ID   EFNB3_HUMAN             Reviewed;         340 AA.
AC   Q15768; O00680; Q8TBH7; Q92875;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   07-JUL-2009, entry version 86.
DE   RecName: Full=Ephrin-B3;
DE   AltName: Full=EPH-related receptor tyrosine kinase ligand 8;
DE            Short=LERK-8;
DE   AltName: Full=EPH-related receptor transmembrane ligand ELK-L3;
DE   Flags: Precursor;
GN   Name=EFNB3; Synonyms=EPLG8, LERK8;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cerretti D.P.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=97271551; PubMed=9126477; DOI=10.1006/geno.1997.4615;
RA   Tang X.X., Pleasure D.E., Ikegaki N.;
RT   "cDNA cloning, chromosomal localization, and expression pattern of
RT   EPLG8, a new member of the EPLG gene family encoding ligands of EPH-
RT   related protein-tyrosine kinase receptors.";
RL   Genomics 41:17-24(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain cortex;
RX   MEDLINE=96404527; PubMed=8808709;
RA   Gale N.W., Flenniken A., Compton D.C., Jenkins N.A., Copeland N.G.,
RA   Gilbert D.J., Davis S., Wilkinson D.G., Yancopoulos G.D.;
RT   "Elk-L3, a novel transmembrane ligand for the Eph family of receptor
RT   tyrosine kinases, expressed in embryonic floor plate, roof plate and
RT   hindbrain segments.";
RL   Oncogene 13:1343-1352(1996).
RN   [4]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 28-42.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [6]
RP   INTERACTION WITH GRIP1 AND GRIP2.
RC   TISSUE=Fetal brain;
RX   MEDLINE=99211388; PubMed=10197531; DOI=10.1016/S0896-6273(00)80706-0;
RA   Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H.,
RA   Klein R.;
RT   "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft
RT   membrane microdomains.";
RL   Neuron 22:511-524(1999).
RN   [7]
RP   INTERACTION WITH NIPAH VIRUS PROTEIN G, AND MUTAGENESIS OF
RP   124-LEU-TRP-125.
RX   PubMed=16477309; DOI=10.1371/journal.ppat.0020007;
RA   Negrete O.A., Wolf M.C., Aguilar H.C., Enterlein S., Wang W.,
RA   Muehlberger E., Su S.V., Bertolotti-Ciarlet A., Flick R., Lee B.;
RT   "Two key residues in ephrinB3 are critical for its use as an
RT   alternative receptor for Nipah virus.";
RL   PLoS Pathog. 2:78-86(2006).
CC   -!- FUNCTION: May play a pivotal role in forebrain function. Binds to,
CC       and induce the collapse of, commissural axons/growth cones in
CC       vitro. May play a role in constraining the orientation of
CC       longitudinally projecting axons (By similarity).
CC   -!- SUBUNIT: Interacts with GRIP1 and GRIP2. Binds to Nipah virus G
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain; expressed in
CC       embryonic floor plate, roof plate and hindbrain segments.
CC   -!- SIMILARITY: Belongs to the ephrin family.
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DR   EMBL; U57001; AAB05170.1; -; mRNA.
DR   EMBL; U66406; AAC51203.1; -; mRNA.
DR   EMBL; U62775; AAC50707.1; -; mRNA.
DR   EMBL; BC022499; AAH22499.1; -; mRNA.
DR   EMBL; BC042944; AAH42944.1; -; mRNA.
DR   IPI; IPI00019501; -.
DR   RefSeq; NP_001397.1; -.
DR   UniGene; Hs.26988; -.
DR   HSSP; P52800; 1IKO.
DR   PhosphoSite; Q15768; -.
DR   PRIDE; Q15768; -.
DR   Ensembl; ENSG00000108947; Homo sapiens.
DR   GeneID; 1949; -.
DR   KEGG; hsa:1949; -.
DR   UCSC; uc002gis.1; human.
DR   GeneCards; GC17P007549; -.
DR   H-InvDB; HIX0021522; -.
DR   HGNC; HGNC:3228; EFNB3.
DR   HPA; HPA001623; -.
DR   MIM; 602297; gene.
DR   PharmGKB; PA27663; -.
DR   HOGENOM; Q15768; -.
DR   HOVERGEN; Q15768; -.
DR   OMA; Q15768; MGAPHSG.
DR   Pathway_Interaction_DB; ephbfwdpathway; EPHB forward signaling.
DR   NextBio; 7899; -.
DR   PMAP-CutDB; Q15768; -.
DR   ArrayExpress; Q15768; -.
DR   Bgee; Q15768; -.
DR   CleanEx; HS_EFNB3; -.
DR   GermOnline; ENSG00000108947; Homo sapiens.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR   GO; GO:0046875; F:ephrin receptor binding; IDA:MGI.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; TAS:ProtInc.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR001799; Ephrin.
DR   InterPro; IPR019765; Ephrin_CS.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 1.
DR   PANTHER; PTHR11304; Ephrin; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   ProDom; PD002533; Ephrin; 1.
DR   PROSITE; PS01299; EPHRIN; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Developmental protein; Differentiation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Host-virus interaction; Membrane; Neurogenesis; Polymorphism; Signal;
KW   Transmembrane.
FT   SIGNAL        1     27
FT   CHAIN        28    340       Ephrin-B3.
FT                                /FTId=PRO_0000008395.
FT   TOPO_DOM     28    226       Extracellular (Potential).
FT   TRANSMEM    227    247       Potential.
FT   TOPO_DOM    248    340       Cytoplasmic (Potential).
FT   MOTIF       338    340       PDZ-binding (Potential).
FT   CARBOHYD    210    210       N-linked (GlcNAc...) (Potential).
FT   DISULFID     62    104       By similarity.
FT   DISULFID     92    156       By similarity.
FT   VARIANT     166    166       R -> Q.
FT                                /FTId=VAR_002356.
FT   MUTAGEN     124    125       LW->YM: Complete loss of Nipah protein G
FT                                binding.
SQ   SEQUENCE   340 AA;  35835 MW;  EDFF2A23C2FDE79F CRC64;
     MGPPHSGPGG VRVGALLLLG VLGLVSGLSL EPVYWNSANK RFQAEGGYVL YPQIGDRLDL
     LCPRARPPGP HSSPNYEFYK LYLVGGAQGR RCEAPPAPNL LLTCDRPDLD LRFTIKFQEY
     SPNLWGHEFR SHHDYYIIAT SDGTREGLES LQGGVCLTRG MKVLLRVGQS PRGGAVPRKP
     VSEMPMERDR GAAHSLEPGK ENLPGDPTSN ATSRGAEGPL PPPSMPAVAG AAGGLALLLL
     GVAGAGGAMC WRRRRAKPSE SRHPGPGSFG RGGSLGLGGG GGMGPREAEP GELGIALRGG
     GAADPPFCPH YEKVSGDYGH PVYIVQDGPP QSPPNIYYKV
//