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P52795 (EFNB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin-B1
Alternative name(s):
CEK5 receptor ligand
Short name=CEK5-L
ELK ligand
Short name=ELK-L
EPH-related receptor tyrosine kinase ligand 2
Short name=LERK-2
Stimulated by retinoic acid gene 1 protein
Gene names
Name:Efnb1
Synonyms:Epl2, Eplg2, Lerk2, Stra1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length345 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. Binds to the receptor tyrosine kinases EPHB3 (preferred), EPHB1 and EPHA1. 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. Ref.5

Subunit structure

Interacts with GRIP1 and GRIP2.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed on lateral floor plate cells, specifically on commissural axon segments that have passed through the floor plate. Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disc.

Developmental stage

Expressed in the floor plate throughout the period of commissural axon pathfinding.

Post-translational modification

Inducible phosphorylation of tyrosine residues in the cytoplasmic domain.

Sequence similarities

Belongs to the ephrin family.

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

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 345321Ephrin-B1
PRO_0000008388

Regions

Topological domain25 – 236212Extracellular Potential
Transmembrane237 – 25721Helical; Potential
Topological domain258 – 34588Cytoplasmic Potential
Domain30 – 164135Ephrin RBD
Motif343 – 3453PDZ-binding Potential

Amino acid modifications

Modified residue2861Phosphoserine By similarity
Glycosylation1391N-linked (GlcNAc...) Potential
Disulfide bond64 ↔ 101 By similarity
Disulfide bond89 ↔ 153 By similarity

Experimental info

Sequence conflict901S → T in AAA53231. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P52795 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 8C96FD3DC5CBC405

FASTA34537,859
        10         20         30         40         50         60 
MARPGQRWLS KWLVAMVVLT LCRLATPLAK NLEPVSWSSL NPKFLSGKGL VIYPKIGDKL 

        70         80         90        100        110        120 
DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT CNKPHQEIRF TIKFQEFSPN 

       130        140        150        160        170        180 
YMGLEFKKYH DYYITSTSNG SLEGLENREG GVCRTRTMKI VMKVGQDPNA VTPEQLTTSR 

       190        200        210        220        230        240 
PSKESDNTVK TATQAPGRGS QGDSDGKHET VNQEEKSGPG AGGGGSGDSD SFFNSKVALF 

       250        260        270        280        290        300 
AAVGAGCVIF LLIIIFLTVL LLKLRKRHRK HTQQRAAALS LSTLASPKGG SGTAGTEPSD 

       310        320        330        340 
IIIPLRTTEN NYCPHYEKVS GDYGHPVYIV QEMPPQSPAN IYYKV 

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization and chromosomal localization of mouse Eplg2, a gene encoding a binding protein for the receptor tyrosine kinase elk."
Fletcher F.A., Renshaw B., Hollingsworth T., Baum P., Lyman S.D., Jenkins N.A., Gilbert D.J., Copeland N.G., Davison B.L.
Genomics 24:127-132(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[2]"Efficient cloning of cDNAs of retinoic acid-responsive genes in P19 embryonal carcinoma cells and characterization of a novel mouse gene, Stra1 (mouse LERK-2/Eplg2)."
Bouillet P., Oulad-Abdelghani M., Vicaire S., Garnier J.-M., Schuhbaur B., Dolle P., Chambon P.
Dev. Biol. 170:420-433(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"cDNA cloning and characterization of a ligand for the Cek5 receptor protein-tyrosine kinase."
Shao H., Lou L., Pandey A., Pasquale E.B., Dixit V.M.
J. Biol. Chem. 269:26606-26609(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[4]"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].
Strain: FVB/N.
Tissue: Mammary gland.
[5]"Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons."
Imondi R., Wideman C., Kaprielian Z.
Development 127:1397-1410(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U07602 expand/collapse EMBL AC list , U07598, U07599, U07600 Genomic DNA. Translation: AAC53247.1.
Z48781 mRNA. Translation: CAA88695.1.
U12983 mRNA. Translation: AAA53231.1.
BC006797 mRNA. Translation: AAH06797.1.
BC021656 mRNA. Translation: AAH21656.1.
PIRI48780.
RefSeqNP_034240.1. NM_010110.4.
UniGeneMm.3374.

3D structure databases

ProteinModelPortalP52795.
SMRP52795. Positions 32-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199394. 1 interaction.
DIPDIP-29206N.
IntActP52795. 5 interactions.
MINTMINT-1793539.
STRING10090.ENSMUSP00000050716.

PTM databases

PhosphoSiteP52795.

Proteomic databases

PaxDbP52795.
PRIDEP52795.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052839; ENSMUSP00000050716; ENSMUSG00000031217.
GeneID13641.
KEGGmmu:13641.
UCSCuc009tvi.1. mouse.

Organism-specific databases

CTD1947.
MGIMGI:102708. Efnb1.

Phylogenomic databases

eggNOGNOG262190.
HOGENOMHOG000220931.
HOVERGENHBG051448.
InParanoidP52795.
KOK05463.
OMAPDSFFNS.
OrthoDBEOG7288S5.
PhylomeDBP52795.

Gene expression databases

ArrayExpressP52795.
BgeeP52795.
CleanExMM_EFNB1.
GenevestigatorP52795.

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

NextBio284342.
PROP52795.
SOURCESearch...

Entry information

Entry nameEFNB1_MOUSE
AccessionPrimary (citable) accession number: P52795
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot