EFNB2_HUMAN
ID EFNB2_HUMAN Reviewed; 333 AA.
AC P52799; Q5JV56;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Ephrin-B2;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 5;
DE Short=LERK-5;
DE AltName: Full=HTK ligand;
DE Short=HTK-L;
DE Flags: Precursor;
GN Name=EFNB2; Synonyms=EPLG5, HTKL, LERK5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8559144; DOI=10.1016/0161-5890(95)00108-5;
RA Cerretti D.P., Vanden Bos T., Nelson N., Kozlosky C.J., Reddy P.,
RA Maraskovsky E., Park L.S., Lyman S.D., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Fletcher R.A.;
RT "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine
RT kinases.";
RL Mol. Immunol. 32:1197-1205(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7534404; DOI=10.1073/pnas.92.6.1866;
RA Bennett B.D., Zeigler F.C., Gu Q., Fendly B., Goddard A.D., Gillett N.,
RA Matthews W.;
RT "Molecular cloning of a ligand for the EPH-related receptor protein-
RT tyrosine kinase Htk.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:1866-1870(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9533549;
RA Vogt T., Stolz W., Welsh J., Jung B., Kerbel R.S., Kobayashi H.,
RA Landthaler M., McClelland M.;
RT "Overexpression of Lerk-5/Eplg5 messenger RNA: a novel marker for increased
RT tumorigenicity and metastatic potential in human malignant melanomas.";
RL Clin. Cancer Res. 4:791-797(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION IN ANGIOGENESIS.
RX PubMed=12734395; DOI=10.1242/jcs.00426;
RA Fueller T., Korff T., Kilian A., Dandekar G., Augustin H.G.;
RT "Forward EphB4 signaling in endothelial cells controls cellular repulsion
RT and segregation from ephrinB2 positive cells.";
RL J. Cell Sci. 116:2461-2470(2003).
RN [7]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH NIPAH VIRUS
RP GLYCOPROTEIN.
RX PubMed=16007075; DOI=10.1038/nature03838;
RA Negrete O.A., Levroney E.L., Aguilar H.C., Bertolotti-Ciarlet A.,
RA Nazarian R., Tajyar S., Lee B.;
RT "EphrinB2 is the entry receptor for Nipah virus, an emergent deadly
RT paramyxovirus.";
RL Nature 436:401-405(2005).
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HENDRA VIRUS
RP GLYCOPROTEIN.
RX PubMed=15998730; DOI=10.1073/pnas.0504887102;
RA Bonaparte M.I., Dimitrov A.S., Bossart K.N., Crameri G., Mungall B.A.,
RA Bishop K.A., Choudhry V., Dimitrov D.S., Wang L.F., Eaton B.T.,
RA Broder C.C.;
RT "Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah
RT virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10652-10657(2005).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH NIPAH VIRUS GLYCOPROTEIN,
RP AND MUTAGENESIS OF 121-LEU-TRP-122.
RX PubMed=16477309; DOI=10.1371/journal.ppat.0020007;
RA Negrete O.A., Wolf M.C., Aguilar H.C., Enterlein S., Wang W.,
RA Muehlberger E., Su S.V., Bertolotti-Ciarlet A., Flick R., Lee B.;
RT "Two key residues in ephrinB3 are critical for its use as an alternative
RT receptor for Nipah virus.";
RL PLoS Pathog. 2:78-86(2006).
RN [10]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HENDRA VIRUS
RP GLYCOPROTEIN.
RX PubMed=17376907; DOI=10.1128/jvi.02022-06;
RA Bishop K.A., Stantchev T.S., Hickey A.C., Khetawat D., Bossart K.N.,
RA Krasnoperov V., Gill P., Feng Y.R., Wang L., Eaton B.T., Wang L.F.,
RA Broder C.C.;
RT "Identification of Hendra virus G glycoprotein residues that are critical
RT for receptor binding.";
RL J. Virol. 81:5893-5901(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=28931592; DOI=10.1091/mbc.e17-07-0450;
RA Okumura F., Joo-Okumura A., Obara K., Petersen A., Nishikimi A., Fukui Y.,
RA Nakatsukasa K., Kamura T.;
RT "Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by
RT EphB2.";
RL Mol. Biol. Cell 28:3532-3541(2017).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 28-165 IN COMPLEX WITH EPHB4, AND
RP DISULFIDE BONDS.
