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Database: UniProt
Entry: A0A3Q1DGV6_AMPOC
LinkDB: A0A3Q1DGV6_AMPOC
Original site: A0A3Q1DGV6_AMPOC 
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
//
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