ID A0A0Q3LUH7_AMAAE Unreviewed; 1327 AA.
AC A0A0Q3LUH7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN ORFNames=AAES_160707 {ECO:0000313|EMBL:KQK74101.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK74101.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK74101.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK74101.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU000311}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU000311}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily.
CC {ECO:0000256|RuleBase:RU000311}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQK74101.1}.
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DR EMBL; LMAW01003089; KQK74101.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3LUH7; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005021; F:vascular endothelial growth factor receptor activity; IEA:InterPro.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:InterPro.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
DR InterPro; IPR041348; VEGFR-2_TMD.
DR InterPro; IPR009135; VEGFR1_rcpt.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF390; VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 2.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF21339; VEGFR-1-like_Ig-like; 1.
DR Pfam; PF17988; VEGFR-2_TMD; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 3.
DR PRINTS; PR01832; VEGFRECEPTOR.
DR PRINTS; PR01833; VEGFRECEPTR1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 6.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 7.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 6.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE 3: Inferred from homology;
KW Angiogenesis {ECO:0000256|ARBA:ARBA00022657};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319,
KW ECO:0000256|RuleBase:RU000311}; Kinase {ECO:0000256|ARBA:ARBA00023137};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000311};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00023137};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000311};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1327
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006205361"
FT DOMAIN 30..121
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 240..323
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 326..417
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 424..545
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 552..644
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 651..737
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 819..1151
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT ACT_SITE 1015
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 853
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1020
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1033
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1327 AA; 148917 MW; DBF256799E5DC9E1 CRC64;
MPRQLLSGTV LLGAALLLAG SSSGSKLKVP ELSIXGTQHV VQAGQSLNLT CRGEMLHSWS
LPETLSKDSK RLKVIKYACG RNGKQSCSSL TLSRTQASDT GNYSCKYPTS PAKKKKESTV
YVFINDAGSP FVEMHSDIPK IIHMTVGREM IIPCRVTAPN IAVTLKKIPG ETLIPDGKTI
IWDSMKGFRI PKATYKFIGL LSCETTVGGH KYSTKYLTHR ETNTIFDVQL STPRLVKLLK
GDSLAINCTV TAAWNTRVQM TWTYPGEARR RGSVTQRIDQ KNTEANIFYS ILIVDKVRDI
DKGQYTCHVK SGPSIKAVNT TVIVYDKVFI NLRRRRKTAL EAVAGRKSYR LSMKVKAFPS
PEVTWLKDGL PAAEKCARYM VKDYSLIIKD VAEEDAGNYT IILSIHQWNL SKNLTVTLTV
NVKPQIYENA VSSFPDPNLY LLGSKQVLTC TVYGIPQPKI KWMWYPCRQN HSRTRHGFCS
YTEGSFILKA GSNIGNKIQS ITERTAVIEG KNKTASTLIV AETKSSGIYS CMASNKVGKS
ERNVSFIVTD VPSGFHISLE KMPIEGENLI LSCSANKFLY KDIAWILPRT VNNQTKAKRS
LKKEYSITLT LTIKNVSLAH SGTYACRARN IYTGKEVLQK KDVTIRAQEA PALLRHLTDQ
TVNTSNSAIL ECQVHGIPEP QISWFKNHEE IQQESGIILG PGSRMLFIER VKEEDEGLYQ
CVATNLKGSV ESAAYVTVQG TSERSNLELI TLTCTCVAAT LFWLLLTLFI RKLKRPYSSE
MKTNHYLSII MDPDEVPLDE QCERLPYDAS KWEIARERLK LGKSLGHGAF GKVVQASAFG
IKKSPTCRIV AVKMLKEGAT ASEYKALMTE LKILIHIGHH LNIVNLLGAC TKNGGPLMVI
VEYCKYGNLS NYLKSKRNFF CPNKDSSLQG EPMKEKKDIE LVEGKKQRLA SVTSSESFAS
SGFQEDKSLS DVEEXEEDVD ELYKLPLTME DLISYSFQVA RGMEFLSSRK CIHRDLAARN
ILLSENNVVK ICDFGLARDI YKNPDYVRKG DARLPLKWMA PESIFDKIYN TKSDVWSYGV
LLWEIFSLGA SPYPGVQIDE DFCSRLKEGT RMRAPEQASE EIYQIMLDCW RNNPNDRPRF
SELVKKLGDL LQANVQQDGK DYVPLDTIFT KESGFPPASD PVCNESFPVT NSNWGSTENI
RYINTFKIKP PQRIKTFEEL PIKETLVWND YQADSGMVLA PEELKRFTWT GSKQKRTPFS
IKGASRSKES VLSGITKPRS FCSFSCDQLS DSKRRYTYGN VVLEKMRASH SPPPDYNSVV
LYSQPPV
//