RX PubMed=16867992; DOI=10.1074/jbc.m605766200;
RA Chrencik J.E., Brooun A., Kraus M.L., Recht M.I., Kolatkar A.R., Han G.W.,
RA Seifert J.M., Widmer H., Auer M., Kuhn P.;
RT "Structural and biophysical characterization of the EphB4*ephrinB2 protein-
RT protein interaction and receptor specificity.";
RL J. Biol. Chem. 281:28185-28192(2006).
RN [14] {ECO:0007744|PDB:2I85}
RP STRUCTURE BY NMR OF 25-166, AND DISULFIDE BONDS.
RA Ran X., Fan J., Song J.;
RT "NMR solution structure of human ephrinB2 ectodomain.";
RL Submitted (SEP-2006) to the PDB data bank.
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-165 IN COMPLEXES WITH NIPAH
RP VIRUS AND HENDRA VIRUS GLYCOPROTEINS, DISULFIDE BONDS, AND GLYCOSYLATION AT
RP ASN-36.
RX PubMed=18488039; DOI=10.1038/nsmb.1435;
RA Bowden T.A., Aricescu A.R., Gilbert R.J., Grimes J.M., Jones E.Y.,
RA Stuart D.I.;
RT "Structural basis of Nipah and Hendra virus attachment to their cell-
RT surface receptor ephrin-B2.";
RL Nat. Struct. Mol. Biol. 15:567-572(2008).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 27-167 IN COMPLEX WITH EPHA4,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-36.
RX PubMed=19836338; DOI=10.1016/j.str.2009.07.018;
RA Bowden T.A., Aricescu A.R., Nettleship J.E., Siebold C., Rahman-Huq N.,
RA Owens R.J., Stuart D.I., Jones E.Y.;
RT "Structural plasticity of EPH receptor A4 facilitates cross-class ephrin
RT signaling.";
RL Structure 17:1386-1397(2009).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-169 IN COMPLEX WITH EPHA4, AND
RP DISULFIDE BONDS.
RX PubMed=19875447; DOI=10.1074/jbc.m109.064824;
RA Qin H., Noberini R., Huan X., Shi J., Pasquale E.B., Song J.;
RT "Structural characterization of the EphA4-Ephrin-B2 complex reveals new
RT features enabling Eph-ephrin binding promiscuity.";
RL J. Biol. Chem. 285:644-654(2010).
CC -!- FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family
CC of receptor tyrosine kinases which are crucial for migration, repulsion
CC and adhesion during neuronal, vascular and epithelial development.
CC Binds promiscuously Eph receptors residing on adjacent cells, leading
CC to contact-dependent bidirectional signaling into neighboring cells.
CC The signaling pathway downstream of the receptor is referred to as
CC forward signaling while the signaling pathway downstream of the ephrin
CC ligand is referred to as reverse signaling. Binds to receptor tyrosine
CC kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a
CC central role in heart morphogenesis and angiogenesis through regulation
CC of cell adhesion and cell migration. EPHB4-mediated forward signaling
CC controls cellular repulsion and segregation from EFNB2-expressing
CC cells. May play a role in constraining the orientation of
CC longitudinally projecting axons. {ECO:0000269|PubMed:12734395}.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Hendra virus and
CC Nipah virus. {ECO:0000269|PubMed:15998730, ECO:0000269|PubMed:16007075,
CC ECO:0000269|PubMed:16477309, ECO:0000269|PubMed:17376907}.
CC -!- SUBUNIT: Interacts with PDZRN3 (By similarity). Binds to the receptor
CC tyrosine kinases EPHA4, EPHB4 and EPHA3. {ECO:0000250,
CC ECO:0000269|PubMed:16867992, ECO:0000269|PubMed:19836338,
CC ECO:0000269|PubMed:19875447}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Hendra virus and Nipah
CC virus G protein (PubMed:16007075, PubMed:16477309, PubMed:17376907,
CC PubMed:15998730). {ECO:0000269|PubMed:15998730,
CC ECO:0000269|PubMed:16007075, ECO:0000269|PubMed:16477309,
CC ECO:0000269|PubMed:17376907}.
