ID   BEX3_HUMAN              Reviewed;         111 AA.
AC   Q00994; B2RD17; D3DXA3; Q5JQT4; Q5JQT5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   07-OCT-2020, entry version 173.
DE   RecName: Full=Protein BEX3 {ECO:0000305};
DE   AltName: Full=Brain-expressed X-linked protein 3 {ECO:0000312|HGNC:HGNC:13388};
DE   AltName: Full=Nerve growth factor receptor-associated protein 1;
DE   AltName: Full=Ovarian granulosa cell 13.0 kDa protein HGR74;
DE   AltName: Full=p75NTR-associated cell death executor;
GN   Name=BEX3 {ECO:0000312|HGNC:HGNC:13388}; Synonyms=DXS6984E, NADE, NGFRAP1;
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] (ISOFORM 1).
RC   TISSUE=Ovary;
RX   PubMed=2171551; DOI=10.1089/dna.1990.9.479;
RA   Rapp G., Freudenstein J., Klaudiny J., Mucha J., Wempe F., Zimmer M.,
RA   Scheit K.H.;
RT   "Characterization of three abundant mRNAs from human ovarian granulosa
RT   cells.";
RL   DNA Cell Biol. 9:479-485(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=15958283; DOI=10.1016/j.gene.2005.05.012;
RA   Alvarez E., Zhou W., Witta S.E., Freed C.R.;
RT   "Characterization of the Bex gene family in humans, mice, and rats.";
RL   Gene 357:18-28(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RA   Zhou X., Wang W., Lu F., Hu S., Jiang L., Yan D., Zhang X., Yu X., Yu J.,
RA   Qu J.;
RT   "A comparative gene expression profile of the whole eye from human, mouse,
RT   and guinea pig.";
RL   Mol. Vis. 13:2214-2221(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
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   [9]
RP   3D-STRUCTURE MODELING OF 1-111.
RA   Arunkumar S.;
RT   "Theoretical model for p75NTR-associated cell death executor.";
RL   Submitted (JAN-2005) to the PDB data bank.
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 (By similarity). May play an important role in the
CC       pathogenesis of neurogenetic diseases. {ECO:0000250}.
CC   -!- SUBUNIT: Self-associates. Binds to the DEATH domain of p75NTR/NGFR.
CC       Interacts with 14-3-3 epsilon (YWHAE). Interacts with DIABLO/SMAC.
CC       {ECO:0000250|UniProtKB:Q9WTZ9}.
CC   -!- INTERACTION:
CC       Q00994; Q00994: BEX3; NbExp=4; IntAct=EBI-741753, EBI-741753;
CC       Q00994; Q13515: BFSP2; NbExp=3; IntAct=EBI-741753, EBI-10229433;
CC       Q00994; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-741753, EBI-11524851;
CC       Q00994; Q8IYX3: CCDC116; NbExp=4; IntAct=EBI-741753, EBI-744311;
CC       Q00994; Q8WYA6: CTNNBL1; NbExp=3; IntAct=EBI-741753, EBI-748128;
CC       Q00994; Q9Y6C2: EMILIN1; NbExp=3; IntAct=EBI-741753, EBI-744586;
CC       Q00994; Q9Y6C2-2: EMILIN1; NbExp=6; IntAct=EBI-741753, EBI-11748557;
CC       Q00994; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-741753, EBI-744099;
CC       Q00994; A1L4K1: FSD2; NbExp=6; IntAct=EBI-741753, EBI-5661036;
CC       Q00994; Q0D2H9: GOLGA8DP; NbExp=3; IntAct=EBI-741753, EBI-10181276;
CC       Q00994; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-741753, EBI-10181260;
CC       Q00994; Q9UNL4: ING4; NbExp=3; IntAct=EBI-741753, EBI-2866661;
CC       Q00994; Q8WYH8: ING5; NbExp=3; IntAct=EBI-741753, EBI-488533;
CC       Q00994; O76011: KRT34; NbExp=3; IntAct=EBI-741753, EBI-1047093;
CC       Q00994; P59942: MCCD1; NbExp=3; IntAct=EBI-741753, EBI-11987923;
CC       Q00994; Q99750: MDFI; NbExp=3; IntAct=EBI-741753, EBI-724076;
CC       Q00994; Q7Z6G3-2: NECAB2; NbExp=6; IntAct=EBI-741753, EBI-10172876;
CC       Q00994; P23297: S100A1; NbExp=3; IntAct=EBI-741753, EBI-743686;
CC       Q00994; Q8WXG8: S100Z; NbExp=5; IntAct=EBI-741753, EBI-12198403;
CC       Q00994; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-741753, EBI-358489;
CC       Q00994; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-741753, EBI-2554984;
CC       Q00994; Q92574: TSC1; NbExp=5; IntAct=EBI-741753, EBI-1047085;
CC       Q00994; Q99598: TSNAX; NbExp=3; IntAct=EBI-741753, EBI-742638;
CC       Q00994; Q8N6Y0: USHBP1; NbExp=6; IntAct=EBI-741753, EBI-739895;
CC       Q00994; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-741753, EBI-740727;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between the
CC       cytoplasm and the nucleus. Associates with replicating mitochondria (By
CC       similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q00994-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q00994-2; Sequence=VSP_046343;
CC   -!- TISSUE SPECIFICITY: Found in ovarian granulosa cells, testis, prostate
CC       and seminal vesicle tissue. High levels also detected in liver.
