[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0161-5890(95)00108-5; PubMed=8559144 [NCBI, ExPASy, EBI, Israel, Japan] Cerretti D.P., Vanden Bos T., Nelson N., Kozlosky C.J., Reddy P., Maraskovsky E., Park L.S., Lyman S.D., Copeland N.G., Gilbert D.J., Jenkins N.A., Fletcher R.A.; "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases."; Mol. Immunol. 32:1197-1205(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=CB57BL/6J X SJL/J; PubMed=7534404 [NCBI, ExPASy, EBI, Israel, Japan] Bennett B.D., Zeigler F.C., Gu Q., Fendly B., Goddard A.D., Gillett N., Matthews W.; "Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk."; Proc. Natl. Acad. Sci. U.S.A. 92:1866-1870(1995).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=ICR; TISSUE=Brain; PubMed=7651410 [NCBI, ExPASy, EBI, Israel, Japan] Bergemann A.D., Cheng H.J., Brambilla R., Klein R., Flanagan J.G.; "ELF-2, a new member of the Eph ligand family, is segmentally expressed in mouse embryos in the region of the hindbrain and newly forming somites."; Mol. Cell. Biol. 15:4921-4929(1995).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=C57BL/6; 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]	FUNCTION. PubMed=10704386 [NCBI, ExPASy, EBI, Israel, Japan] Imondi R., Wideman C., Kaprielian Z.; "Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons."; Development 127:1397-1410(2000).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-307, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0608638104; PubMed=17389395 [NCBI, ExPASy, EBI, Israel, Japan] Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; "Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
[7]	X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 30-170. DOI=10.1016/S1534-5807(01)00002-8; PubMed=11703926 [NCBI, ExPASy, EBI, Israel, Japan] Toth J., Cutforth T., Gelinas A.D., Bethoney K.A., Bard J., Harrison C.J.; "Crystal structure of an ephrin ectodomain."; Dev. Cell 1:83-92(2001).
[8]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-168 IN COMPLEX WITH EPHB2. DOI=10.1038/414933a; PubMed=11780069 [NCBI, ExPASy, EBI, Israel, Japan] Himanen J.-P., Rajashankar K.R., Lackmann M., Cowan C.A., Henkemeyer M., Nikolov D.B.; "Crystal structure of an Eph receptor-ephrin complex."; Nature 414:933-938(2001).

Comments

FUNCTION: Binds to the receptor tyrosine kinases EPHB2 and EPHB4. May play a role in constraining the orientation of longitudinally projecting axons.
SUBUNIT: Interacts with PDZRN3 (By similarity). Binds to the receptor tyrosine kinase EPHB4.
INTERACTION:
Q03137:Epha4; NbExp=1; IntAct=EBI-1032676, EBI-1539152;
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 disk.
DEVELOPMENTAL STAGE: Expressed in the floor plate throughout the period of commissural axon pathfinding.
PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic domain (By similarity).
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

U16819; AAA99708.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L38847; AAC42052.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U30244; AAA82934.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC057009; AAH57009.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I49766; I49766.

NP_034241.2; -.

3D structure databases

PDB

1IKO; X-ray; 1.92 A; P=30-207.	[ExPASy / RCSB / EBI]
1KGY; X-ray; 2.70 A; E/F/G/H=31-168.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1IKO; -.
1KGY; -.

ModBase

P52800.

Protein-protein interaction databases

DIP

DIP:29208N; -.

IntAct

P52800; 2.

PTM databases

PhosphoSite

P52800; -.

Organism-specific databases

MGI

MGI:105097; Efnb2.

Gene expression databases

ArrayExpress

P52800; -.

CleanEx

MM_EFNB2; -.
MM_ELF2; -.

GermOnline

ENSMUSG00000001300; Mus musculus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005886;	Cellular component: plasma membrane (inferred from direct assay from MGI).
GO:0005102;	Molecular function: receptor binding (inferred from physical interaction from MGI).
GO:0030154;	Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
GO:0001945;	Biological process: lymph vessel development (inferred from mutant phenotype from MGI).
GO:0007399;	Biological process: nervous system development (inferred from electronic annotation from UniProtKB-KW).
GO:0007219;	Biological process: Notch signaling pathway (inferred from direct assay from UniProtKB).
GO:0009887;	Biological process: organ morphogenesis (inferred from mutant phenotype from MGI).
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.

Proteomics databases

PRIDE

P52800; -.

Genome annotation databases

Ensembl

ENSMUSG00000001300; Mus musculus. [Contig view]

GeneID

13642; -.

KEGG

mmu:13642; -.

Phylogenomic databases

HOVERGEN

P52800; -.

Other

284346; -.

Efnb2; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Developmental protein; Differentiation; Glycoprotein; Membrane; Neurogenesis; Phosphoprotein; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 28`	`28`	`Potential.`
`CHAIN`	`29 336`	`308`	`Ephrin-B2.`	`PRO_0000008393`
`TOPO_DOM`	`29 232`	`204`	`Extracellular (Potential).`
`TRANSMEM`	`233 253`	`21`	`Potential.`
`TOPO_DOM`	`254 336`	`83`	`Cytoplasmic (Potential).`
`MOTIF`	`334 336`	`3`	`PDZ-binding (Potential).`
`MOD_RES`	`307 307`		`Phosphotyrosine.`
`MOD_RES`	`328 328`		`Phosphoserine (By similarity).`
`MOD_RES`	`333 333`		`Phosphotyrosine (By similarity).`
`CARBOHYD`	`39 39`		`N-linked (GlcNAc...).`
`CARBOHYD`	`142 142`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`65 104`
`DISULFID`	`92 156`
`CONFLICT`	`3 4`		`Missing (in Ref. 3).`
`CONFLICT`	`177 177`		`A -> T (in Ref. 1; AAA99708).`
`TURN`	`47 49`	`3`
`STRAND`	`50 53`	`4`
`STRAND`	`60 64`	`5`
`STRAND`	`70 72`	`3`
`STRAND`	`78 84`	`7`
`HELIX`	`86 91`	`6`
`STRAND`	`101 104`	`4`
`STRAND`	`112 116`	`5`
`STRAND`	`133 138`	`6`
`HELIX`	`145 147`	`3`
`HELIX`	`154 158`	`5`
`STRAND`	`162 167`	`6`

Sequence information

Length: 336 AA [This is the length of the unprocessed precursor]

Molecular weight: 37202 Da [This is the MW of the unprocessed precursor]

CRC64: D08894996E399554 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAMARSRRDS VWKYCWGLLM VLCRTAISRS IVLEPIYWNS SNSKFLPGQG LVLYPQIGDK 

        70         80         90        100        110        120 
LDIICPKVDS KTVGQYEYYK VYMVDKDQAD RCTIKKENTP LLNCARPDQD VKFTIKFQEF 

       130        140        150        160        170        180 
SPNLWGLEFQ KNKDYYIIST SNGSLEGLDN QEGGVCQTRA MKILMKVGQD ASSAGSARNH 

       190        200        210        220        230        240 
GPTRRPELEA GTNGRSSTTS PFVKPNPGSS TDGNSAGHSG NNLLGSEVAL FAGIASGCII 

       250        260        270        280        290        300 
FIVIIITLVV LLLKYRRRHR KHSPQHTTTL SLSTLATPKR GGNNNGSEPS DVIIPLRTAD 

       310        320        330 
SVFCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV

P52800 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools