BEX1_MOUSE
ID BEX1_MOUSE Reviewed; 128 AA.
AC Q9R224; A3KGA2; O88858; Q9R1J2;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein BEX1;
DE AltName: Full=Brain-expressed X-linked protein 1 homolog;
DE AltName: Full=Reduced expression protein 3;
DE Short=REX-3;
GN Name=Bex1; Synonyms=Rex3;
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 [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Blastocyst;
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9806360; DOI=10.1016/s0303-7207(98)00127-0;
RA Faria T.N., LaRosa G.J., Wilen E., Liao J., Gudas L.J.;
RT "Characterization of genes which exhibit reduced expression during the
RT retinoic acid-induced differentiation of F9 teratocarcinoma cells:
RT involvement of cyclin D3 in RA-mediated growth arrest.";
RL Mol. Cell. Endocrinol. 143:155-166(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 TISSUE SPECIFICITY.
RX PubMed=11989783; DOI=10.1023/a:1014565320998;
RA Yang Q.-S., Xia F., Gu S.-H., Yuan H.-L., Chen J.-Z., Yang Q.-S., Ying K.,
RA Xie Y., Mao Y.-M.;
RT "Cloning and expression pattern of a spermatogenesis-related gene, BEX1,
RT mapped to chromosome Xq22.";
RL Biochem. Genet. 40:1-12(2002).
RN [8]
RP INTERACTION WITH OMP.
RX PubMed=12054873; DOI=10.1016/s0022-2836(02)00282-6;
RA Baldisseri D.M., Margolis J.W., Weber D.J., Koo J.H., Margolis F.L.;
RT "Olfactory marker protein (OMP) exhibits a beta-clam fold in solution:
RT implications for target peptide interaction and olfactory signal
RT transduction.";
RL J. Mol. Biol. 319:823-837(2002).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH OMP.
RX PubMed=12911636; DOI=10.1046/j.1471-4159.2003.01940.x;
RA Behrens M., Margolis J.W., Margolis F.L.;
RT "Identification of members of the Bex gene family as olfactory marker
RT protein (OMP) binding partners.";
RL J. Neurochem. 86:1289-1296(2003).
RN [10]
RP INTERACTION WITH OMP.
RX PubMed=15198671; DOI=10.1111/j.1471-4159.2004.02463.x;
RA Koo J.H., Gill S., Pannell L.K., Menco B.P.M., Margolis J.W.,
RA Margolis F.L.;
RT "The interaction of Bex and OMP reveals a dimer of OMP with a short half-
RT life.";
RL J. Neurochem. 90:102-116(2004).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=15861462; DOI=10.1002/cne.20486;
RA Koo J.H., Saraswati M., Margolis F.L.;
RT "Immunolocalization of Bex protein in the mouse brain and olfactory
RT system.";
RL J. Comp. Neurol. 487:1-14(2005).
CC -!- FUNCTION: Signaling adapter molecule involved in p75NTR/NGFR signaling.
CC Plays a role in cell cycle progression and neuronal differentiation.
CC Inhibits neuronal differentiation in response to nerve growth factor
CC (NGF). May act as a link between the cell cycle and neurotrophic factor
CC signaling, possibly by functioning as an upstream modulator of receptor
CC signaling, coordinating biological responses to external signals with
CC internal cellular states (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with neurotrophin receptor p75NTR/NGFR (By
CC similarity). Interacts with OMP. {ECO:0000250,
CC ECO:0000269|PubMed:12054873, ECO:0000269|PubMed:12911636,
CC ECO:0000269|PubMed:15198671}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12911636}. Cytoplasm
CC {ECO:0000269|PubMed:12911636}. Note=Shuttles between the cytoplasm and
CC the nucleus.
