BEX3_MOUSE
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};
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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
