EFNB3_MOUSE
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 03-AUG-2022, entry version 168.
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 GlyGen; O35393; 1 site.
DR iPTMnet; O35393; -.
DR PhosphoSitePlus; O35393; -.
DR SwissPalm; O35393; -.
DR PaxDb; O35393; -.
DR PeptideAtlas; O35393; -.
DR PRIDE; O35393; -.
DR ProteomicsDB; 275443; -.
DR Antibodypedia; 644; 299 antibodies from 30 providers.
DR DNASU; 13643; -.
DR Ensembl; ENSMUST00000004036; ENSMUSP00000004036; ENSMUSG00000003934.
DR GeneID; 13643; -.
DR KEGG; mmu:13643; -.
DR UCSC; uc007jqi.2; mouse.
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; VMAANLE; -.
DR OrthoDB; 903831at2759; -.
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 71 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 220 other tissues.
DR ExpressionAtlas; O35393; baseline and differential.
DR Genevisible; O35393; MM.
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:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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: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; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR019765; Ephrin_CS.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; PTHR11304; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01347; EPHRIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
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