CC -!- TISSUE SPECIFICITY: Primarily localized to neuronal cells within
CC several regions of the brain, including the olfactory epithelium, bulb,
CC peri/paraventricular nuclei, suprachiasmatic nucleus, arcuate nucleus,
CC median eminence, lateral hypothalamic area, thalamus, hippocampus and
CC cerebellum (at protein level). Expressed in brain, mid term embryos and
CC to a lesser extent in ovary. In testis, it is expressed in the
CC pachytene spermatocytes and spermatids but not in spermatogonia.
CC {ECO:0000269|PubMed:10072429, ECO:0000269|PubMed:11989783,
CC ECO:0000269|PubMed:15861462, ECO:0000269|PubMed:9806360}.
CC -!- INDUCTION: Down-regulated following RA treatment. Up-regulated in
CC parthenogenetic embryos. {ECO:0000269|PubMed:9806360}.
CC -!- PTM: Phosphorylated. Phosphorylation of Ser-105 protects it from the
CC proteasome (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Degraded by the proteasome (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BEX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC61929.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF097437; AAD47168.1; -; Genomic_DNA.
DR EMBL; AF097438; AAD24429.1; -; mRNA.
DR EMBL; AF051347; AAC61929.1; ALT_INIT; mRNA.
DR EMBL; AL671493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466616; EDL23851.1; -; Genomic_DNA.
DR EMBL; BC061179; AAH61179.1; -; mRNA.
DR EMBL; BC089464; AAH89464.1; -; mRNA.
DR RefSeq; NP_033078.2; NM_009052.2.
DR AlphaFoldDB; Q9R224; -.
DR BioGRID; 202868; 1.
DR MINT; Q9R224; -.
DR STRING; 10090.ENSMUSP00000060005; -.
DR iPTMnet; Q9R224; -.
DR PhosphoSitePlus; Q9R224; -.
DR MaxQB; Q9R224; -.
DR PaxDb; Q9R224; -.
DR PeptideAtlas; Q9R224; -.
DR PRIDE; Q9R224; -.
DR ProteomicsDB; 273603; -.
DR Ensembl; ENSMUST00000058125; ENSMUSP00000060005; ENSMUSG00000050071.
DR Ensembl; ENSMUST00000113118; ENSMUSP00000108743; ENSMUSG00000050071.
DR Ensembl; ENSMUST00000113120; ENSMUSP00000108745; ENSMUSG00000050071.
DR GeneID; 19716; -.
DR KEGG; mmu:19716; -.
DR UCSC; uc009uig.1; mouse.
DR CTD; 55859; -.
DR MGI; MGI:1328321; Bex1.
DR VEuPathDB; HostDB:ENSMUSG00000050071; -.
DR eggNOG; ENOG502RW3Y; Eukaryota.
DR GeneTree; ENSGT00940000153412; -.
DR HOGENOM; CLU_123122_1_0_1; -.
DR InParanoid; Q9R224; -.
DR OMA; HEHHDEF; -.
DR OrthoDB; 1532209at2759; -.
DR PhylomeDB; Q9R224; -.
DR TreeFam; TF337909; -.
DR BioGRID-ORCS; 19716; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Bex1; mouse.
DR PRO; PR:Q9R224; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9R224; protein.
DR Bgee; ENSMUSG00000050071; Expressed in otic placode and 253 other tissues.
DR Genevisible; Q9R224; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0061564; P:axon development; IGI:MGI.
DR GO; GO:0031103; P:axon regeneration; IMP:MGI.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR DisProt; DP01183; -.
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 Cytoplasm; Developmental protein; Differentiation; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..128
FT /note="Protein BEX1"
FT /id="PRO_0000229774"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3MKQ2"
FT CONFLICT 40
FT /note="T -> I (in Ref. 1; AAC61929 and 3; AAD24429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 128 AA; 15119 MW; 6C8897FFA9C987C9 CRC64;
MESKDQGVKN LNMENDHQKK EEKEEKPQDT IRREPAVALT SEAGKNCAPR GGRRRFRVRQ
PIAHYRWDLM QRVGEPQGRM REENVQRFGG DVRQLMEKLR ERQLSHSLRA VSTDPPHHDH
HDEFCLMP
