EFNB1_MOUSE
ID EFNB1_MOUSE Reviewed; 345 AA.
AC P52795;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Ephrin-B1;
DE AltName: Full=CEK5 receptor ligand;
DE Short=CEK5-L;
DE AltName: Full=EFL-3;
DE AltName: Full=ELK ligand;
DE Short=ELK-L;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 2;
DE Short=LERK-2;
DE AltName: Full=Stimulated by retinoic acid gene 1 protein;
DE Contains:
DE RecName: Full=Ephrin-B1 C-terminal fragment {ECO:0000250|UniProtKB:P98172};
DE Short=Ephrin-B1 CTF {ECO:0000250|UniProtKB:P98172};
DE Contains:
DE RecName: Full=Ephrin-B1 intracellular domain {ECO:0000250|UniProtKB:P98172};
DE Short=Ephrin-B1 ICD {ECO:0000250|UniProtKB:P98172};
DE Flags: Precursor;
GN Name=Efnb1; Synonyms=Epl2, Eplg2, Lerk2, Stra1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=7896266; DOI=10.1006/geno.1994.1589;
RA Fletcher F.A., Renshaw B., Hollingsworth T., Baum P., Lyman S.D.,
RA Jenkins N.A., Gilbert D.J., Copeland N.G., Davison B.L.;
RT "Genomic organization and chromosomal localization of mouse Eplg2, a gene
RT encoding a binding protein for the receptor tyrosine kinase elk.";
RL Genomics 24:127-132(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7649373; DOI=10.1006/dbio.1995.1226;
RA Bouillet P., Oulad-Abdelghani M., Vicaire S., Garnier J.-M., Schuhbaur B.,
RA Dolle P., Chambon P.;
RT "Efficient cloning of cDNAs of retinoic acid-responsive genes in P19
RT embryonal carcinoma cells and characterization of a novel mouse gene, Stra1
RT (mouse LERK-2/Eplg2).";
RL Dev. Biol. 170:420-433(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=7929389; DOI=10.1016/s0021-9258(18)47059-7;
RA Shao H., Lou L., Pandey A., Pasquale E.B., Dixit V.M.;
RT "cDNA cloning and characterization of a ligand for the Cek5 receptor
RT protein-tyrosine kinase.";
RL J. Biol. Chem. 269:26606-26609(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=10197531; DOI=10.1016/s0896-6273(00)80706-0;
RA Brueckner K., Pablo Labrador J., Scheiffele P., Herb A., Seeburg P.H.,
RA Klein R.;
RT "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft
RT membrane microdomains.";
RL Neuron 22:511-524(1999).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10704386; DOI=10.1242/dev.127.7.1397;
RA Imondi R., Wideman C., Kaprielian Z.;
RT "Complementary expression of transmembrane ephrins and their receptors in
RT the mouse spinal cord: a possible role in constraining the orientation of
RT longitudinally projecting axons.";
RL Development 127:1397-1410(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [8]
RP INTERACTION WITH ZHX2, AND SUBCELLULAR LOCATION.
RX PubMed=19515908; DOI=10.1523/jneurosci.5841-08.2009;
RA Wu C., Qiu R., Wang J., Zhang H., Murai K., Lu Q.;
RT "ZHX2 Interacts with Ephrin-B and regulates neural progenitor maintenance
RT in the developing cerebral cortex.";
RL J. Neurosci. 29:7404-7412(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH TLE1.
RX PubMed=21429299; DOI=10.5483/bmbrep.2011.44.3.199;
RA Kamata T., Bong Y.S., Mood K., Park M.J., Nishanian T.G., Lee H.S.;
RT "EphrinB1 interacts with the transcriptional co-repressor Groucho/xTLE4.";
RL BMB Rep. 44:199-204(2011).
RN [11]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
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 (PubMed:7929389, PubMed:10704386). Binding to Eph receptors residing on
CC adjacent cells leads to contact-dependent bidirectional signaling into
CC neighboring cells (PubMed:7929389, PubMed:10704386). Shows high
CC affinity for the receptor tyrosine kinase EPHB1/ELK (By similarity).
