EFNB1_RAT
ID EFNB1_RAT Reviewed; 345 AA.
AC P52796;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Ephrin-B1;
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 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=Eplg2, Lerk2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=7936648;
RA Fletcher F.A., Carpenter M., Shilling H., Baum P., Ziegler S., Gimpel S.,
RA Hollingsworth T., Vanden Bos T., Davison B.L., Lyman S.D., Beckmann M.P.;
RT "LERK-2, a binding protein for the receptor-tyrosine kinase ELK, is
RT evolutionarily conserved and expressed in a developmentally regulated
RT pattern.";
RL Oncogene 9:3241-3248(1994).
RN [2]
RP INTERACTION WITH GRIP1 AND GRIP2.
RC TISSUE=Fetal brain;
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).
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:7936648). Binding to Eph receptors residing on adjacent cells
CC leads to contact-dependent bidirectional signaling into neighboring
CC cells (By similarity). Shows high affinity for the receptor tyrosine
CC kinase EPHB1/ELK (PubMed:7936648). Can also bind EPHB2 and EPHB3 (By
CC similarity). Binds to, and induces the collapse of, commissural
CC axons/growth cones in vitro. May play a role in constraining the
CC orientation of longitudinally projecting axons (By similarity).
CC {ECO:0000250|UniProtKB:P52795, ECO:0000269|PubMed:7936648}.
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with GRIP1 and GRIP2 (via
CC PDZ domain 6) (PubMed:10197531). Interacts with TLE1 (By similarity).
CC The intracellular domain peptide interacts with ZHX2; the interaction
CC enhances ZHX2 transcriptional repression activity (By similarity).
CC {ECO:0000250|UniProtKB:P52795, ECO:0000269|PubMed:10197531}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:7936648};
CC Single-pass type I membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000250|UniProtKB:P98172}. Note=May recruit GRIP1 and GRIP2 to
CC membrane raft domains. {ECO:0000250|UniProtKB:P98172}.
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:0000250|UniProtKB:P98172}. Note=Colocalizes with ZHX2 in the
CC nucleus. {ECO:0000250|UniProtKB:P98172}.
CC -!- TISSUE SPECIFICITY: Detected in lung, kidney, heart and testis.
CC {ECO:0000269|PubMed:7936648}.
CC -!- DEVELOPMENTAL STAGE: Detected at embryonic stage E18 in kidney, heart,
CC brain, lung, skeletal muscle and thymus. Expression is particularly
CC strong in kidney. {ECO:0000269|PubMed:7936648}.
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; U07560; AAA53092.1; -; mRNA.
DR PIR; I58406; I58406.
DR AlphaFoldDB; P52796; -.
DR SMR; P52796; -.
DR STRING; 10116.ENSRNOP00000009635; -.
DR GlyGen; P52796; 1 site.
DR PhosphoSitePlus; P52796; -.
DR PaxDb; P52796; -.
DR RGD; 2540; Efnb1.
DR eggNOG; KOG3858; Eukaryota.
DR InParanoid; P52796; -.
DR PhylomeDB; P52796; -.
DR Reactome; R-RNO-2682334; EPH-Ephrin signaling.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-3928664; Ephrin signaling.
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR PRO; PR:P52796; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0009880; P:embryonic pattern specification; ISO:RGD.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IMP:RGD.
DR GO; GO:0001755; P:neural crest cell migration; ISO:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:0031295; P:T cell costimulation; ISO:RGD.
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 Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Membrane; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..345
FT /note="Ephrin-B1"
FT /id="PRO_0000008389"
FT CHAIN 217..345
FT /note="Ephrin-B1 C-terminal fragment"
FT /evidence="ECO:0000250|UniProtKB:P98172"
FT /id="PRO_0000445795"
FT CHAIN 259..345
FT /note="Ephrin-B1 intracellular domain"
FT /evidence="ECO:0000250|UniProtKB:P98172"
FT /id="PRO_0000445796"
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:0000250|UniProtKB:P98172"
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"
SQ SEQUENCE 345 AA; 37951 MW; 1B3045C5C7358F7E CRC64;
MARPGQRWLS KWLVAMVVLT LCRLATPLAK NLEPVSWSSL NPKFLSGKGL VIYPKIGDKL
DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT CNKPQQEIRF TIKFQEFSPN
YMGLEFKKYH DYYITSTSNG SLEGLENREG GVCRTRTMKI VMKVGQDPNA VTPEQLTTSR
PSKESDNTVK TATQAPGRGS QGDSDGKHET VNQQEKSGPG AGGSGSGDTD SFFNSKVALF
AAVGAGCVIF LLIIIFLTVL LLKLRKRHRK HTQQRAAALS LSTLASPKGD SGTAGTEPSD
IIIPLRTTEN NYCPHYEKVS GDYGHPVYIV QEMPPQSPAN IYYKV
