ID   EPB1A_XENLA             Reviewed;         985 AA.
AC   Q91571;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Ephrin type-B receptor 1-A;
DE            EC=2.7.10.1;
DE   AltName: Full=Tyrosine-protein kinase receptor XEK;
DE   Flags: Precursor;
GN   Name=ephb1-a; Synonyms=xek;
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=7700636;
RA   Jones T.L., Karavanova I., Maeno M., Ong R.C., Kung H.-F., Daar I.O.;
RT   "Expression of an amphibian homolog of the Eph family of receptor tyrosine
RT   kinases is developmentally regulated.";
RL   Oncogene 10:1111-1117(1995).
RN   [2]
RP   FUNCTION IN TARGETED CELL MIGRATION.
RX   PubMed=9259557; DOI=10.1016/s0960-9822(06)00255-7;
RA   Smith A., Robinson V., Patel K., Wilkinson D.G.;
RT   "The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand
RT   regulate targeted migration of branchial neural crest cells.";
RL   Curr. Biol. 7:561-570(1997).
CC   -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
CC       transmembrane ephrin-B family ligands residing on adjacent cells,
CC       leading to contact-dependent bidirectional signaling into neighboring
CC       cells. The signaling pathway downstream of the receptor is referred to
CC       as forward signaling while the signaling pathway downstream of the
CC       ephrin ligand is referred to as reverse signaling. May play a role in
CC       axon guidance during nervous system development. May also play an
CC       important redundant role with other ephrin-B receptors in development
CC       and maturation of dendritic spines and synapse formation. More
CC       generally, may play a role in targeted cell migration and adhesion.
CC       Upon activation by ephrin-B ligands activates the MAPK/ERK and the JNK
CC       signaling cascades to regulate cell migration and adhesion
CC       respectively. {ECO:0000269|PubMed:9259557}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC       is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC       probably required to induce biological responses (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein. Early endosome membrane {ECO:0000250}. Cell
CC       projection, dendrite {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Maternally expressed, it decreases at mid blastula
CC       transition and reappears at late neurulation. Expressed at higher
CC       levels in the anterior and dorsal regions of embryonic stages 16, 24
CC       and 37. In adult it appears to be ubiquitously expressed with higher
CC       expression in brain and ovary. Expression in the brain, brachial
CC       arches, trigeminal facial ganglion, and the retina of swimming tadpole
CC       stage of development.
CC   -!- PTM: Phosphorylated. Autophosphorylation is stimulated by ligands (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00159}.
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DR   EMBL; U14164; AAA74888.1; -; mRNA.
DR   PIR; I51672; I51672.
DR   RefSeq; NP_001084070.1; NM_001090601.1.
DR   AlphaFoldDB; Q91571; -.
DR   SMR; Q91571; -.
DR   GlyCosmos; Q91571; 3 sites, No reported glycans.
DR   GeneID; 399288; -.
DR   CTD; 399288; -.
DR   BRENDA; 2.7.10.1; 6725.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR   GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR   GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR   GO; GO:0060996; P:dendritic spine development; ISS:UniProtKB.
DR   GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR   CDD; cd10476; EphR_LBD_B1; 1.
DR   CDD; cd00063; FN3; 2.
DR   CDD; cd05065; PTKc_EphR_B; 1.
DR   CDD; cd09551; SAM_EPH-B1; 1.
DR   Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR   InterPro; IPR027936; Eph_TM.
DR   InterPro; IPR034231; EphB1_rcpt_lig-bd.
DR   InterPro; IPR042819; EphB1_SAM.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR   PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR   PANTHER; PTHR46877:SF17; EPHRIN TYPE-B RECEPTOR 1; 1.
DR   Pfam; PF14575; EphA2_TM; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM01411; Ephrin_rec_like; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS51550; EPH_LBD; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell adhesion; Cell membrane; Cell projection; Endosome;
KW   Glycoprotein; Kinase; Membrane; Neurogenesis; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..985
FT                   /note="Ephrin type-B receptor 1-A"
FT                   /id="PRO_0000016826"
FT   TOPO_DOM        20..542
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        564..985
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          21..203
FT                   /note="Eph LBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT   DOMAIN          324..434
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          435..532
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          620..883
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          912..976
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   MOTIF           983..985
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        745
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         626..634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         652
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        482
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   985 AA;  110104 MW;  BE72CD1BFF51E623 CRC64;
     MELNVLLLLL CLSGGQVGAV EETLMDTRTA TAELGWTANP SSGWEEVSGY DENLNTIRTY
     QVCNVFGPKQ NNWLLTTFIP RRGAHRVYVE MRFTVRDCSS LPNVPGSCKE TFNLYYYETD
     SNIENKISTF WNESPYLKVD TIAADESFSQ VDFGGRLMKV NTEVRSFGPL TRSGFYLAFQ
     DYGACMSLLS VRVFFKEMPS VVQNLLVFPE TMTGAESTSL VIARGTCIPN AEEVDVPIKL
     YCNGDGEWMV PIGKCTCKAG YEPENHVVCK ACPAAMFKAN QGMGICAQCP ANSRSTSEAS
     PICICRNGYY RADFDTPEAP CTSVPSGPRN VISIVNETAI TLEWHPPRET GGRDDVDYNI
     VCKKCRADRR ACSRCDDNVD FVPRQLGLTD TRVFISNLWA HTPYTFETQA VNGVTNKSPF
     PPQHVSVNIT TNQAAPSSVP IMHQVKATMK SITLSWPQQE QPNGIILDYE IRYYEKDHHE
     FNSSLARSQT NTARRTGGRV WMFMSVQVRA RTVAGYGKFS SKCGFQTLTA EDYKSELREQ
     LPLTGSAAAG VVFIVSLVAI SIVCSRKRTY SKEAVYSDKL QHYSTGRGSP GMKIYIDPFT
     YEDPNEAVRE FAKEIDVSFV KIEEVIGAGE FGEVYKGRLK LPSKREISVA IKTLKAGYSE
     KQRRDFLSEA SIMGQFDHPN IIRLEGVVTK SRPVMIITEF MENGALDSFL RQNDGQFTVI
     QLVGMLRGIA AGMKYLSEMN YVHRDLAARN ILVNSNLVCK VSDFGLSRYL QDDTSDPTYT
     SSLGGKIPVR WTAQEAIAYR KFTSASDVWS YGIVMWEVMS YGERPYWTMS NQDVINAIEQ
     DYRLPPPMDC PAALHQLMLD CWQKDRNSRP RLAEIVNTLR PMIRNPASLK TVATIPAVPS
     QPLLDRSIPD ISAFTSVDDW LSAIKMGQYR DNFLSSGFTS LQLVAQMTSE DLLRIGITLA
     GHQKKILNSI QSMRVQITQS PTSIA
//