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Q15768 (EFNB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin-B3
Alternative name(s):
EPH-related receptor transmembrane ligand ELK-L3
EPH-related receptor tyrosine kinase ligand 8
Short name=LERK-8
Gene names
Name:EFNB3
Synonyms:EPLG8, LERK8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. 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 structure

Interacts with GRIP1 and GRIP2. Binds to Nipah virus G protein. Ref.8 Ref.9

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.

Sequence similarities

Belongs to the ephrin family.

Contains 1 ephrin RBD (ephrin receptor-binding) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.7
Chain28 – 340313Ephrin-B3
PRO_0000008395

Regions

Topological domain28 – 226199Extracellular Potential
Transmembrane227 – 24721Helical; Potential
Topological domain248 – 34093Cytoplasmic Potential
Domain28 – 167140Ephrin RBD
Motif338 – 3403PDZ-binding Potential

Amino acid modifications

Glycosylation2101N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 104 By similarity
Disulfide bond92 ↔ 156 By similarity

Natural variations

Natural variant1661R → Q.
VAR_002356

Experimental info

Mutagenesis124 – 1252LW → YM: Complete loss of Nipah protein G binding. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q15768 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: EDFF2A23C2FDE79F

FASTA34035,835
        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 

« Hide

References

« Hide 'large scale' references
[1]Cerretti D.P.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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."
Tang X.X., Pleasure D.E., Ikegaki N.
Genomics 41:17-24(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Elk-L3, a novel transmembrane ligand for the Eph family of receptor tyrosine kinases, expressed in embryonic floor plate, roof plate and hindbrain segments."
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.
Oncogene 13:1343-1352(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain cortex.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-42.
[8]"EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains."
Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H., Klein R.
Neuron 22:511-524(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIP1 AND GRIP2.
Tissue: Fetal brain.
[9]"Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus."
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.
PLoS Pathog. 2:78-86(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NIPAH VIRUS PROTEIN G, MUTAGENESIS OF 124-LEU-TRP-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57001 mRNA. Translation: AAB05170.1.
U66406 mRNA. Translation: AAC51203.1.
U62775 mRNA. Translation: AAC50707.1.
AK314841 mRNA. Translation: BAG37359.1.
CH471108 Genomic DNA. Translation: EAW90133.1.
CH471108 Genomic DNA. Translation: EAW90135.1.
BC022499 mRNA. Translation: AAH22499.1.
BC042944 mRNA. Translation: AAH42944.1.
RefSeqNP_001397.1. NM_001406.3.
UniGeneHs.26988.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BKFX-ray4.65C/D27-169[»]
ProteinModelPortalQ15768.
SMRQ15768. Positions 29-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108269. 7 interactions.
DIPDIP-59196N.
IntActQ15768. 4 interactions.
STRING9606.ENSP00000226091.

PTM databases

PhosphoSiteQ15768.

Polymorphism databases

DMDM2494367.

Proteomic databases

PaxDbQ15768.
PRIDEQ15768.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226091; ENSP00000226091; ENSG00000108947.
GeneID1949.
KEGGhsa:1949.
UCSCuc002gis.3. human.

Organism-specific databases

CTD1949.
GeneCardsGC17P007608.
HGNCHGNC:3228. EFNB3.
HPAHPA001623.
MIM602297. gene.
neXtProtNX_Q15768.
PharmGKBPA27663.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268537.
HOGENOMHOG000220931.
HOVERGENHBG051448.
InParanoidQ15768.
KOK05463.
OMAPGKENMP.
OrthoDBEOG7288S5.
PhylomeDBQ15768.

Enzyme and pathway databases

SignaLinkQ15768.

Gene expression databases

BgeeQ15768.
CleanExHS_EFNB3.
GenevestigatorQ15768.

Family and domain databases

Gene3D2.60.40.420. 1 hit.
InterProIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
PANTHERPTHR11304. PTHR11304. 1 hit.
PfamPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSPR01347. EPHRIN.
ProDomPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF49503. SSF49503. 1 hit.
PROSITEPS01299. EPHRIN_RBD_1. 1 hit.
PS51551. EPHRIN_RBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEFNB3. human.
GeneWikiEFNB3.
GenomeRNAi1949.
NextBio7899.
PMAP-CutDBQ15768.
PROQ15768.
SOURCESearch...

Entry information

Entry nameEFNB3_HUMAN
AccessionPrimary (citable) accession number: Q15768
Secondary accession number(s): B2RBW2 expand/collapse secondary AC list , D3DTQ6, O00680, Q8TBH7, Q92875
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM