ID   EFNB3_MOUSE             Reviewed;         340 AA.
AC   O35393;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Ephrin-B3;
DE   Flags: Precursor;
GN   Name=Efnb3;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=9484836; DOI=10.1038/sj.onc.1201557;
RA   Bergemann A.D., Zhang L., Chiang M.-K., Brambilla R., Klein R.,
RA   Flanagan J.G.;
RT   "Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of
RT   the developing neural tube.";
RL   Oncogene 16:471-480(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [3]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=10704386; DOI=10.1242/dev.127.7.1397;
RA   Imondi R., Wideman C., Kaprielian Z.;
RT   "Complementary expression of transmembrane ephrins and their receptors in
RT   the mouse spinal cord: a possible role in constraining the orientation of
RT   longitudinally projecting axons.";
RL   Development 127:1397-1410(2000).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-271, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [7]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA   Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA   Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT   "Gene expression profiling of muscle stem cells identifies novel regulators
RT   of postnatal myogenesis.";
RL   Front. Cell Dev. Biol. 4:58-58(2016).
CC   -!- FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family
CC       of receptor tyrosine kinases which are crucial for migration, repulsion
CC       and adhesion during neuronal, vascular and epithelial development.
CC       Binds promiscuously Eph receptors residing on adjacent cells, leading
CC       to contact-dependent bidirectional signaling into neighboring cells.
CC       The signaling pathway downstream of the receptor is referred to as
CC       forward signaling while the signaling pathway downstream of the ephrin
CC       ligand is referred to as reverse signaling. May play a pivotal role in
CC       forebrain function. Binds to, and induce the collapse of, commissural
CC       axons/growth cones in vitro. May play a role in constraining the
CC       orientation of longitudinally projecting axons.
CC       {ECO:0000269|PubMed:10704386}.
CC   -!- SUBUNIT: Interacts with GRIP1 and GRIP2. {ECO:0000250}.
CC   -!- INTERACTION:
CC       O35393; Q4VCP5: G; Xeno; NbExp=5; IntAct=EBI-8668154, EBI-15716439;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed on lateral floor plate cells,
CC       specifically on commissural axon segments that have passed through the
CC       floor plate. Expressed in cells of the retinal ganglion cell layer
CC       during retinal axon guidance to the optic disk (PubMed:9484836,
CC       PubMed:10704386). Expressed in myogenic progenitor cells
CC       (PubMed:27446912). {ECO:0000269|PubMed:10704386,
CC       ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:9484836}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the floor plate throughout the period
CC       of commissural axon pathfinding (PubMed:9484836, PubMed:10704386). In
CC       myogenic progenitor cells, highly expressed during early development
CC       (11.5 dpc) and progressively repressed as developments proceeds
CC       (PubMed:27446912). {ECO:0000269|PubMed:10704386,
CC       ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:9484836}.
CC   -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00884}.
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DR   EMBL; AF025288; AAC53537.1; -; mRNA.
DR   EMBL; BC052001; AAH52001.1; -; mRNA.
DR   EMBL; BC058617; AAH58617.1; -; mRNA.
DR   CCDS; CCDS24896.1; -.
DR   RefSeq; NP_031937.1; NM_007911.5.
DR   PDB; 3D12; X-ray; 3.00 A; B/E=29-169.
DR   PDBsum; 3D12; -.
DR   AlphaFoldDB; O35393; -.
DR   SMR; O35393; -.
DR   BioGRID; 199396; 5.
DR   DIP; DIP-44833N; -.
DR   IntAct; O35393; 6.
DR   MINT; O35393; -.
DR   STRING; 10090.ENSMUSP00000004036; -.
DR   GlyCosmos; O35393; 1 site, No reported glycans.
DR   GlyGen; O35393; 1 site.
DR   iPTMnet; O35393; -.
DR   PhosphoSitePlus; O35393; -.
DR   SwissPalm; O35393; -.
DR   PaxDb; 10090-ENSMUSP00000004036; -.
