EPHB2_COTJA
ID EPHB2_COTJA Reviewed; 987 AA.
AC Q90344;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ephrin type-B receptor 2;
DE EC=2.7.10.1;
DE AltName: Full=EPH-like kinase 5;
DE Short=EK5;
DE Short=qEK5;
DE Contains:
DE RecName: Full=EphB2/CTF1 {ECO:0000250|UniProtKB:P54763};
DE Contains:
DE RecName: Full=EphB2/CTF2 {ECO:0000250|UniProtKB:P54763};
DE Flags: Precursor;
GN Name=EPHB2; Synonyms=QEK5;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8612986; DOI=10.1006/dbio.1995.8083;
RA Kenny D., Bronner-Fraser M., Marcelle C.;
RT "The receptor tyrosine kinase QEK5 mRNA is expressed in a gradient within
RT the neural retina and the tectum.";
RL Dev. Biol. 172:708-716(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. Functions in axon
CC guidance during development. In addition to axon guidance, also
CC regulates dendritic spines development and maturation and stimulates
CC the formation of excitatory synapses (By 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 -!- 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, axon {ECO:0000250}.
CC Cell projection, dendrite {ECO:0000250}.
CC -!- PTM: Ligand binding induces cleavage by matrix metalloproteinases
CC (MMPs) such as MMP7/MMP9, producing an EphB2/N-terminal fragment (NTF)
CC and a C-terminal long fragment (EphB2-LF). EphB2-LF is further cleaved
CC by MMPs, producing EphB2/CTF1 which is further cleaved by the
CC PS1/gamma-secretase producing EphB2/CTF2.
CC {ECO:0000250|UniProtKB:P54763}.
CC -!- PTM: Polyubiquitinated; ligand binding stimulates ubiquitination.
CC Ubiquitinated by RNF186 at Lys-892, mainly through 'Lys-27'-linked
CC polyubiquitin chains. {ECO:0000250|UniProtKB:P29323}.
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; X91737; CAA62862.1; -; mRNA.
DR AlphaFoldDB; Q90344; -.
DR BMRB; Q90344; -.
DR SMR; Q90344; -.
DR BRENDA; 2.7.10.1; 1673.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; 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:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; 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:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR CDD; cd10477; EphR_LBD_B2; 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; IPR034238; EphB2_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; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
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; 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; 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; Isopeptide bond; Kinase; Membrane;
KW Neurogenesis; Nucleotide-binding; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..987
FT /note="Ephrin type-B receptor 2"
FT /id="PRO_0000016830"
FT CHAIN 537..987
FT /note="EphB2/CTF1"
FT /evidence="ECO:0000250|UniProtKB:P54763"
FT /id="PRO_0000445967"
FT CHAIN 563..987
FT /note="EphB2/CTF2"
FT /evidence="ECO:0000250|UniProtKB:P54763"
FT /id="PRO_0000445968"
FT TOPO_DOM 20..544
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..987
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..203
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 325..435
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 436..531
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 622..885
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 914..978
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 985..987
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 747
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 628..636
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 536..537
FT /note="Cleavage; by a metalloproteinase"
FT /evidence="ECO:0000250|UniProtKB:P54763"
FT SITE 562..563
FT /note="Cleavage; by gamma-secretase/PS1"
FT /evidence="ECO:0000250|UniProtKB:P54763"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..185
FT /evidence="ECO:0000250"
FT DISULFID 98..108
FT /evidence="ECO:0000250"
FT CROSSLNK 892
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P29323"
SQ SEQUENCE 987 AA; 110331 MW; 05D6ECC68B718DD7 CRC64;
MGPLWFCCLP LALLPLLAAV EETLMDSTTA TAELGWMVHP PSGWEEVSGY DENMNTIRTY
QVCNVFESSQ NNWLRTKYIR RRGAHRIHVE MKFSVRDCSS IPNVPGSCKE TFNLYYYESD
FDSATKTFPN WMENPWMKVD TIAADERFSQ VDLGGRVMKI NTEVRSFGPV SKNGFYLAFQ
DYWGCMSLIA VRVFYRKCPR VIQNGADFQE TLSGAESTSL VASRGTCINK AEEVDVPIKQ
HCNGDGEWLV PIGRCMCRPG YESVANGTVC RGCPSGTFKA SQGDEGCVHC PINSRTTSEG
ATNCVCRNGY YRADADPVDM PCTTIPSAPQ SVISSVNETS LMLEWTPPRD SGGREDLVYN
IICKSCGSGR GACTRCGDNV QFAPRQLGLT EPRIYISDLL AHTQYTFEIQ AVNGVTDQSP
FSPQFASVNI TTNQAAPSAV SIMHQVSRTV DSITLSWSQP DQPNGVILDY ELQYYEKNLS
ELNSTAVKSP TNTVTVQNLK AGTIYVFQVR ARTVAGYGRY SGKMYFQTMT EAEYQTSVQE
KLPLIIGSSA AGLVFLIAVV VIIIVCNRRG FERADSEYTD KLQHYTSGHM TPGMKIYIDP
FTYEDPNEAV REFAKEIDIS CVKIEQVIGA GEFGEVCSGH LKLPGKREIF VAIKTLKSGY
TEKQRRDFLS EASIMGQFDH PNVIHLEGVV TKSSPVMIIT EFMENGSLDS FLRQNDGQFT
VIQLVGMLRG IAAGMKYLAD MNYVHRDLAA RNTLVNSNLV CKVSDFGLSR FLEDDTSDPT
YTSALGGKIP IRWTAPEAIQ YRKFTSASDV WSYGIVMWEV MSYGERPYWD MTNQDVINAI
EQDYRLPPPM DCPNALHQLM LDCWQKDRNH RPKFGQIVNT LDKMIRNPNS LKAMAPLSSG
VNLPLLDRTI PDYTSFNTVD EWLDAIKMSQ YKESYASAGF TTFDIVSQMT VEDILRVGVT
LAGHQKKILN SIQVMRAQMN QIQSVEV