CC       {ECO:0000269|PubMed:15958283}.
CC   -!- DOMAIN: The nuclear export signal is required for export from the
CC       nucleus and the interactions with itself and p75NTR/NGFR.
CC       {ECO:0000250}.
CC   -!- PTM: Ubiquitinated. Degraded by the proteasome (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Binds transition metals. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}.
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DR   EMBL; M38188; AAA63232.1; -; mRNA.
DR   EMBL; AF187064; AAF75129.1; -; mRNA.
DR   EMBL; AY833562; AAX40680.1; -; mRNA.
DR   EMBL; AK315371; BAG37764.1; -; mRNA.
DR   EMBL; EL953547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL606763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471190; EAW54710.1; -; Genomic_DNA.
DR   EMBL; CH471190; EAW54712.1; -; Genomic_DNA.
DR   EMBL; BC003190; AAH03190.1; -; mRNA.
DR   CCDS; CCDS14508.1; -. [Q00994-1]
DR   CCDS; CCDS14509.1; -. [Q00994-2]
DR   PIR; C35826; C35826.
DR   RefSeq; NP_055195.1; NM_014380.2. [Q00994-1]
DR   RefSeq; NP_996798.1; NM_206915.2. [Q00994-1]
DR   RefSeq; NP_996800.1; NM_206917.2. [Q00994-2]
DR   PDB; 1SA6; Model; -; A=1-111.
DR   PDBsum; 1SA6; -.
DR   SMR; Q00994; -.
DR   BioGRID; 117956; 33.
DR   IntAct; Q00994; 37.
DR   MINT; Q00994; -.
DR   STRING; 9606.ENSP00000361728; -.
DR   iPTMnet; Q00994; -.
DR   BioMuta; BEX3; -.
DR   DMDM; 547642; -.
DR   MassIVE; Q00994; -.
DR   PaxDb; Q00994; -.
DR   PeptideAtlas; Q00994; -.
DR   PRIDE; Q00994; -.
DR   ProteomicsDB; 57900; -. [Q00994-1]
DR   Antibodypedia; 540; 252 antibodies.
DR   DNASU; 27018; -.
DR   Ensembl; ENST00000361298; ENSP00000354843; ENSG00000166681. [Q00994-2]
DR   Ensembl; ENST00000372634; ENSP00000361717; ENSG00000166681. [Q00994-2]
DR   Ensembl; ENST00000372635; ENSP00000361718; ENSG00000166681. [Q00994-1]
DR   Ensembl; ENST00000372645; ENSP00000361728; ENSG00000166681. [Q00994-1]
DR   GeneID; 27018; -.
DR   KEGG; hsa:27018; -.
DR   UCSC; uc004ekh.5; human. [Q00994-1]
DR   CTD; 27018; -.
DR   DisGeNET; 27018; -.
DR   EuPathDB; HostDB:ENSG00000166681.13; -.
DR   GeneCards; BEX3; -.
DR   HGNC; HGNC:13388; BEX3.
DR   HPA; ENSG00000166681; Low tissue specificity.
DR   MIM; 300361; gene.
DR   neXtProt; NX_Q00994; -.
DR   OpenTargets; ENSG00000166681; -.
DR   PharmGKB; PA31616; -.
DR   eggNOG; ENOG502TF4N; Eukaryota.
DR   GeneTree; ENSGT00940000153412; -.
DR   HOGENOM; CLU_123122_0_0_1; -.
DR   InParanoid; Q00994; -.
DR   KO; K12465; -.
DR   OMA; PMQNREE; -.
DR   OrthoDB; 1340122at2759; -.
DR   PhylomeDB; Q00994; -.
DR   TreeFam; TF337909; -.
DR   PathwayCommons; Q00994; -.
DR   Reactome; R-HSA-205025; NADE modulates death signalling.
DR   BioGRID-ORCS; 27018; 4 hits in 479 CRISPR screens.
DR   ChiTaRS; BEX3; human.
DR   GeneWiki; NGFRAP1; -.
DR   GenomeRNAi; 27018; -.
DR   Pharos; Q00994; Tbio.
DR   PRO; PR:Q00994; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q00994; protein.
DR   Bgee; ENSG00000166681; Expressed in cerebellar vermis and 251 other tissues.
DR   Genevisible; Q00994; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; TAS:Reactome.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
DR   GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
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   3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Metal-binding;
KW   Nucleus; Reference proteome; Ubl conjugation.
FT   CHAIN           1..111
FT                   /note="Protein BEX3"
FT                   /id="PRO_0000096688"
FT   REGION          68..111
FT                   /note="Interaction with 14-3-3 epsilon"
FT                   /evidence="ECO:0000250"
FT   REGION          68..93
FT                   /note="Interaction with p75NTR/NGFR"
FT                   /evidence="ECO:0000250"
FT   MOTIF           77..87
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..10
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.5"
FT                   /id="VSP_046343"
SQ   SEQUENCE   111 AA;  12959 MW;  29AA0573282C933E CRC64;
     MANIHQENEE MEQPMQNGEE DRPLGGGEGH QPAGNRRGQA RRLAPNFRWA IPNRQINDGM
     GGDGDDMEIF MEEMREIRRK LRELQLRNCL RILMGELSNH HDHHDEFCLM P
//