ID A0A3Q1HVV1_ANATE Unreviewed; 1331 AA.
AC A0A3Q1HVV1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
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 Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000011965.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000011965.2}
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 Ensembl; ENSATET00000012161.2; ENSATEP00000011965.2; ENSATEG00000008275.2.
DR GeneTree; ENSGT00940000155404; -.
DR Proteomes; UP000265040; 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; 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; 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:UP000265040};
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 906..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 584..684
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 806..903
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 971..1247
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 519..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1108
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT BINDING 981
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1005
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1052..1058
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1112..1113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ SEQUENCE 1331 AA; 150499 MW; CEC50E89034B2C91 CRC64;
MLFLYMNLLN KDIRNNVTNL QSLENCTIIE GHLKILLMFK TKTEDFAGLS YPKLRVVTDY
VLLFRVYGLE TLSDLFPNLT VIRGNNLFFN YALVIYEMLQ LKEVGLHSLM NITRGAVRIE
KNPDLCYLAT LDWSKILDSV EDNFIVANKN ERECGDVCPG TAHGQTICIQ NTINGHFRGR
CWSQRHCQRS KCVCHGACSL QGQCCHEQCL GGCSEPGNVS SCVACRNLQH GNTCVEKCPP
GYYVFRGWRC VSFSFCQDRD SGCYEYVIHN GACIPECPSG YTTVNSTMLT CSPCAGLCPK
LCVGNKTIDS VTSAQALRGC TVLHGNLIIK IRGGNNIAAE LEASLGQLEE ITGYLTVRRA
YALVSLSFLR KLRIIRGEHL ETDDYAFYAL DNQNLRELWD WSKHNLTIQH GRMFFHYNSK
LCMSEIRKME EVTGTKDRNQ KNNIAVRNNG DQASCETKLL KFTVIKTTSN MIMLKWEPFW
PLDFRDLLGF MVLYKEAPYR NVTEFDGQDA CGSNSWAIAD VDPPSRSTDG KKPEDPGHLI
RPLKPWTQYA IMVKTQLSSS DEHQVHGAKS EIIYVRTNAS KPSVPLDPIS SSNSSSQIIL
KWKPPTSPNG NITHYRVICR KQLEDSDLYK FDYCLQGMKL PSRTPTHLDS EDEQKWNHTD
EPTSGGRCCA CPKTDNQLKK EQEEIEYRKT FENYLHNEVF LLPNTSQLLY LFFCFFRPSR
RRRSVGVANA TQTPHFLTTA PSLAFGSSTV ELKVLSKEST VISNLHHFTS YKIEIMACNH
PTDLKRCSMA TYVSARTMPE EKADDIPGPV THEIVTAEPP YVLIKWNAPP SPNGLIILYE
VFYRRVGETE VHTACVSRPA YIKSNGTKLS LLHPGNYSVR VRATSLAGNG SFTETMYFFM
PNPDPGLIWI VTGPVICFIL LLFVGGGIFW ILKKRQTEGP TGPLIASSNP EYISANDVYV
PDEWEVPREK INLLRELGQG SFGMVYEGIA KDIVKGDPET RVAVKTVNES ASLRERIEFL
NEASVMKAFS CHHVVRLLGV VSKGQPTLVV MELMTHGDLK SYLRSLRPDS ENNPSGRPPP
TLKEMIQMAA EIADGMAYLN AKKFVHRDLA ARNCMVAEDF TVKIGDFGMT RDIYETDYYR
KGGKGLLPVR WMAPESLKDG VFTAHSDCWS FGVVLWEIST LAEQPYQGLS NEQVLKFVMD
GGYLDRPENC PERMHNLMQM CWQYNPKMRP TFHEIIEMLR EDLHPSFQEV SFFYSEENKV
PETEEFDLDL DNMESIPLDP SSYLQREESL GRDSGPSVAL RGNYEEHVPY THMNGGKKNG
RILSLPRSSP S
//