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Ephrin-B2 (ELF-2) (EPH-related receptor tyrosine kinase ligand 5) (LERK-5) (HTK ligand) (HTK-L)

 EFNB2_MOUSE             Reviewed;         336 AA.
P52800;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 158.
RecName: Full=Ephrin-B2;
AltName: Full=ELF-2;
AltName: Full=EPH-related receptor tyrosine kinase ligand 5;
Short=LERK-5;
AltName: Full=HTK ligand;
Short=HTK-L;
Flags: Precursor;
Name=Efnb2; Synonyms=Elf2, Epl5, Eplg5, Htkl, Lerk5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8559144; DOI=10.1016/0161-5890(95)00108-5;
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; DOI=10.1073/pnas.92.6.1866;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=ICR; TISSUE=Brain;
PubMed=7651410; DOI=10.1128/MCB.15.9.4921;
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/6J; 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).
[5]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10704386;
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 SER-263 AND THR-277, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-280, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[8]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=27446912; DOI=10.3389/fcell.2016.00058;
Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J.,
de Reynies A., Aurade F., Chang T.H., Zammit P.S., Relaix F.;
"Gene expression profiling of muscle stem cells identifies novel
regulators of postnatal myogenesis.";
Front. Cell Dev. Biol. 4:58-58(2016).
[9]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 30-207, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-39.
PubMed=11703926; DOI=10.1016/S1534-5807(01)00002-8;
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).
[10]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-168 IN COMPLEX WITH EPHB2,
AND DISULFIDE BOND.
PubMed=11780069; DOI=10.1038/414933a;
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).
-!- 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 receptor tyrosine kinase including
EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role
in heart morphogenesis and angiogenesis through regulation of cell
adhesion and cell migration. EPHB4-mediated forward signaling
controls cellular repulsion and segregation from EFNB2-expressing
cells. May play a role in constraining the orientation of
longitudinally projecting axons. {ECO:0000269|PubMed:10704386}.
-!- SUBUNIT: Interacts with PDZRN3. Binds to the ephrin receptor
EPHA3, EPHA4 and EPHB4 (By similarity). {ECO:0000250}.
-!- INTERACTION:
O88797:Dab2 (xeno); NbExp=2; IntAct=EBI-1032676, EBI-6109302;
Q03137:Epha4; NbExp=2; IntAct=EBI-1032676, EBI-1539152;
P12931:SRC (xeno); NbExp=2; IntAct=EBI-1032676, EBI-621482;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P52799}; Single-pass type I membrane
protein {ECO:0000255}.
-!- 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
(PubMed:7651410, PubMed:10704386). Expressed in myogenic
progenitor cells (PubMed:27446912). {ECO:0000269|PubMed:10704386,
ECO:0000269|PubMed:27446912, ECO:0000269|PubMed:7651410}.
-!- DEVELOPMENTAL STAGE: Expressed in the floor plate throughout the
period of commissural axon pathfinding (PubMed:7651410,
PubMed:10704386). In myogenic progenitor cells, highly expressed
during early development (E11.5) and progressively repressed as
developments proceeds (PubMed:27446912).
{ECO:0000269|PubMed:10704386, ECO:0000269|PubMed:27446912,
ECO:0000269|PubMed:7651410}.
-!- PTM: Inducible phosphorylation of tyrosine residues in the
cytoplasmic domain. {ECO:0000250}.
-!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
-!- SEQUENCE CAUTION:
Sequence=AAC42052.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U16819; AAA99708.1; -; mRNA.
EMBL; L38847; AAC42052.1; ALT_INIT; mRNA.
EMBL; U30244; AAA82934.1; -; mRNA.
EMBL; BC057009; AAH57009.1; -; mRNA.
CCDS; CCDS22090.1; -.
PIR; I49766; I49766.
RefSeq; NP_034241.2; NM_010111.5.
UniGene; Mm.209813; -.
PDB; 1IKO; X-ray; 1.92 A; P=30-207.
PDB; 1KGY; X-ray; 2.70 A; E/F/G/H=31-168.
PDBsum; 1IKO; -.
PDBsum; 1KGY; -.
ProteinModelPortal; P52800; -.
SMR; P52800; -.
BioGrid; 199395; 1.
DIP; DIP-29208N; -.
IntAct; P52800; 17.
MINT; P52800; -.
STRING; 10090.ENSMUSP00000001319; -.
iPTMnet; P52800; -.
PhosphoSitePlus; P52800; -.
PaxDb; P52800; -.
PeptideAtlas; P52800; -.
PRIDE; P52800; -.
Ensembl; ENSMUST00000001319; ENSMUSP00000001319; ENSMUSG00000001300.