CC -!- INTERACTION:
CC P52799; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-7532268, EBI-12109402;
CC P52799; P54764: EPHA4; NbExp=4; IntAct=EBI-7532268, EBI-5773557;
CC P52799; P54760: EPHB4; NbExp=3; IntAct=EBI-7532268, EBI-702121;
CC P52799; O43639: NCK2; NbExp=7; IntAct=EBI-7532268, EBI-713635;
CC P52799; O89343: G; Xeno; NbExp=2; IntAct=EBI-7532268, EBI-15702753;
CC P52799; Q9IH62: G; Xeno; NbExp=5; IntAct=EBI-7532268, EBI-15702710;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28931592};
CC Single-pass type I membrane protein {ECO:0000255}. Cell junction,
CC adherens junction {ECO:0000250|UniProtKB:P52800}.
CC -!- TISSUE SPECIFICITY: Lung and kidney.
CC -!- PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic
CC domain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; U16797; AAA99707.1; -; mRNA.
DR EMBL; L38734; AAC41752.1; -; mRNA.
DR EMBL; U81262; AAD03786.1; -; mRNA.
DR EMBL; AL138689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069342; AAH69342.1; -; mRNA.
DR EMBL; BC074856; AAH74856.1; -; mRNA.
DR EMBL; BC074857; AAH74857.1; -; mRNA.
DR EMBL; BC105955; AAI05956.1; -; mRNA.
DR EMBL; BC105956; AAI05957.1; -; mRNA.
DR EMBL; BC105957; AAI05958.1; -; mRNA.
DR CCDS; CCDS9507.1; -.
DR PIR; I84743; I84743.
DR RefSeq; NP_004084.1; NM_004093.3.
DR PDB; 2HLE; X-ray; 2.05 A; B=28-165.
DR PDB; 2I85; NMR; -; A=25-166.
DR PDB; 2VSK; X-ray; 3.30 A; B/D=28-165.
DR PDB; 2VSM; X-ray; 1.80 A; B=28-165.
DR PDB; 2WO2; X-ray; 2.45 A; B=27-167.
DR PDB; 3GXU; X-ray; 2.50 A; B=27-169.
DR PDB; 4UF7; X-ray; 1.70 A; C/E=27-167.
DR PDB; 6P7Y; X-ray; 2.84 A; B/D=27-170.
DR PDB; 6PDL; X-ray; 2.70 A; B/D/F/H=27-167.
DR PDBsum; 2HLE; -.
DR PDBsum; 2I85; -.
DR PDBsum; 2VSK; -.
DR PDBsum; 2VSM; -.
DR PDBsum; 2WO2; -.
DR PDBsum; 3GXU; -.
DR PDBsum; 4UF7; -.
DR PDBsum; 6P7Y; -.
DR PDBsum; 6PDL; -.
DR AlphaFoldDB; P52799; -.
DR BMRB; P52799; -.
DR SMR; P52799; -.
DR BioGRID; 108268; 127.
DR DIP; DIP-46378N; -.
DR IntAct; P52799; 54.
DR MINT; P52799; -.
DR STRING; 9606.ENSP00000245323; -.
DR GlyConnect; 1937; 8 N-Linked glycans (2 sites).
DR GlyGen; P52799; 3 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; P52799; -.
DR PhosphoSitePlus; P52799; -.
DR BioMuta; EFNB2; -.
DR DMDM; 1706673; -.
DR EPD; P52799; -.
DR jPOST; P52799; -.
DR MassIVE; P52799; -.
DR MaxQB; P52799; -.
DR PaxDb; P52799; -.
DR PeptideAtlas; P52799; -.
DR PRIDE; P52799; -.
DR ProteomicsDB; 56538; -.
DR Antibodypedia; 2406; 525 antibodies from 45 providers.
DR DNASU; 1948; -.
DR Ensembl; ENST00000646441.1; ENSP00000493716.1; ENSG00000125266.8.
DR GeneID; 1948; -.
DR KEGG; hsa:1948; -.
DR MANE-Select; ENST00000646441.1; ENSP00000493716.1; NM_004093.4; NP_004084.1.
DR UCSC; uc001vqi.4; human.
DR CTD; 1948; -.
DR DisGeNET; 1948; -.
DR GeneCards; EFNB2; -.
DR HGNC; HGNC:3227; EFNB2.
DR HPA; ENSG00000125266; Low tissue specificity.
DR MIM; 600527; gene.
DR neXtProt; NX_P52799; -.
DR OpenTargets; ENSG00000125266; -.
DR PharmGKB; PA27662; -.
DR VEuPathDB; HostDB:ENSG00000125266; -.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000155868; -.
DR HOGENOM; CLU_072080_0_0_1; -.
DR InParanoid; P52799; -.
