EPHB3_DANRE
ID EPHB3_DANRE Reviewed; 500 AA.
AC O13147;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ephrin type-B receptor 3;
DE EC=2.7.10.1;
DE AltName: Full=EPH-like kinase 3;
DE AltName: Full=Tyrosine-protein kinase receptor ZEK3;
DE Flags: Fragment;
GN Name=ephb3; Synonyms=ek3, zek3;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9186052;
RX DOI=10.1002/(sici)1097-0177(199706)209:2<166::aid-aja3>3.0.co;2-g;
RA Bovenkamp D.E., Greer P.;
RT "Novel Eph-family receptor tyrosine kinase is widely expressed in the
RT developing zebrafish nervous system.";
RL Dev. Dyn. 209:166-181(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. 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). May play a role in early pattern formation within the
CC developing nervous system. {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: Widely expressed in the developing nervous system.
CC -!- PTM: Phosphorylated. Autophosphorylates upon ligand-binding.
CC Autophosphorylation on Tyr-168 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; U89379; AAC60221.1; -; mRNA.
DR AlphaFoldDB; O13147; -.
DR SMR; O13147; -.
DR STRING; 7955.ENSDARP00000040208; -.
DR PRIDE; O13147; -.
DR ZFIN; ZDB-GENE-990415-60; ephb3a.
DR eggNOG; KOG0196; Eukaryota.
DR InParanoid; O13147; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Cell projection; Developmental protein; Kinase;
KW Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT CHAIN <1..500
FT /note="Ephrin type-B receptor 3"
FT /id="PRO_0000160277"
FT TOPO_DOM <1..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN <1..64
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 187..450
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 421..500
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 76..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 498..500
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 312
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 193..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 168
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 500 AA; 55911 MW; DBEA421E31E693B2 CRC64;
PLLVLDLIIQ ERGESFSHTV TAQHTSAKVE GLKAGTVYSV QVRARTVAGY GRYSNPVDFS
TSLYVCPVSS SSTSMHLRRR EELTTTTTGL KSREERFQKS DDPERSVQDL LPLIVGSASA
GFVVILAMIV IAVVCLRRQR TGSELEYTEK LQQYVSPGVK VYIDPFTYED PNEAVHEFAR
EIDISCVKIE EVIGAGEFGE VCRGRLKQAG RKETTVAIKT LKAGYTEHQR RDFLSEASIM
GQFDHPNVIH LEGVLTRSCP VLIVTEFMEN GALDSFLRLN DGRFTVTQLV GMLRGIAAGM
KYLSDMNYVH RDLAARNVLV NSNLVCKVSD FGLSRFLDDN SSDPTYTSSL GGKIPIRWTA
PEAIAFRKFT SASDVWSYGI VMWEVMSFGE RPYWDMSNQD VMNAVEQDYR LPPPMDCPAV
LHQLMLECWV KERNMRPRFG QIVSTLDKFL RNAASLKVLT STHSGDLCRI GGTLPGHQRK
SIGDAQDIKQ QMSQTLPIRV
