EPHB3_CHICK
ID EPHB3_CHICK Reviewed; 988 AA.
AC Q07498;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ephrin type-B receptor 3;
DE EC=2.7.10.1;
DE AltName: Full=EPH-like kinase 10;
DE Short=EK10;
DE Short=cEK10;
DE Flags: Fragment;
GN Name=EPHB3; Synonyms=CEK10;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Embryo;
RX PubMed=8510926;
RA Sajjadi F.G., Pasquale E.B.;
RT "Five novel avian Eph-related tyrosine kinases are differentially
RT expressed.";
RL Oncogene 8:1807-1813(1993).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q07498-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q07498-2; Sequence=VSP_003019;
CC -!- TISSUE SPECIFICITY: Present in 10-day embryonic brain and body tissues.
CC Prominent expression in kidney. Lower expression in lung, and barely
CC detectable in brain, liver, heart, skeletal muscle and thymus.
CC -!- PTM: Phosphorylated. Autophosphorylates upon ligand-binding.
CC Autophosphorylation on Tyr-604 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; Z19061; CAA79511.1; -; mRNA.
DR PIR; I50611; I50611.
DR AlphaFoldDB; Q07498; -.
DR SMR; Q07498; -.
DR STRING; 9031.ENSGALP00000038993; -.
DR PaxDb; Q07498; -.
DR VEuPathDB; HostDB:geneid_396179; -.
DR eggNOG; KOG0196; Eukaryota.
DR InParanoid; Q07498; -.
DR OrthoDB; 933071at2759; -.
DR PhylomeDB; Q07498; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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 GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10478; EphR_LBD_B3; 1.
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; IPR034245; EphB3_rcpt_lig-bd.
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; 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 Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW Developmental protein; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT CHAIN <1..988
FT /note="Ephrin type-B receptor 3"
FT /id="PRO_0000160276"
FT TOPO_DOM <1..534
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 535..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..988
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 11..189
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 311..424
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 425..522
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 623..886
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 915..979
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 986..988
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 748
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 629..637
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 604
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..171
FT /evidence="ECO:0000250"
FT VAR_SEQ 558..572
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8510926"
FT /id="VSP_003019"
FT NON_TER 1
SQ SEQUENCE 988 AA; 109579 MW; EEA0D39C03FFD3C8 CRC64;
GVSSRARRPP GSSRSSRRGV TSELAWTTHP ETGWEEVSGY DEAMNPIRTY QVCNVREANQ
NNWLRTKFIQ RQDVQRVYVE LKFTVRDCNS IPNIPGSCKE TFNLFYYESD TDSASANSPF
WMENPYIKVD TIAPDESFSK LESGRVNTKV RSFGPLSKNG FYLAFQDLGA CMSLISVRAF
YKKCSNTIAG FAIFPETLTG AEPTSLVIAP GTCIPNAVEV SVPLKLYCNG DGEWMVPVGA
CTCAAGYEPA MKDTQCQACG PGTFKSKQGE GPCSPCPPNS RTTAGAATVC ICRSGFFRAD
ADPADSACTS VPSAPRSVIS NVNETSLVLE WSEPQDAGGR DDLLYNVICK KCSVERRLCS
RCDDNVEFVP RQLGLTGLTE RRIYISKVMA HPQYTFEIQA VNGISSKSPY PPHFASVNIT
TNQAAPSAVP TMHLHSSTGN SMTLSWTPPE RPNGIILDYE IKYSEKQGQG DGIANTVTSQ
KNSVRLDGLK ANARYMVQVR ARTVAGYGRY SLPTEFQTTA EDGSTSKTFQ ELPLIVGSAT
AGLLFVIVVV IIAIVCFRKG MVTEQLLSSP LGRKQRNSTD PEYTEKLQQY VTPGMKVYID
PFTYEDPNEA VREFAKEIDI SCVKIEEVIG AGEFGEVCRG RLKLPGRREI FVAIKTLKVG
YTERQRRDFL SEASIMGQFD HPNIIHLEGV VTKSRPVMII TEFMENCALD SFLRLNDGQF
TVIQLVGMLR GIAAGMKYLS EMNYVHRDLA ARNILVNSNL VCKVSDFGLS RFLEDDPADP
TYTSSLGGKI PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW DMSNQDVINA
VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFAQIVN TLDKLIRNAA SLKVIASVQS
GVSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKENFVNAG FASFDLVAQM TAEDLLRIGV
TLAGHQKKIL SSIQDMRLQM NQTLPVQV
