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   16-JAN-2019, entry version 119.
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; Myomorpha;
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; -; 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   UniGene; Mm.90787; -.
DR   BioGrid; 198339; 3.
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; 27018; -.
DR   MGI; MGI:1338016; Bex3.
DR   eggNOG; ENOG410JCIT; Eukaryota.
DR   eggNOG; ENOG41113TP; LUCA.
DR   GeneTree; ENSGT00940000153412; -.
DR   HOGENOM; HOG000236300; -.
DR   HOVERGEN; HBG080240; -.
DR   InParanoid; Q9WTZ9; -.
DR   KO; K12465; -.
DR   OMA; PMQNREE; -.
DR   OrthoDB; 1577482at2759; -.
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; Expressed in 267 organ(s), highest expression level in mandibular prominence.
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; IEA:Ensembl.
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.
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                                {ECO:0000269|PubMed:11830582}.
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
//