GeneID; 13642; -.
KEGG; mmu:13642; -.
UCSC; uc009kue.1; mouse.
CTD; 1948; -.
MGI; MGI:105097; Efnb2.
eggNOG; KOG3858; Eukaryota.
eggNOG; ENOG4111FMJ; LUCA.
GeneTree; ENSGT00940000155868; -.
HOGENOM; HOG000220931; -.
HOVERGEN; HBG051448; -.
InParanoid; P52800; -.
KO; K05463; -.
OMA; NRDYYII; -.
OrthoDB; EOG091G0BPC; -.
Reactome; R-MMU-2682334; EPH-Ephrin signaling.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-3928664; Ephrin signaling.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
EvolutionaryTrace; P52800; -.
PRO; PR:P52800; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000001300; Expressed in 322 organ(s), highest expression level in olfactory bulb.
CleanEx; MM_EFNB2; -.
CleanEx; MM_ELF2; -.
ExpressionAtlas; P52800; baseline and differential.
Genevisible; P52800; MM.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:SynGO.
GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; IPI:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0007411; P:axon guidance; IBA:GO_Central.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0001945; P:lymph vessel development; IMP:MGI.
GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IMP:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:0072178; P:nephric duct morphogenesis; IMP:MGI.
GO; GO:1903849; P:positive regulation of aorta morphogenesis; IMP:MGI.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
GO; GO:0099054; P:presynapse assembly; ISO:MGI.
GO; GO:0050920; P:regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IDA:SynGO.
GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
GO; GO:0031295; P:T cell costimulation; IDA:MGI.
GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:MGI.
CDD; cd10426; Ephrin-B_Ectodomain; 1.
Gene3D; 2.60.40.420; -; 1.
InterPro; IPR008972; Cupredoxin.
InterPro; IPR031328; Ephrin.
InterPro; IPR034255; Ephrin-B_Ecto.
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; Angiogenesis; Cell membrane; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
Membrane; Methylation; Neurogenesis; Phosphoprotein;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 336 Ephrin-B2.
/FTId=PRO_0000008393.
TOPO_DOM 29 232 Extracellular. {ECO:0000255}.
TRANSMEM 233 253 Helical. {ECO:0000255}.
TOPO_DOM 254 336 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 167 Ephrin RBD. {ECO:0000255|PROSITE-
ProRule:PRU00884}.
MOTIF 334 336 PDZ-binding. {ECO:0000255}.
MOD_RES 263 263 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 277 277 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 280 280 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:11703926}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 65 104 {ECO:0000244|PDB:1IKO,
ECO:0000269|PubMed:11703926,
ECO:0000269|PubMed:11780069}.
DISULFID 92 156 {ECO:0000244|PDB:1IKO,
ECO:0000269|PubMed:11703926,
ECO:0000269|PubMed:11780069}.
CONFLICT 177 177 A -> T (in Ref. 1; AAA99708).
{ECO:0000305}.
TURN 47 49 {ECO:0000244|PDB:1IKO}.
STRAND 50 53 {ECO:0000244|PDB:1IKO}.
STRAND 60 64 {ECO:0000244|PDB:1IKO}.
STRAND 70 72 {ECO:0000244|PDB:1IKO}.
STRAND 78 84 {ECO:0000244|PDB:1IKO}.
HELIX 86 91 {ECO:0000244|PDB:1IKO}.
STRAND 101 104 {ECO:0000244|PDB:1IKO}.
STRAND 112 116 {ECO:0000244|PDB:1IKO}.
STRAND 133 138 {ECO:0000244|PDB:1IKO}.
HELIX 145 147 {ECO:0000244|PDB:1IKO}.
HELIX 154 158 {ECO:0000244|PDB:1IKO}.
STRAND 162 167 {ECO:0000244|PDB:1IKO}.
SEQUENCE 336 AA; 37202 MW; D08894996E399554 CRC64;
MAMARSRRDS VWKYCWGLLM VLCRTAISRS IVLEPIYWNS SNSKFLPGQG LVLYPQIGDK
LDIICPKVDS KTVGQYEYYK VYMVDKDQAD RCTIKKENTP LLNCARPDQD VKFTIKFQEF
SPNLWGLEFQ KNKDYYIIST SNGSLEGLDN QEGGVCQTRA MKILMKVGQD ASSAGSARNH
GPTRRPELEA GTNGRSSTTS PFVKPNPGSS TDGNSAGHSG NNLLGSEVAL FAGIASGCII
FIVIIITLVV LLLKYRRRHR KHSPQHTTTL SLSTLATPKR GGNNNGSEPS DVIIPLRTAD
SVFCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV


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