Q15768 (EFNB3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Differentiation Host-virus interaction Neurogenesis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adult walking behavior Inferred from electronic annotation. Source: Compara axon choice point recognition Inferred from electronic annotation. Source: Compara cell-cell signaling Traceable author statement Ref.2. Source: ProtInc nervous system development Traceable author statement Ref.2. Source: ProtInc virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to plasma membrane Traceable author statement Ref.2. Source: ProtInc
Molecular_function	ephrin receptor binding Inferred from direct assay Ref.3. Source: MGI transmembrane-ephrin receptor activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Ref.7
	Chain	28 – 340	313	Ephrin-B3		PRO_0000008395
Regions
	Topological domain	28 – 226	199	Extracellular Potential
	Transmembrane	227 – 247	21	Helical; Potential
	Topological domain	248 – 340	93	Cytoplasmic Potential
	Domain	28 – 167	140	Ephrin RBD
	Motif	338 – 340	3	PDZ-binding Potential
Amino acid modifications
	Glycosylation	210	1	N-linked (GlcNAc...) Potential
	Disulfide bond	62 ↔ 104		By similarity
	Disulfide bond	92 ↔ 156		By similarity
Natural variations
	Natural variant	166	1	R → Q.		VAR_002356
Experimental info
	Mutagenesis	124 – 125	2	LW → YM: Complete loss of Nipah protein G binding. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q15768 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: EDFF2A23C2FDE79F	FASTA	340	35,835
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00019501.
RefSeq	NP_001397.1. NM_001406.3.
UniGene	Hs.26988.
3D structure databases
ProteinModelPortal	Q15768.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-59196N.
IntAct	Q15768. 4 interactions.
STRING	9606.ENSP00000226091.
PTM databases
PhosphoSite	Q15768.
Polymorphism databases
DMDM	2494367.
Proteomic databases
PaxDb	Q15768.
PRIDE	Q15768.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000226091; ENSP00000226091; ENSG00000108947.
GeneID	1949.
KEGG	hsa:1949.
UCSC	uc002gis.3. human.
Organism-specific databases
CTD	1949.
GeneCards	GC17P007608.
HGNC	HGNC:3228. EFNB3.
HPA	HPA001623.
MIM	602297. gene.
neXtProt	NX_Q15768.
PharmGKB	PA27663.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG268537.
HOGENOM	HOG000220931.
HOVERGEN	HBG051448.
InParanoid	Q15768.
KO	K05463.
OMA	MGAPHSG.
OrthoDB	EOG4ZW5BN.
PhylomeDB	Q15768.
Enzyme and pathway databases
Pathway_Interaction_DB	ephbfwdpathway. EPHB forward signaling.
Gene expression databases
Bgee	Q15768.
CleanEx	HS_EFNB3.
Genevestigator	Q15768.
GermOnline	ENSG00000108947. Homo sapiens.
Family and domain databases
Gene3D	2.60.40.420. 1 hit.
InterPro	IPR008972. Cupredoxin. IPR001799. Ephrin. IPR019765. Ephrin_CS. [Graphical view]
PANTHER	PTHR11304. PTHR11304. 1 hit.
Pfam	PF00812. Ephrin. 1 hit. [Graphical view]
PRINTS	PR01347. EPHRIN.
ProDom	PD002533. Ephrin. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF49503. Cupredoxin. 1 hit.
PROSITE	PS01299. EPHRIN_RBD_1. 1 hit. PS51551. EPHRIN_RBD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	EFNB3. human.
GenomeRNAi	1949.
NextBio	7899.
PMAP-CutDB	Q15768.
SOURCE	Search...

Entry information

Entry name

EFNB3_HUMAN

Accession

Primary (citable) accession number: Q15768
Secondary accession number(s): B2RBW2 , D3DTQ6, O00680, Q8TBH7, Q92875

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.