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UniProtKB/Swiss-Prot entry Q15768


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name EFNB3_HUMAN
Primary accession number Q15768
Secondary accession numbers O00680 Q8TBH7 Q92875
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name Ephrin-B3 [Precursor]
Synonyms EPH-related receptor tyrosine kinase ligand 8
LERK-8
EPH-related receptor transmembrane ligand ELK-L3
Gene name
Name: EFNB3
Synonyms: EPLG8, LERK8
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Cerretti D.P.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
DOI=10.1006/geno.1997.4615; PubMed=9126477 [NCBI, ExPASy, EBI, Israel, Japan]
Tang X.X., Pleasure D.E., Ikegaki N.;
"cDNA cloning, chromosomal localization, and expression pattern of EPLG8, a new member of the EPLG gene family encoding ligands of EPH-related protein-tyrosine kinase receptors.";
Genomics 41:17-24(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain cortex;
PubMed=8808709 [NCBI, ExPASy, EBI, Israel, Japan]
Gale N.W., Flenniken A., Compton D.C., Jenkins N.A., Copeland N.G., Gilbert D.J., Davis S., Wilkinson D.G., Yancopoulos G.D.;
"Elk-L3, a novel transmembrane ligand for the Eph family of receptor tyrosine kinases, expressed in embryonic floor plate, roof plate and hindbrain segments.";
Oncogene 13:1343-1352(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 28-42.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[6]
INTERACTION WITH GRIP1 AND GRIP2.
TISSUE=Fetal brain;
DOI=10.1016/S0896-6273(00)80706-0; PubMed=10197531 [NCBI, ExPASy, EBI, Israel, Japan]
Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H., Klein R.;
"EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains.";
Neuron 22:511-524(1999).
[7]
INTERACTION WITH NIPAH VIRUS PROTEIN G, AND MUTAGENESIS OF 124-LEU-TRP-125.
DOI=10.1371/journal.ppat.0020007; PubMed=16477309 [NCBI, ExPASy, EBI, Israel, Japan]
Negrete O.A., Wolf M.C., Aguilar H.C., Enterlein S., Wang W., Muehlberger E., Su S.V., Bertolotti-Ciarlet A., Flick R., Lee B.;
"Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus.";
PLoS Pathog. 2:78-86(2006).
Comments
  • FUNCTION: May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons (By similarity).
  • SUBUNIT: Interacts with GRIP1 and GRIP2. Binds to Nipah virus G protein.
  • SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
  • TISSUE SPECIFICITY: Highly expressed in brain; expressed in embryonic floor plate, roof plate and hindbrain segments.
  • SIMILARITY: Belongs to the ephrin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U57001; AAB05170.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U66406; AAC51203.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U62775; AAC50707.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022499; AAH22499.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC042944; AAH42944.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001397.1; -.
UniGene Hs.26988
3D structure databases
HSSP P52800; 1IKO. [HSSP ENTRY / PDB]
ModBase Q15768.
PTM databases
PhosphoSite Q15768; -.
Organism-specific databases
H-InvDB HIX0021522; -.
HGNC HGNC:3228; EFNB3.
GenAtlas EFNB3.
HPA HPA001623; -.
MIM 602297; gene. [NCBI / EBI]
PharmGKB PA27663; -.
GeneCards Q15768.
Gene expression databases
ArrayExpress Q15768; -.
CleanEx HS_EFNB3; -.
GermOnline ENSG00000108947; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0046875; Molecular function: ephrin receptor binding (inferred from direct assay from MGI).
GO:0005005; Molecular function: transmembrane-ephrin receptor activity (traceable author statement from ProtInc).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0048013; Biological process: ephrin receptor signaling pathway (inferred from direct assay from MGI).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR008972; Cupredoxin.
IPR001799; Ephrin.
Graphical view of domain structure.
Gene3D G3DSA:2.60.40.420; Cupredoxin; 1.
PANTHER PTHR11304; Ephrin; 1.
Pfam PF00812; Ephrin; 1.
Pfam graphical view of domain structure.
PRINTS PR01347; EPHRIN.
ProDom PD002533; Ephrin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS01299; EPHRIN; 1.
BLOCKS Q15768.
ProtoNet Q15768.
Genome annotation databases
Ensembl ENSG00000108947; Homo sapiens. [Contig view]
GeneID 1949; -.
KEGG hsa:1949; -.
Phylogenomic databases
HOGENOM Q15768; -.
HOVERGEN Q15768; -.
Other
NextBio 7899; -.
SOURCE EFNB3; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Developmental protein; Differentiation; Direct protein sequencing; Glycoprotein; Host-virus interaction; Membrane; Neurogenesis; Polymorphism; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    27  27      
CHAIN   28   340  313     Ephrin-B3. PRO_0000008395
TOPO_DOM   28   226  199     Extracellular (Potential). 
TRANSMEM   227   247  21     Potential. 
TOPO_DOM   248   340  93     Cytoplasmic (Potential). 
MOTIF   338   340  3     PDZ-binding (Potential). 
CARBOHYD   210   210        N-linked (GlcNAc...) (Potential). 
DISULFID   62   104        By similarity. 
DISULFID   92   156        By similarity. 
VARIANT   166   166  1     R -> Q. VAR_002356 
MUTAGEN   124   125        LW->YM: Complete loss of Nipah protein G binding. 
Sequence information
Length: 340 AA [This is the length of the unprocessed precursor] Molecular weight: 35835 Da [This is the MW of the unprocessed precursor] CRC64: EDFF2A23C2FDE79F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGPPHSGPGG VRVGALLLLG VLGLVSGLSL EPVYWNSANK RFQAEGGYVL YPQIGDRLDL 

        70         80         90        100        110        120 
LCPRARPPGP HSSPNYEFYK LYLVGGAQGR RCEAPPAPNL LLTCDRPDLD LRFTIKFQEY 

       130        140        150        160        170        180 
SPNLWGHEFR SHHDYYIIAT SDGTREGLES LQGGVCLTRG MKVLLRVGQS PRGGAVPRKP 

       190        200        210        220        230        240 
VSEMPMERDR GAAHSLEPGK ENLPGDPTSN ATSRGAEGPL PPPSMPAVAG AAGGLALLLL 

       250        260        270        280        290        300 
GVAGAGGAMC WRRRRAKPSE SRHPGPGSFG RGGSLGLGGG GGMGPREAEP GELGIALRGG 

       310        320        330        340 
GAADPPFCPH YEKVSGDYGH PVYIVQDGPP QSPPNIYYKV 

Q15768 in FASTA format

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