EPHB3_XENLA
ID EPHB3_XENLA Reviewed; 974 AA.
AC Q91735;
DT 01-DEC-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 3;
DE EC=2.7.10.1;
DE AltName: Full=Tyrosine-protein kinase receptor TCK;
DE Flags: Precursor;
GN Name=ephb3; Synonyms=tck;
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).
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. Generally has an
CC overlapping and redundant function with EPHB2. Like EPHB2, functions in
CC axon guidance during development. In addition to its role in axon
CC guidance also plays an important redundant role with other ephrin-B
CC receptors in development and maturation of dendritic spines and the
CC formation of excitatory synapses. May control other aspects of
CC development through regulation of cell migration and positioning (By
CC similarity). {ECO:0000250}.
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 {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the embryo in pre-somitic mesoderm,
CC caudal somites, midbrain, and cement gland. Most abundant in adult
CC brain, eye, heart, lung and ovary. Lower levels in intestine, kidney,
CC oviduct and pharynx.
CC -!- DEVELOPMENTAL STAGE: Expressed during early development.
CC -!- PTM: Phosphorylated. Autophosphorylates upon ligand-binding.
CC Autophosphorylation on Tyr-590 is required for interaction with SH2
CC domain-containing proteins (By 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; L43620; AAA93526.1; -; mRNA.
DR RefSeq; NP_001081434.1; NM_001087965.1.
DR AlphaFoldDB; Q91735; -.
DR SMR; Q91735; -.
DR PRIDE; Q91735; -.
DR GeneID; 397834; -.
DR CTD; 2049; -.
DR BRENDA; 2.7.10.1; 6725.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
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:0005003; F:ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; 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:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR027936; Eph_TM.
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; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
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; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF07647; SAM_2; 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; 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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cell projection; Developmental protein;
KW Disulfide bond; Glycoprotein; Kinase; Membrane; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..974
FT /note="Ephrin type-B receptor 3"
FT /id="PRO_0000016833"
FT TOPO_DOM 17..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..974
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..196
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 318..426
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 427..522
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 609..872
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 901..965
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 972..974
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 734
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 615..623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 641
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 590
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..178
FT /evidence="ECO:0000250"
SQ SEQUENCE 974 AA; 108264 MW; F881412E86628533 CRC64;
MLPAVFVILA LSAVQGLEET LMDTKWTTSE LAWVAYPDSG WEEVSGYDEA SNPIRTYQVC
NVRDSNQNNW LRTQFIPRQD VQRVYVELKF TVRDCNSLPN LRGSCKETFN FFYYESDSDS
ASADSPFWME NPYIKVDTIA PDESFSRRDS GRVNTKIRSF GPISRAGFYL AFQDLGACVS
LISVRVFFKK CPRTTAGFAS FPETITGAEP TSLVIAPGTC VPNALEVSVP LKLYCNGDGD
WMVPVGACTC AAGFEPAGKD TQCQACKRGT YKSKQGEGSC MPCPANSRAI SSAATICSCQ
NGYYRADGES AETACTSVPS APRQVISNVN ETSVVLEWAE PGHLGGRDDV LYNVICKKCL
ERLCSRCDDN VQFWPRQLGV TQRLVSVSHL QAHTKYSFEI QAVNGVSGKS PHIPNYFTVN
ITTNQAAPSS VPMVQSHGSL ANSLTLSWAP PESPNGIILD YEIKYYAKGH IGAGNTVTSQ
RTTVRMEGMT PDTVYVVQVR ARTVAGYGAY SEPREFQTIA EDGDRSSLQE QVPMVVGSVT
AGLIFIIAVV IIVIVCFSRK QRNDSESEYT EKLQQYMVPG MKLYIDPFTY EDPNEAVRDF
AKEIDISCVK IEEVIGAGEF GEVCRGKLKQ AGRREQFVAI KTLKAGYTEQ QRRDFLGEAS
IMGQFDHPNI IRLEGVVTRS RPVMILTEFM ENGALDSFLR MNDGQFTVIQ LVGILRGIAS
GMKYLSEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRFLE NSRSDPTYTS ALGGKIPIRW
TAPEAISYRK FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVINAIEQD YRLPPPMDCP
SALHQLMLDC WLRDRNLRPK FSQIVSSLDK LIRNAASLKV TSPGQAGVSQ QLLDRTVPDY
TTFPTVSDWL EAIKMGQYQE NFLSAGFTSF HLVAQMTAED LLRIGVTLAG HQKKLLNSVQ
DMRLQMSQTL PVQV
