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   24-JAN-2024, entry version 184.
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   GlyCosmos; P52795; 1 site, No reported glycans.
DR   GlyGen; P52795; 1 site.
DR   iPTMnet; P52795; -.
DR   PhosphoSitePlus; P52795; -.
DR   SwissPalm; P52795; -.
DR   PaxDb; 10090-ENSMUSP00000050716; -.
DR   PeptideAtlas; P52795; -.
DR   ProteomicsDB; 277769; -.
DR   Pumba; P52795; -.
DR   Antibodypedia; 43761; 648 antibodies from 36 providers.
DR   DNASU; 13641; -.
DR   Ensembl; ENSMUST00000052839.7; ENSMUSP00000050716.7; ENSMUSG00000031217.9.
DR   GeneID; 13641; -.
DR   KEGG; mmu:13641; -.
DR   UCSC; uc009tvi.1; mouse.
DR   AGR; MGI:102708; -.
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; YLWMFIL; -.
DR   OrthoDB; 5402021at2759; -.
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 80 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 321 other cell types or tissues.
DR   ExpressionAtlas; P52795; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; 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:0042734; C:presynaptic 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:2000785; P:regulation of autophagosome 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; Cupredoxins - blue copper proteins; 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; EPHRIN; 1.
DR   PANTHER; PTHR11304:SF17; EPHRIN-B1; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR   PROSITE; PS51551; EPHRIN_RBD_2; 1.
DR   Genevisible; P52795; MM.
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
//