ID A0A3Q1DGV6_AMPOC Unreviewed; 1368 AA.
AC A0A3Q1DGV6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000031556.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000031556.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 SMR; A0A3Q1DGV6; -.
DR STRING; 80972.ENSAOCP00000031556; -.
DR Ensembl; ENSAOCT00000032994.1; ENSAOCP00000031556.1; ENSAOCG00000023289.1.
DR GeneTree; ENSGT00940000155404; -.
DR OMA; WTEATHF; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000257160; Unplaced.
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; 2.
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:UP000257160};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1368
FT /note="Tyrosine-protein kinase receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018729740"
FT TRANSMEM 943..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 624..724
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 843..938
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1008..1283
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 760..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1144
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT BINDING 1018
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1042
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1089..1095
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1148..1149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ SEQUENCE 1368 AA; 154948 MW; 6F96F7A1E6750EDE CRC64;
MVSVMWLRTL YLGFVVTAVW LVMSCHRATG EICPSKDIRN NVTNLQTLEN CTVIEGHLKI
LLMFRTKPED FRGLNFPKLT VVTDYLLLFR VYGLESLSDL FPNLTVIRGN NLFFNYALVV
FEMLQLREIG LHSLMNITRG AVRIEKNPDL CYLSTLDWSK ILDSVEDNYI MANKNDRECG
DVCPGAAVGK TTCQTTTING HFSERCWTQN HCQRMCPVQC KHRACTKDGQ CCHDQCLGGC
LKPNSASHCV ACRGLQHEGN CVERCPKNHF TYKGWRCVSF AFCQDLHNRC KSEKERSKSP
DCHEYVIHNA ACIPECPSGY TTVKSSSLNC TPCAGLCPKV CMGLKTVDSV TAAQALRGCT
VLNGSLVINL RGGNNIAAEL EASLGQLEEI TGYLTVRRSY ALVSLSFFRK LRVIRGEEQE
IGNYSFYALD NQNLRQLWDW SKHKLTILQG RMFFHYNSKL CMSEIRKMEE VTGTKERQVK
NDIASKTNGD QASCENHVLK FTQIRTMSDK IMVKWEPFWP PDFRDLLGFM VLYKEAPFQN
VTEFDGQDAC GSNSWVIADV DPPRRATEGD KDQFEPGHLI LPLKPWTQYA IMVKTQLSAS
DEHQVHGAKS EIIYVRTNAT KPSVPLDPIS SSNSSSQIIL KWKPPNDPNG NITHYLVFCQ
RQPEASELYK FDYCQKGMKL PSRVPTQVDS DEEQKWNQTE EQGQGTRCCA CPKTDKELKK
EKENSEYSKT FENYLHNEVF EIKHSRQRRS VMGIANRTHP FLTTTPTLPG GTGTPDDEDE
ETFESTKTVV TVHAKESTVI SNLRHFTSYQ IEIHACNHVT DSARCSMAAY VSARTMPEHK
ADDILGPINY DVTENTVHIT WQEPAAPNGM IILYEVNYKR LGDTEELHYC VSRNMYKVTR
GCKLKVMHPG NYTVRIRATS LAGNGSWTEP TYFYVQDASD PLYIVKIVIG PIICFVLLLF
VAVAGFIMFK KNQTQGPSGP IYASSNPEYL SANDVYEEDE WEVAREKIAI LRELGQGSFG
MVYEGIAKDI IKGEGETHVA VKTVNESASL RERIEFLNEA SVMKAFSCHH VVRLLGVVSK
GQPTLVVMEL MTHGDLKSYL RSLRPDAENN PGRPPPTLKE MIQMAAEIAD GMAYLNAKKF
VHRDLAARNC MVAHDLTVKI GDFGMTRDIY ETDYYRKGGK GLLPVRWMAP ESLKDGVFTA
HSDCWSFGVV LWEISTLAEQ PYQGLSNEQV LKFVMDGGYL DRPDNCADRL HNLMQMCWQY
NPKMRPTFQE IIEMLREDLH PSFQEVSFFY SEENKPPESE DFDLDMENME SIPLDPSSYS
QREQCSDRDE ASSMGLRGSY EEHHIPFTHM NGGKTNGRIL ALPRSSPS
//