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Ephrin-B3 (EPH-related receptor transmembrane ligand ELK-L3) (EPH-related receptor tyrosine kinase ligand 8) (LERK-8)

 EFNB3_HUMAN             Reviewed;         340 AA.
Q15768; B2RBW2; D3DTQ6; O00680; Q8TBH7; Q92875;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-OCT-2018, entry version 165.
RecName: Full=Ephrin-B3;
AltName: Full=EPH-related receptor transmembrane ligand ELK-L3;
AltName: Full=EPH-related receptor tyrosine kinase ligand 8;
Short=LERK-8;
Flags: Precursor;
Name=EFNB3; Synonyms=EPLG8, LERK8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Cerretti D.P.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9126477; DOI=10.1006/geno.1997.4615;
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;
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=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
PROTEIN SEQUENCE OF 28-42.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
INTERACTION WITH GRIP1 AND GRIP2.
TISSUE=Fetal brain;
PubMed=10197531; DOI=10.1016/S0896-6273(00)80706-0;
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).
[9]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH NIPAH VIRUS PROTEIN
G, AND MUTAGENESIS OF 124-LEU-TRP-125.
PubMed=16477309; DOI=10.1371/journal.ppat.0020007;
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).
[10]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HENDRA VIRUS
GLYCOPROTEIN.
PubMed=17376907; DOI=10.1128/JVI.02022-06;
Bishop K.A., Stantchev T.S., Hickey A.C., Khetawat D., Bossart K.N.,
Krasnoperov V., Gill P., Feng Y.R., Wang L., Eaton B.T., Wang L.F.,
Broder C.C.;
"Identification of Hendra virus G glycoprotein residues that are
critical for receptor binding.";
J. Virol. 81:5893-5901(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- 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).
{ECO:0000250}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for nipah virus
and hendra virus. {ECO:0000269|PubMed:16477309,
ECO:0000269|PubMed:17376907}.
-!- SUBUNIT: Interacts with GRIP1 and GRIP2.
{ECO:0000269|PubMed:10197531}.
-!- SUBUNIT: (Microbial infection) Interacts with nipah virus and
hendra virus glycoprotein (PubMed:16477309, PubMed:17376907).
{ECO:0000269|PubMed:16477309, ECO:0000269|PubMed:17376907}.
-!- 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. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
-----------------------------------------------------------------------
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EMBL; U57001; AAB05170.1; -; mRNA.
EMBL; U66406; AAC51203.1; -; mRNA.
EMBL; U62775; AAC50707.1; -; mRNA.
EMBL; AK314841; BAG37359.1; -; mRNA.
EMBL; CH471108; EAW90133.1; -; Genomic_DNA.
EMBL; CH471108; EAW90135.1; -; Genomic_DNA.
EMBL; BC022499; AAH22499.1; -; mRNA.
EMBL; BC042944; AAH42944.1; -; mRNA.
CCDS; CCDS11120.1; -.
RefSeq; NP_001397.1; NM_001406.3.
UniGene; Hs.26988; -.
PDB; 4BKF; X-ray; 4.65 A; C/D=27-169.
PDBsum; 4BKF; -.
ProteinModelPortal; Q15768; -.
SMR; Q15768; -.
BioGrid; 108269; 40.
DIP; DIP-59196N; -.
IntAct; Q15768; 9.
STRING; 9606.ENSP00000226091; -.
iPTMnet; Q15768; -.
PhosphoSitePlus; Q15768; -.
BioMuta; EFNB3; -.
DMDM; 2494367; -.
EPD; Q15768; -.
PaxDb; Q15768; -.
PeptideAtlas; Q15768; -.
PRIDE; Q15768; -.
ProteomicsDB; 60749; -.
Ensembl; ENST00000226091; ENSP00000226091; ENSG00000108947.
GeneID; 1949; -.
KEGG; hsa:1949; -.
UCSC; uc002gis.4; human.
CTD; 1949; -.
DisGeNET; 1949; -.
EuPathDB; HostDB:ENSG00000108947.4; -.
GeneCards; EFNB3; -.
