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Database: UniProt
Entry: A0A3P9A2V0_ESOLU
LinkDB: A0A3P9A2V0_ESOLU
Original site: A0A3P9A2V0_ESOLU 
ID   A0A3P9A2V0_ESOLU        Unreviewed;      1372 AA.
AC   A0A3P9A2V0;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, 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   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC   Esocidae; Esox.
OX   NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000034918.2, ECO:0000313|Proteomes:UP000265140};
RN   [1] {ECO:0000313|Ensembl:ENSELUP00000034918.2, ECO:0000313|Proteomes:UP000265140}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25069045;
RA   Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA   von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT   "The genome and linkage map of the northern pike (Esox lucius): conserved
RT   synteny revealed between the salmonid sister group and the Neoteleostei.";
RL   PLoS ONE 9:e102089-e102089(2014).
RN   [2] {ECO:0000313|Ensembl:ENSELUP00000034918.2}
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; ENSELUT00000022095.2; ENSELUP00000034918.2; ENSELUG00000013713.2.
DR   GeneTree; ENSGT00940000155404; -.
DR   Proteomes; UP000265140; LG03.
DR   Bgee; ENSELUG00000013713; Expressed in liver and 15 other cell types or tissues.
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; 3.
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:UP000265140};
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        939..959
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          613..713
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          829..929
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1000..1276
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          733..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1287..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..758
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1137
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         1010
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1034
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1081..1087
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1141..1142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1155
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1372 AA;  154473 MW;  BC6C91A19FFE26E0 CRC64;
     MDRLLSKFHP ISLWALVKSS APLSTGICSS KDIRNNVTNL RSLENCTVIE GHLKIILMFK
     TKPEDFRGLS YPKLAVITDF LLLFRVYGME SLKDLFPNLT VIRGNNLFFN YALVFFEMLQ
     LRDIGLHSLM NITRGAVRIE KNPDLCYLST LDWSKILDSV EDNYIVANKN ERECGDVCPG
     AAKGKTTCQQ TTINGQFNER CWTHKHCQRM CPPSCKHRAC TKDNQCCHES CLGGCSEPQN
     SSSCVACKNL QHQGACVDRC PPGYYTYRGW RCVPFSFCQH LHNKCMQSKS SDCPEYVIHN
     GACIPECPSG YTTVNSTTLV CTPCAGLCPK VCMGQKMVDS VTAAQALRGC TVLNGSMEIN
     LRGGNNIAAE LEANLGQLEE ITGYLTVRRS YALVSLSFLR KLRVIRGATL IDGGYSFYAL
     DNQNLRQLWD WNKHNLTILQ GRMFFQLNIK LCMSEIRRME EVTGTKDRHP KNDIVSKTNG
     DQASCENQEL KFTLVRATHD KILIRWEPFW PPDFRDLLGF MVFYKEAPYA NVTEFDGQDA
     CGSNWVIVDL DPPARATEGK PQVEPGTLIL SLKPWTQYAI MVKTQLSASD EHQVLGAKSK
     IIYHRTEATK PSVPLDPISS SNSSSQIILK WKPPTDPNGN ITHYLVYCQQ QPEASELYKF
     DYCQKGMKLP SRMPTQVDSD GEAKWNQTED EGQGGRCCAC PKTEKQLKKE AEDSEYRKTF
     ENYIHNEVFE PKPRQRRSAM GVANQTHQSS LTTPPTLPEG FATRSPGDED GNNVESAKIR
     LKVFAKESTV ISGLRHFTSY QIDVMACNDP TDPNRCSMAA FVSARTMPEA DDIVGHITYD
     VSEYTVHIKW LEPKAPNGMI ILYEVNYKRL GDTEVTELHH CVSRKMYQQS KGCKLRVVHP
     GNYTVRIRAT SLAGNGSWTE PTHFYVQDLR VDPSNLVKII IGPVIFIVLL IVVASGVFVR
     CGMSNTSTFA CVQPLTVHAF VRACSAVYEP DDWEVGRDKI NILRELGQGS FGMVYEGVAK
     DIVKGEPETR VAVKTVNESA SLRERIEFLN EASVMKGFTC HHVVRLMGVV SKGQPTLVVM
     ELMTHGDLKS YLRCLRPDSE NNPTGRPPPT LREMIQMAAE IADGMAYLNA KKFVHRDLAA
     RNCMVGQDFT VKIGDFGMTR DIYETDYYRK GGKGLLPVRW MAPESLKDGV FTAHSDCWSF
     GVVLWEISTL AEQPYQGLSN EQVLKFVMDG GYLDRPDNCA DRLHNLMSMC WQYNPKLRPS
     FQEIIEMLHE DLHPSFQEVS FYYSQENKPP EQDDFDLDMD MESIPLDPSS YSQRGDHSSS
     YSQRGDHSSE RGEAGSSLGL RQNSYEEHIP YTHMNGAKTN GRILALPRSS PS
//
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