EFNB1_XENLA
ID EFNB1_XENLA Reviewed; 329 AA.
AC O13097;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ephrin-B1;
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=XlERK;
DE Flags: Precursor;
GN Name=efnb1; Synonyms=eplg2, lerk2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9174051; DOI=10.1038/sj.onc.1201082;
RA Jones T.L., Karavanova I., Chong L., Zhou R.P., Daar I.O.;
RT "Identification of XLerk, an Eph family ligand regulated during mesoderm
RT induction and neurogenesis in Xenopus laevis.";
RL Oncogene 14:2159-2166(1997).
RN [2]
RP SEQUENCE REVISION TO 61-63; 195; 210-212 AND 260.
RA Daar I.O.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH TLE4, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
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).
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 (By similarity). May have a
CC role in the developing mesenchymal and nervous tissue. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TLE4 through the PDZ-binding motif.
CC {ECO:0000269|PubMed:21429299}.
CC -!- INTERACTION:
CC O13097; Q8AW92: lmo4-a; NbExp=2; IntAct=EBI-15667006, EBI-15667028;
CC O13097; P52631: Stat3; Xeno; NbExp=4; IntAct=EBI-15667006, EBI-10764775;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in most tissues with
CC highest levels in the kidney, oocytes, ovary and testis.
CC -!- DEVELOPMENTAL STAGE: At stages 16 and 32, expressed in the neural
CC groove, rhombomeres, forebrain and branchial arches.
CC {ECO:0000269|PubMed:21429299}.
CC -!- DOMAIN: The PDZ-binding motif is required for TLE4-binding.
CC {ECO:0000269|PubMed:21429299}.
CC -!- PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic
CC domain. Tyrosine phosphorylation inhibits TLE4-binding.
CC {ECO:0000269|PubMed:21429299}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
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DR EMBL; U31427; AAC35995.2; -; mRNA.
DR RefSeq; NP_001080948.2; NM_001087479.2.
DR AlphaFoldDB; O13097; -.
DR SMR; O13097; -.
DR BioGRID; 98894; 1.
DR DIP; DIP-60983N; -.
DR IntAct; O13097; 5.
DR GeneID; 394292; -.
DR KEGG; xla:394292; -.
DR CTD; 394292; -.
DR Xenbase; XB-GENE-1011784; efnb1.L.
DR OMA; CNKPQQE; -.
DR OrthoDB; 903831at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 394292; Expressed in internal ear and 19 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046875; F:ephrin receptor binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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 Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Membrane; Neurogenesis; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..329
FT /note="Ephrin-B1"
FT /id="PRO_0000008391"
FT TOPO_DOM 21..226
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..157
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT REGION 163..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 327..329
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 164..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT DISULFID 82..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
SQ SEQUENCE 329 AA; 36593 MW; D1D6721FF0A2AF1E CRC64;
MEGLRRLLGL LLVLYRLCSA LGKNLEPVTW NSQNPRFISG KGLVLYPEIG DRLDIICPKG
DSSQPYEYYK LYMVRRDQLE ACSTVIDPNV LVTCNQPGKE YRFTIKFQEF SPNYMGLEFR
RNQDYYITST SNSTLQGLEN REGGVCQTRS MKIIMKVGQD PNAVPPEQLT TTRPSKEADN
TGKIATFGPW NGPVENPGKS DTNLSDKPTA GGGVDGFFNS KIAVFAAIGA GCVIFILIII
FLVVLLIKIR KRHRKHTQQR AAALSLSTLA SPKCSGNAGS EPSDIIIPLR TTENNYCPHY
EKVSGDYGHP VYIVQEMPPQ SPANIYYKV