DR   PeptideAtlas; O35393; -.
DR   ProteomicsDB; 275443; -.
DR   Antibodypedia; 644; 322 antibodies from 30 providers.
DR   DNASU; 13643; -.
DR   Ensembl; ENSMUST00000004036.6; ENSMUSP00000004036.6; ENSMUSG00000003934.6.
DR   GeneID; 13643; -.
DR   KEGG; mmu:13643; -.
DR   UCSC; uc007jqi.2; mouse.
DR   AGR; MGI:109196; -.
DR   CTD; 1949; -.
DR   MGI; MGI:109196; Efnb3.
DR   VEuPathDB; HostDB:ENSMUSG00000003934; -.
DR   eggNOG; KOG3858; Eukaryota.
DR   GeneTree; ENSGT00940000160323; -.
DR   HOGENOM; CLU_072080_0_0_1; -.
DR   InParanoid; O35393; -.
DR   OMA; IYWNSMN; -.
DR   OrthoDB; 5402021at2759; -.
DR   PhylomeDB; O35393; -.
DR   Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR   Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-MMU-3928664; Ephrin signaling.
DR   Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR   BioGRID-ORCS; 13643; 2 hits in 76 CRISPR screens.
DR   ChiTaRS; Efnb3; mouse.
DR   EvolutionaryTrace; O35393; -.
DR   PRO; PR:O35393; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; O35393; Protein.
DR   Bgee; ENSMUSG00000003934; Expressed in embryonic brain and 223 other cell types or tissues.
DR   ExpressionAtlas; O35393; baseline and differential.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098839; C:postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR   GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0016198; P:axon choice point recognition; IMP:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; IDA:ARUK-UCL.
DR   GO; GO:1905608; P:positive regulation of presynapse assembly; ISO:MGI.
DR   GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:MGI.
DR   GO; GO:0031295; P:T cell costimulation; IDA:MGI.
DR   GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IDA:SynGO.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR031328; Ephrin.
DR   InterPro; IPR019765; Ephrin_CS.
DR   InterPro; IPR001799; Ephrin_RBD.
DR   PANTHER; PTHR11304; EPHRIN; 1.
DR   PANTHER; PTHR11304:SF34; EPHRIN-B3; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR   PROSITE; PS51551; EPHRIN_RBD_2; 1.
DR   Genevisible; O35393; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Membrane; Methylation; Neurogenesis; Phosphoprotein;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..340
FT                   /note="Ephrin-B3"
FT                   /id="PRO_0000008396"
FT   TOPO_DOM        28..227
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        249..340
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..167
FT                   /note="Ephrin RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   REGION          168..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           338..340
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        182..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         271
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         274
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15768"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   DISULFID        62..104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   DISULFID        92..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   STRAND          57..62
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   STRAND          80..84
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   HELIX           87..90
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   STRAND          107..109
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   STRAND          111..119
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   STRAND          134..139
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   TURN            145..149
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:3D12"
FT   STRAND          162..166
FT                   /evidence="ECO:0007829|PDB:3D12"
SQ   SEQUENCE   340 AA;  35885 MW;  52F3D58FD209A6B8 CRC64;
     MGAPHFGPGG VQVGALLLLG FAGLVSGLSL EPVYWNSANK RFQAEGGYVL YPQIGDRLDL
     LCPRARPPGP HSSPSYEFYK LYLVEGAQGR RCEAPPAPNL LLTCDRPDLD LRFTIKFQEY
     SPNLWGHEFR SHHDYYIIAT SDGTREGLES LQGGVCLTRG MKVLLRVGQS PRGGAVPRKP
     VSEMPMERDR GAAHSAEPGR DTIPGDPSSN ATSRGAEGPL PPPSMPAVAG AAGGMALLLL
     GVAGAGGAMC WRRRRAKPSE SRHPGPGSFG RGGSLGLGGG GGMGPREAEP GELGIALRGG
     GTADPPFCPH YEKVSGDYGH PVYIVQDGPP QSPPNIYYKV
//