ID A0A0A0A3W1_CHAVO Unreviewed; 1338 AA.
AC A0A0A0A3W1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
DE Flags: Fragment;
GN ORFNames=N301_07235 {ECO:0000313|EMBL:KGL88088.1};
OS Charadrius vociferus (Killdeer) (Aegialitis vocifera).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Charadriiformes; Charadriidae; Charadrius.
OX NCBI_TaxID=50402 {ECO:0000313|EMBL:KGL88088.1, ECO:0000313|Proteomes:UP000053858};
RN [1] {ECO:0000313|EMBL:KGL88088.1, ECO:0000313|Proteomes:UP000053858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N301 {ECO:0000313|EMBL:KGL88088.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001171,
CC ECO:0000256|RuleBase:RU000312};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Insulin receptor subfamily.
CC {ECO:0000256|RuleBase:RU000312}.
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DR EMBL; KL870363; KGL88088.1; -; Genomic_DNA.
DR STRING; 50402.A0A0A0A3W1; -.
DR Proteomes; UP000053858; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043560; F:insulin receptor substrate binding; IEA:InterPro.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00064; FU; 1.
DR CDD; cd05061; PTKc_InsR; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.80.20.20; Receptor L-domain; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040969; Insulin_TMD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_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; IPR016246; Tyr_kinase_insulin-like_rcpt.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF535; INSULIN RECEPTOR; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF17870; Insulin_TMD; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000620; Insulin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00261; FU; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000620-2, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW Reference proteome {ECO:0000313|Proteomes:UP000053858};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000312};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 916..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 588..690
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 814..909
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 979..1254
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1315..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1115
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT BINDING 989
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1013
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1060..1066
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1119..1120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL88088.1"
FT NON_TER 1338
FT /evidence="ECO:0000313|EMBL:KGL88088.1"
SQ SEQUENCE 1338 AA; 151556 MW; 6C8BDD39B94DEA9E CRC64;
VCRSMDIRNN LTRLNMLENC TVIEGHLQIL LMFKTKPEDF RELSFPKLTM ITDYLLLFRV
YGLESLKGLF PNLTVIRGTH LFFNYALVIF EMVHLKEIGL YNLMNITRGA VRIEKNNELC
YLSTIDWSRI LDSVEDNYIV ANKDDKEECG DVCPGTVKGK SNCPPTVING IFIERCWTHD
RCQRVCPAAC KSQGCTSDGQ CCHSECLGDC TEPNNPEKCV ACRNFYLEGK CVDTCPPGYY
RFEGWRCVTF SFCQELHNKC KNARESGCHV IHNNECVHEC PSGYIMNSSN LHCTPCAGPC
PKVCDYGKEK TIDSVTSAQE LRGCTVVNGS LVINIRGGNN IAAELEANLG LIEEISGYLK
IRRSYALVSL SFFRKLHLIR GETLEAGNYS FYALDNQNLR QLWDWSKHNL TIARGKLFFH
YNPKLCLSEI HKMEEISGTK GRQERNDIAL KTNGDQASCE NELLKFSSIR TSHDKILLKW
EPYWPPDFRD LLGFMLFYKE APYQNVTEFD GQDACGSNSW TVVDVDPPPR SNEPKAQAQP
GWLLRGLKPW TQYAVFVKTL VTFSDERRTY GAKSEIIYVQ TNATVPSVPL DPISVSNSSS
QIILKWKPPS EPNGNITHYL VFWQQQAEDS ELYELDYCLK GLKLPSRTWS PPFESEDPQK
YNQSENEDVS GECCSCPKTD SQIQKELEES AFRKTFENYL HNEVFVPRYR HQTTLLRWPS
RKRRDLGSVA NATVVIPTIA SSPNNSAAAS ENAEEQKPFE KVKSKESLVI SGLRHFTGYR
IELHACNHDA QESRCSVAAY VSARTMPEAK ADDIVGPVTH ELVEKNTVHL KWQEPKEPNG
LIVLYEVNYG RLGETEEAHY CVSRKHFANE QGCKLRGLQP GNYSVRIRAT SLAGNGSWTE
PTYFYVADYL NAQPNIAVII VPIIFAIIIA GIIGAAYVLV KKRQTEGPTG PLYASSNPEY
ISASDVYVPD EWEVPRDKIT LLRELGQGSF GMVYEGIAKD IVKGEPETRV AVKTVNESAS
LRERIEFLNE ASVMKGFSCH HVVRLLGVVS KGQPTLVVME LMAHGDLKSY LRSLRPDAEN
NPGRPPPTLR EMIQMAAEIA DGMAYLNAKK FVHRDLAARN CMVAEDFTVK IGDFGMTRDI
YETDYYRKGG KGLLPVRWMA PESLKDGVFT ACSDVWSFGV VLWEISSLAE QPYQGLSNEQ
VLKFVMDGGY LDQPDNCPER LHSLMQMCWQ YNPKMRPTFI EIIEMLKEDL HPSFHEVSFF
YSEENKPLET EEYEMDFENM ESIPLDPSSY SQRDKVLGRD NGPSMALKGN YEEHIPYTHM
NGGKKNGRIL SMPRSSPS
//