HGNC; HGNC:3228; EFNB3.
HPA; HPA001623; -.
MIM; 602297; gene.
neXtProt; NX_Q15768; -.
OpenTargets; ENSG00000108947; -.
PharmGKB; PA27663; -.
eggNOG; KOG3858; Eukaryota.
eggNOG; ENOG4111FMJ; LUCA.
GeneTree; ENSGT00390000005839; -.
HOGENOM; HOG000220931; -.
HOVERGEN; HBG051448; -.
InParanoid; Q15768; -.
KO; K05463; -.
OMA; SSPSYEF; -.
OrthoDB; EOG091G0BPC; -.
PhylomeDB; Q15768; -.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; Q15768; -.
SIGNOR; Q15768; -.
ChiTaRS; EFNB3; human.
GeneWiki; EFNB3; -.
GenomeRNAi; 1949; -.
PMAP-CutDB; Q15768; -.
PRO; PR:Q15768; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108947; Expressed in 157 organ(s), highest expression level in spinal cord.
CleanEx; HS_EFNB3; -.
Genevisible; Q15768; HS.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:CAFA.
GO; GO:0046875; F:ephrin receptor binding; IDA:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; TAS:ProtInc.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
GO; GO:0016198; P:axon choice point recognition; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IBA:GO_Central.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:MGI.
GO; GO:0050771; P:negative regulation of axonogenesis; ISS:ARUK-UCL.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IEA:Ensembl.
Gene3D; 2.60.40.420; -; 1.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR031328; Ephrin.
InterPro; IPR019765; Ephrin_CS.
InterPro; IPR001799; Ephrin_RBD.
PANTHER; PTHR11304; PTHR11304; 1.
Pfam; PF00812; Ephrin; 1.
PRINTS; PR01347; EPHRIN.
ProDom; PD002533; Ephrin; 1.
SUPFAM; SSF49503; SSF49503; 1.
PROSITE; PS01299; EPHRIN_RBD_1; 1.
PROSITE; PS51551; EPHRIN_RBD_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Developmental protein;
Differentiation; Direct protein sequencing; Disulfide bond;
Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Membrane; Methylation; Neurogenesis;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 27 {ECO:0000269|PubMed:15340161}.
CHAIN 28 340 Ephrin-B3.
/FTId=PRO_0000008395.
TOPO_DOM 28 226 Extracellular. {ECO:0000255}.
TRANSMEM 227 247 Helical. {ECO:0000255}.
TOPO_DOM 248 340 Cytoplasmic. {ECO:0000255}.
DOMAIN 28 167 Ephrin RBD. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
MOTIF 338 340 PDZ-binding. {ECO:0000255}.
MOD_RES 271 271 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O35393}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 210 210 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 62 104 {ECO:0000255|PROSITE-ProRule:PRU00884}.
DISULFID 92 156 {ECO:0000255|PROSITE-ProRule:PRU00884}.
VARIANT 166 166 R -> Q.
/FTId=VAR_002356.
MUTAGEN 124 125 LW->YM: Complete loss of Nipah protein G
binding. {ECO:0000269|PubMed:16477309}.
SEQUENCE 340 AA; 35835 MW; EDFF2A23C2FDE79F CRC64;
MGPPHSGPGG VRVGALLLLG VLGLVSGLSL EPVYWNSANK RFQAEGGYVL YPQIGDRLDL
LCPRARPPGP HSSPNYEFYK LYLVGGAQGR RCEAPPAPNL LLTCDRPDLD LRFTIKFQEY
SPNLWGHEFR SHHDYYIIAT SDGTREGLES LQGGVCLTRG MKVLLRVGQS PRGGAVPRKP
VSEMPMERDR GAAHSLEPGK ENLPGDPTSN ATSRGAEGPL PPPSMPAVAG AAGGLALLLL
GVAGAGGAMC WRRRRAKPSE SRHPGPGSFG RGGSLGLGGG GGMGPREAEP GELGIALRGG
GAADPPFCPH YEKVSGDYGH PVYIVQDGPP QSPPNIYYKV


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