CC Can also bind EPHB2 and EPHB3 (PubMed:7929389). Binds to, and induces
CC the collapse of, commissural axons/growth cones in vitro
CC (PubMed:10704386). May play a role in constraining the orientation of
CC longitudinally projecting axons (PubMed:10704386).
CC {ECO:0000250|UniProtKB:P98172, ECO:0000269|PubMed:10704386,
CC ECO:0000269|PubMed:7929389}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with GRIP1 and GRIP2 (via
CC PDZ domain 6) (By similarity). Interacts with TLE1 (PubMed:21429299).
CC The intracellular domain peptide interacts with ZHX2; the interaction
CC enhances ZHX2 transcriptional repression activity (PubMed:19515908).
CC {ECO:0000250|UniProtKB:P98172, ECO:0000269|PubMed:19515908,
CC ECO:0000269|PubMed:21429299}.
CC -!- INTERACTION:
CC P52795; P49769: Psen1; NbExp=2; IntAct=EBI-8107507, EBI-990067;
CC P52795; O08992: Sdcbp; NbExp=3; IntAct=EBI-8107507, EBI-538265;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7929389,
CC ECO:0000305|PubMed:10704386}; Single-pass type I membrane protein
CC {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:10197531}. Note=May
CC recruit GRIP1 and GRIP2 to membrane raft domains.
CC {ECO:0000269|PubMed:10197531}.
CC -!- SUBCELLULAR LOCATION: [Ephrin-B1 C-terminal fragment]: Cell membrane
CC {ECO:0000250|UniProtKB:P98172}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- SUBCELLULAR LOCATION: [Ephrin-B1 intracellular domain]: Nucleus
CC {ECO:0000269|PubMed:19515908}. Note=Colocalizes with ZHX2 in the
CC nucleus. {ECO:0000269|PubMed:19515908}.
CC -!- TISSUE SPECIFICITY: Expressed on lateral floor plate cells,
CC specifically on commissural axon segments that have passed through the
CC floor plate. Expressed in cells of the retinal ganglion cell layer
CC during retinal axon guidance to the optic disk (PubMed:10704386).
CC Expressed in myogenic progenitor cells (PubMed:27446912).
CC {ECO:0000269|PubMed:10704386, ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the floor plate throughout the period
CC of commissural axon pathfinding (PubMed:10704386). In myogenic
CC progenitor cells, highly expressed during early development (11.5 dpc)
CC and progressively repressed as developments proceeds (PubMed:27446912).
CC {ECO:0000269|PubMed:10704386, ECO:0000269|PubMed:27446912}.
CC -!- PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic
CC domain. {ECO:0000250|UniProtKB:P98172}.
CC -!- PTM: Proteolytically processed. The ectodomain is cleaved, probably by
CC a metalloprotease, to produce a membrane-tethered C-terminal fragment.
CC This fragment is then further processed by the gamma-secretase complex
CC to yield a soluble intracellular domain peptide which can translocate
CC to the nucleus. The intracellular domain peptide is highly labile
CC suggesting that it is targeted for degradation by the proteasome.
CC {ECO:0000250|UniProtKB:P98172}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; U07602; AAC53247.1; -; Genomic_DNA.
DR EMBL; U07598; AAC53247.1; JOINED; Genomic_DNA.
DR EMBL; U07599; AAC53247.1; JOINED; Genomic_DNA.
DR EMBL; U07600; AAC53247.1; JOINED; Genomic_DNA.
DR EMBL; Z48781; CAA88695.1; -; mRNA.
DR EMBL; U12983; AAA53231.1; -; mRNA.
DR EMBL; BC006797; AAH06797.1; -; mRNA.
DR EMBL; BC021656; AAH21656.1; -; mRNA.
DR CCDS; CCDS30298.1; -.
DR PIR; I48780; I48780.
DR RefSeq; NP_034240.1; NM_010110.5.
DR PDB; 6P7S; X-ray; 3.49 A; B/D=29-170.