DR OMA; GSTRHND; -.
DR OrthoDB; 903831at2759; -.
DR PhylomeDB; P52799; -.
DR PathwayCommons; P52799; -.
DR Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-3928664; Ephrin signaling.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR SignaLink; P52799; -.
DR SIGNOR; P52799; -.
DR BioGRID-ORCS; 1948; 16 hits in 1076 CRISPR screens.
DR ChiTaRS; EFNB2; human.
DR EvolutionaryTrace; P52799; -.
DR GeneWiki; EFNB2; -.
DR GenomeRNAi; 1948; -.
DR Pharos; P52799; Tbio.
DR PRO; PR:P52799; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; P52799; protein.
DR Bgee; ENSG00000125266; Expressed in ventricular zone and 205 other tissues.
DR Genevisible; P52799; HS.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0034332; P:adherens junction organization; IEA:Ensembl.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0048514; P:blood vessel morphogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0001945; P:lymph vessel development; IEA:Ensembl.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ARUK-UCL.
DR GO; GO:0072178; P:nephric duct morphogenesis; IEA:Ensembl.
DR GO; GO:1903849; P:positive regulation of aorta morphogenesis; IEA:Ensembl.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISS:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:1901216; P:positive regulation of neuron death; IDA:ARUK-UCL.
DR GO; GO:0099054; P:presynapse assembly; IEA:Ensembl.
DR GO; GO:0050920; P:regulation of chemotaxis; IDA:UniProtKB.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
DR GO; GO:0048845; P:venous blood vessel morphogenesis; IEA:Ensembl.
DR CDD; cd10426; Ephrin-B_Ectodomain; 1.
DR DisProt; DP01588; -.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR034255; Ephrin-B_Ecto.
DR InterPro; IPR019765; Ephrin_CS.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; PTHR11304; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01347; EPHRIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; Cell junction; Cell membrane;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Host cell receptor for virus entry; Host-virus interaction; Membrane;
KW Methylation; Neurogenesis; Phosphoprotein; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..333
FT /note="Ephrin-B2"
FT /id="PRO_0000008392"
FT TOPO_DOM 28..229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..333
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..164
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 165..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 331..333
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 187..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52800"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52800"
FT MOD_RES 277
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P52800"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:18488039,
FT ECO:0000269|PubMed:19836338"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..101
FT /evidence="ECO:0000269|PubMed:16867992,
FT ECO:0000269|PubMed:18488039, ECO:0000269|PubMed:19836338,
FT ECO:0000269|PubMed:19875447, ECO:0000269|Ref.14,
FT ECO:0007744|PDB:2VSK, ECO:0007744|PDB:2VSM"
FT DISULFID 89..153
FT /evidence="ECO:0000269|PubMed:16867992,
FT ECO:0000269|PubMed:18488039, ECO:0000269|PubMed:19836338,
FT ECO:0000269|PubMed:19875447, ECO:0000269|Ref.14,
FT ECO:0007744|PDB:2VSK, ECO:0007744|PDB:2VSM"
FT MUTAGEN 121..122
FT /note="LW->YM: Complete loss of Nipah protein G binding."
FT /evidence="ECO:0000269|PubMed:16477309"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:4UF7"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:4UF7"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:4UF7"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:4UF7"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2I85"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:4UF7"
FT HELIX 83..87
FT /evidence="ECO:0007829|PDB:4UF7"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:4UF7"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2I85"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:4UF7"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:4UF7"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:4UF7"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:4UF7"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:2I85"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:4UF7"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4UF7"
SQ SEQUENCE 333 AA; 36923 MW; 6D9932A632626AEA CRC64;
MAVRRDSVWK YCWGVLMVLC RTAISKSIVL EPIYWNSSNS KFLPGQGLVL YPQIGDKLDI
ICPKVDSKTV GQYEYYKVYM VDKDQADRCT IKKENTPLLN CAKPDQDIKF TIKFQEFSPN
LWGLEFQKNK DYYIISTSNG SLEGLDNQEG GVCQTRAMKI LMKVGQDASS AGSTRNKDPT
RRPELEAGTN GRSSTTSPFV KPNPGSSTDG NSAGHSGNNI LGSEVALFAG IASGCIIFIV
IIITLVVLLL KYRRRHRKHS PQHTTTLSLS TLATPKRSGN NNGSEPSDII IPLRTADSVF
CPHYEKVSGD YGHPVYIVQE MPPQSPANIY YKV
