EPB1B_XENLA
ID EPB1B_XENLA Reviewed; 902 AA.
AC Q91736;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ephrin type-B receptor 1-B;
DE EC=2.7.10.1;
DE AltName: Full=Tyrosine-protein kinase receptor XELK;
DE Flags: Fragment;
GN Name=ephb1-b; Synonyms=xelk;
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=7478602;
RA Scales J.B., Winning R.S., Renaud C.S., Shea L.J., Sargent T.D.;
RT "Novel members of the eph receptor tyrosine kinase subfamily expressed
RT during Xenopus development.";
RL Oncogene 11:1745-1752(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 respectively
CC (By similarity). {ECO:0000250, 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}; Single-pass
CC type I membrane protein {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the embryo in the brain and spinal
CC cord and in the first and fourth visceral arches. Most abundant in
CC adult brain, with lower levels in eye, heart, ovary, oviduct, lung and
CC pharynx.
CC -!- DEVELOPMENTAL STAGE: Expressed during early 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; L43621; AAA93527.1; -; mRNA.
DR AlphaFoldDB; Q91736; -.
DR SMR; Q91736; -.
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; 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; 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; 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; 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; PS00790; RECEPTOR_TYR_KIN_V_1; 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; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN <1..902
FT /note="Ephrin type-B receptor 1-B"
FT /id="PRO_0000160275"
FT TOPO_DOM <1..459
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..902
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..119
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 240..350
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 351..448
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 537..800
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 829..893
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 900..902
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 662
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 543..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 569
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 902 AA; 100851 MW; CCB9ABF7D39273CA CRC64;
HRVYVEMRFT VRDCSSLPNV PGSCKETFNL YYYETDSNID NKISTFWNES PYLKVDTIAA
DESFSQVDFG GRLMKVNTEV RSFGPLTRSG FYLAFQDYGA CMSLLSVRVF FKKCPSVVQN
FAVFPETMTG AESTSLVIAR GTCIPNAEEV DVPIKLYCNG DGEWMVPIGK CTCKAGYEPE
NHVVCKACPA AMFKANQGMG ICAQCPANSR STSEASPICI CRNGYYRADF DTPEAPCTSV
PSGPRNVISI VNETAITLEW HPPRETGGRD DVNYNIICKK CQSDRRGCSH CDDNVDFVPR
QLGLTDTRVF ISNLWVHTPY TFEIQAVNGV TNKSPFPPQH VSVNITTNQA APSSVPIMHQ
VKATMKSITL SWPQPEQPNG IILDYEIRYY EKDHHEFNSS LARSQTNTAS IEGLRPGVVY
VVQVRARTVA GYGKFSSKMC FQTLTEEDYK SELREQLPLI AGSAAAGVVF IVSLVAISIV
CSRKRTYSKE AVYSDKLQHY STGRGSPGMK IYIDPFTYED PNEAVREFAK EIDVSFVKIE
EVIGAGEFGE VYKGRLKLPS KREISVAIKT LKAGYSEKQR RDFLSEASIM GQFDHPNIIR
LEGVVTKSRP VMIITEFMEN GALDSFLRQN DGQFTVIQLV GMLRGIAAGM KYLSEMNYVH
RDLAARNILV NSNLVCKVSD FGLSRYLQDD TSDPTYTSSL GGKIPVRWTA PEAIRYRKFT
SASDVWSYGI VMWEVMSYGE RPYWDMSNQD VINAIEQDYR LPPPMDCPAA LHQLMLDCWQ
KDRNSRPRFG EIVNTLDKMI RNPASLKTVA TIPAVPSQPL LDRSIPDISA FTSVDDWLSA
IKMGQYRDNF LSSGFTSLHV VAQMTSEDLL RIGITLAGHQ KKILNSIQSM RVQISQSPTS
IA
