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Ephrin type-B receptor 3 (EC 2.7.10.1) (Tyrosine-protein kinase receptor TCK)

 EPHB3_XENLA             Reviewed;         974 AA.
Q91735;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 139.
RecName: Full=Ephrin type-B receptor 3;
EC=2.7.10.1;
AltName: Full=Tyrosine-protein kinase receptor TCK;
Flags: Precursor;
Name=ephb3; Synonyms=tck;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7478602;
Scales J.B., Winning R.S., Renaud C.S., Shea L.J., Sargent T.D.;
"Novel members of the eph receptor tyrosine kinase subfamily expressed
during Xenopus development.";
Oncogene 11:1745-1752(1995).
-!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
transmembrane ephrin-B family ligands residing on adjacent cells,
leading to contact-dependent bidirectional signaling into
neighboring cells. The signaling pathway downstream of the
receptor is referred to as forward signaling while the signaling
pathway downstream of the ephrin ligand is referred to as reverse
signaling. Generally has an overlapping and redundant function
with EPHB2. Like EPHB2, functions in axon guidance during
development. In addition to its role in axon guidance plays also
an important redundant role with other ephrin-B receptors in
development and maturation of dendritic spines and the formation
of excitatory synapses. May control other aspects of development
through regulation of cell migration and positioning (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Heterotetramer upon binding of the ligand. The
heterotetramer is composed of an ephrin dimer and a receptor
dimer. Oligomerization is probably required to induce biological
responses (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cell projection, dendrite
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the embryo in pre-somitic
mesoderm, caudal somites, midbrain, and cement gland. Most
abundant in adult brain, eye, heart, lung and ovary. Lower levels
in intestine, kidney, oviduct and pharynx.
-!- DEVELOPMENTAL STAGE: Expressed during early development.
-!- PTM: Phosphorylated. Autophosphorylates upon ligand-binding.
Autophosphorylation on Tyr-590 is required for interaction with
SH2 domain-containing proteins (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; L43620; AAA93526.1; -; mRNA.
RefSeq; NP_001081434.1; NM_001087965.1.
UniGene; Xl.1027; -.
ProteinModelPortal; Q91735; -.
SMR; Q91735; -.
GeneID; 397834; -.
KEGG; xla:397834; -.
CTD; 2049; -.
HOVERGEN; HBG062180; -.
KO; K05112; -.
BRENDA; 2.7.10.1; 6725.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005003; F:ephrin receptor activity; ISS:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0060996; P:dendritic spine development; ISS:UniProtKB.
GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
GO; GO:0022407; P:regulation of cell-cell adhesion; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
CDD; cd10478; EphR_LBD_B3; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034245; EphB3_rcpt_lig-bd.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF07699; Ephrin_rec_like; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF07647; SAM_2; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
2: Evidence at transcript level;
ATP-binding; Cell membrane; Cell projection; Developmental protein;
Disulfide bond; Glycoprotein; Kinase; Membrane; Neurogenesis;
Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal;
Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 974 Ephrin type-B receptor 3.
/FTId=PRO_0000016833.
TOPO_DOM 17 534 Extracellular. {ECO:0000255}.
TRANSMEM 535 555 Helical. {ECO:0000255}.
TOPO_DOM 556 974 Cytoplasmic. {ECO:0000255}.
DOMAIN 18 196 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 318 426 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 427 522 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 609 872 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 901 965 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 615 623 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 972 974 PDZ-binding. {ECO:0000255}.
COMPBIAS 178 315 Cys-rich.
ACT_SITE 734 734 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 641 641 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 590 590 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 178 {ECO:0000250}.
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


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