; ENOG410JCIT; Eukaryota. DR eggNOG; ENOG41113TP; LUCA. DR GeneTree; ENSGT00810000125492; -. DR HOGENOM; HOG000236300; -. DR HOVERGEN; HBG080240; -. DR InParanoid; Q9WTZ9; -. DR KO; K12465; -. DR OMA; LIMANIH; -. DR OrthoDB; EOG091G146U; -. DR PhylomeDB; Q9WTZ9; -. DR TreeFam; TF337909; -. DR Reactome; R-MMU-205025; NADE modulates death signalling. DR ChiTaRS; Ngfrap1; mouse. DR PRO; PR:Q9WTZ9; -. DR Proteomes; UP000000589; Chromosome X. DR Bgee; ENSMUSG00000046432; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IPI:MGI. DR InterPro; IPR007623; BEX. DR InterPro; IPR021156; TF_A-like/BEX-like. DR Pfam; PF04538; BEX; 1. DR PIRSF; PIRSF008633; BEX; 1. PE 1: Evidence at protein level; KW Alternative splicing; Apoptosis; Complete proteome; Cytoplasm; KW Metal-binding; Nucleus; Reference proteome; Ubl conjugation. FT CHAIN 1 124 Protein BEX3. FT /FTId=PRO_0000229781. FT REGION 81 124 Interaction with 14-3-3 epsilon. FT REGION 81 106 Interaction with p75NTR/NGFR. FT MOTIF 90 100 Nuclear export signal. FT COMPBIAS 35 46 Poly-Asn. FT VAR_SEQ 1 10 Missing (in isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_017744. FT MUTAGEN 94 94 L->A: Abolishes nuclear export and FT interactions with itself and p75NTR/NGFR; FT when associated with A-97 and A-99. FT {ECO:0000269|PubMed:11830582}. FT MUTAGEN 97 97 L->A: Abolishes nuclear export and FT interactions with itself and p75NTR/NGFR; FT when associated with A-97 and A-99. FT {ECO:0000269|PubMed:11830582}. FT MUTAGEN 99 99 L->A: Abolishes nuclear export and FT interactions with itself and p75NTR/NGFR; FT when associated with A-94 and A-97. FT {ECO:0000269|PubMed:11830582}. FT MUTAGEN 121 121 C->A: Abolishes localization with FT replicating mitochondria. FT {ECO:0000269|PubMed:15563833}. FT CONFLICT 17 17 N -> D (in Ref. 4; BAB26986). FT {ECO:0000305}. FT CONFLICT 82 82 M -> I (in Ref. 4; BAB22697). FT {ECO:0000305}. SQ SEQUENCE 124 AA; 14542 MW; 3CCCD4F05E66F461 CRC64; MANVHQENEE MEQPLQNGQE DRPVGGGEGH QPAANNNNNN HNHNHNHHRR GQARRLAPNF RWAIPNRQMN DGLGGDGDDM EMFMEEMREI RRKLRELQLR NCLRILMGEL SNHHDHHDEF CLMP //