DR PDBsum; 6P7S; -.
DR AlphaFoldDB; P52795; -.
DR SMR; P52795; -.
DR BioGRID; 199394; 8.
DR CORUM; P52795; -.
DR DIP; DIP-29206N; -.
DR IntAct; P52795; 8.
DR MINT; P52795; -.
DR STRING; 10090.ENSMUSP00000050716; -.
DR GlyGen; P52795; 1 site.
DR iPTMnet; P52795; -.
DR PhosphoSitePlus; P52795; -.
DR PaxDb; P52795; -.
DR PeptideAtlas; P52795; -.
DR PRIDE; P52795; -.
DR ProteomicsDB; 277769; -.
DR Antibodypedia; 43761; 589 antibodies from 36 providers.
DR DNASU; 13641; -.
DR Ensembl; ENSMUST00000052839; ENSMUSP00000050716; ENSMUSG00000031217.
DR GeneID; 13641; -.
DR KEGG; mmu:13641; -.
DR UCSC; uc009tvi.1; mouse.
DR CTD; 1947; -.
DR MGI; MGI:102708; Efnb1.
DR VEuPathDB; HostDB:ENSMUSG00000031217; -.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000160128; -.
DR HOGENOM; CLU_072080_0_0_1; -.
DR InParanoid; P52795; -.
DR OMA; CNKPQQE; -.
DR OrthoDB; 903831at2759; -.
DR PhylomeDB; P52795; -.
DR Reactome; R-MMU-2682334; EPH-Ephrin signaling.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-3928664; Ephrin signaling.
DR Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
DR BioGRID-ORCS; 13641; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Efnb1; mouse.
DR PRO; PR:P52795; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P52795; protein.
DR Bgee; ENSMUSG00000031217; Expressed in ventricular zone and 318 other tissues.
DR ExpressionAtlas; P52795; baseline and differential.
DR Genevisible; P52795; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI.
DR GO; GO:0099054; P:presynapse assembly; ISO:MGI.
DR GO; GO:0031295; P:T cell costimulation; IDA:MGI.
DR GO; GO:0042098; P:T cell proliferation; IDA:MGI.
DR CDD; cd10426; Ephrin-B_Ectodomain; 1.
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; Cell membrane; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..345
FT /note="Ephrin-B1"
FT /id="PRO_0000008388"
FT CHAIN 217..345
FT /note="Ephrin-B1 C-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:P98172"
FT /id="PRO_0000445793"
FT CHAIN 259..345
FT /note="Ephrin-B1 intracellular domain"
FT /evidence="ECO:0000250|UniProtKB:P98172"
FT /id="PRO_0000445794"
FT TOPO_DOM 25..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..164
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 169..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..293
FT /note="Interaction with ZHX2"
FT /evidence="ECO:0000269|PubMed:19515908"
FT MOTIF 259..272
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P98172"
FT MOTIF 343..345
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 170..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98172"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98172"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 89..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT CONFLICT 90
FT /note="S -> T (in Ref. 2; AAA53231)"
FT /evidence="ECO:0000305"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:6P7S"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:6P7S"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:6P7S"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:6P7S"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:6P7S"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6P7S"
SQ SEQUENCE 345 AA; 37859 MW; 8C96FD3DC5CBC405 CRC64;
MARPGQRWLS KWLVAMVVLT LCRLATPLAK NLEPVSWSSL NPKFLSGKGL VIYPKIGDKL
DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT CNKPHQEIRF TIKFQEFSPN
YMGLEFKKYH DYYITSTSNG SLEGLENREG GVCRTRTMKI VMKVGQDPNA VTPEQLTTSR
PSKESDNTVK TATQAPGRGS QGDSDGKHET VNQEEKSGPG AGGGGSGDSD SFFNSKVALF
AAVGAGCVIF LLIIIFLTVL LLKLRKRHRK HTQQRAAALS LSTLASPKGG SGTAGTEPSD
IIIPLRTTEN NYCPHYEKVS GDYGHPVYIV QEMPPQSPAN IYYKV
