EPB1A_XENLA
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 03-AUG-2022, entry version 155.
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 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:0005887; C:integral component of 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; cd09551; SAM_EPH-B1; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
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 Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF00041; fn3; 1.
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; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 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
