EPHB5_CHICK
ID EPHB5_CHICK Reviewed; 1002 AA.
AC Q07497;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ephrin type-B receptor 5;
DE EC=2.7.10.1;
DE AltName: Full=EPH-like kinase 9;
DE Short=EK9;
DE Short=cEK9;
DE Flags: Precursor;
GN Name=EPHB5; Synonyms=CEK9;
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].
RX PubMed=8909550; DOI=10.1083/jcb.135.3.781;
RA Soans C., Holash J.A., Pavlova Y., Pasquale E.B.;
RT "Developmental expression and distinctive tyrosine phosphorylation of the
RT Eph-related receptor tyrosine kinase Cek9.";
RL J. Cell Biol. 135:781-795(1996).
RN [2]
RP PARTIAL NUCLEOTIDE SEQUENCE.
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 for members of the ephrin-B family.
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 -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Most abundant in thymus and detectable in brain,
CC retina, kidney, lung and heart. Not detected in skeletal muscle and
CC liver.
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; U23783; AAB41054.1; -; mRNA.
DR PIR; S33506; S33506.
DR RefSeq; NP_001004387.1; NM_001004387.1.
DR AlphaFoldDB; Q07497; -.
DR SMR; Q07497; -.
DR STRING; 9031.ENSGALP00000023737; -.
DR iPTMnet; Q07497; -.
DR PaxDb; Q07497; -.
DR PRIDE; Q07497; -.
DR GeneID; 418308; -.
DR KEGG; gga:418308; -.
DR CTD; 2051; -.
DR VEuPathDB; HostDB:geneid_418308; -.
DR eggNOG; KOG0196; Eukaryota.
DR InParanoid; Q07497; -.
DR OrthoDB; 933071at2759; -.
DR PhylomeDB; Q07497; -.
DR BRENDA; 2.7.10.1; 1306.
DR PRO; PR:Q07497; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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; IBA:GO_Central.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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; 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; 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; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1002
FT /note="Ephrin type-B receptor 5"
FT /id="PRO_0000016836"
FT TOPO_DOM 30..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..1002
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..213
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 344..452
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 453..548
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 637..900
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 929..993
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 906..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1000..1002
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 907..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 762
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 643..651
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 669
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1002 AA; 111947 MW; 6D9635B500D8B0DA CRC64;
MDSNADISAR RVSGMDWLWL VCFFHLVTSL EEILLDTTGE TSEIGWTSHP PDGWEEVSVR
DDKERQIRTF QVCNMDEPGQ NNWLRTHFIE RRGAHRVHVR LHFSVRDCAS MRTVASTCKE
TFTLYYHQSD VDIASQELPE WHEGPWTKVD TIAADESFSQ VDRTGKVVRM NVKVRSFGPL
TKHGFYLAFQ DSGACMSLVA VQVFFYKCPA VVKGFASFPE TFAGGERTSL VESLGTCVAN
AEEASTTGSS GVRLHCNGEG EWMVATGRCS CKAGYQSVDN EQACQACPIG SFKASVGDDP
CLLCPAHSHA PLPLPGSIEC VCQSHYYRSA SDNSDAPCTG IPSAPRDLSY EIVGSNVLLT
WRLPKDLGGR KDVFFNVICK ECPTRSAGTC VRCGDNVQFE PRQVGLTESR VQVSNLLARV
QYTFEIQAVN LVTELSSEAP QYATINVSTS QSVPSAIPMM HQVSRATSSI TLSWPQPDQP
NGVILDYQLR YFDKAEDEDN SFTLTSETNM ATILNLSPGK IYVFQVRART AVGYGPYSGK
MYFQTLMAGE HSEMAQDRLP LIVGSALGGL AFLVIAAIAI LAIIFKSKRR ETPYTDRLQQ
YISTRGLGVK YYIDPSTYED PNEAIREFAK EIDVSFIKIE EVIGSGEFGE VCFGRLKHPG
KREYTVAIKT LKSGYTDEQR REFLSEASIM GQFEHPNVIH LEGVVTKSRP VMIVTEFMEN
GSLDSFLRQK EGQFSVLQLV GMLRGIAAGM RYLSDMNYVH RDLAARNILV NSNLVCKVSD
FGLSRFLEDD ASNPTYTGAL GCKIPIRWTA PEAVQYRKFT SSSDVWSYGI VMWEVMSYGE
RPYWDMSNQD VINAIDQDYR LPPPPDCPTV LHLLMLDCWQ KDRVQRPKFE QIVSALDKMI
RKPSALKATG TGSSRPSQPL LSNSPPDFPS LSNAHEWLDA IKMGRYKENF DQAGLITFDV
ISRMTLEDLQ RIGITLVGHQ KKILNSIQLM KVHLNQLEPV EV
