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Database: UniProt
Entry: G3P8C9_GASAC
LinkDB: G3P8C9_GASAC
Original site: G3P8C9_GASAC 
ID   G3P8C9_GASAC            Unreviewed;      1366 AA.
AC   G3P8C9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000013853.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000013853.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000013853.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-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   STRING; 69293.ENSGACP00000013853; -.
DR   Ensembl; ENSGACT00000013878.1; ENSGACP00000013853.1; ENSGACG00000010475.1.
DR   eggNOG; KOG4258; Eukaryota.
DR   GeneTree; ENSGT00940000155404; -.
DR   InParanoid; G3P8C9; -.
DR   OMA; FFILCTC; -.
DR   TreeFam; TF351636; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000010475; Expressed in intestinal epithelial cell and 10 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:0043009; P:chordate embryonic development; IEA:Ensembl.
DR   GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR   GO; GO:0006096; P:glycolytic process; IEA:Ensembl.
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; 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; 2.
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:UP000007635};
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        942..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          626..716
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          841..938
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1006..1282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          686..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1308..1366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1312..1326
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1143
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         1016
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1040
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1087..1093
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1147..1148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1161
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1366 AA;  153971 MW;  8C842BAB927302B3 CRC64;
     MRRWTLRLRA QIVCFIVGTC IVFQCGLIHG EICQSKDIRN NVTNLQSVEN CTIIEGHLKI
     LLMFKTKTED FRGLSYPRLQ VVTDYVLLFR VYGLEALTDL FPNLAVIRGN NLFFNYALVI
     YEMLQLKEVG LHSLMNITRG AVRIEKNPDL CYLATLDWSK VLDSVEDNFI VDNKNDRECG
     DVCPGTAQGQ TTCPQNTING HFRSRCWSQN HCQRMCLDNC RHSACNHKGQ CCHDQCLGGC
     SEPGNASSCV ACRNLQHGNN CMEKCPPGYY VFRGWRCVSF SFCQQELHNQ CKDSKKLNQD
     RELGCHEYVI HNGACIPECP SGYTTINSTT LTCSPCAGLC PKLCAGNKTI DSVTSAQALR
     GCTVLHGNMI IKIRGGNNIA AELEASLGQL EEITGHLTVR RAYALVSLSF LRKLRVIRGE
     HLEGDVFAFY ALDNQNLHEL WDWSKHNLTI HHGRMFFHYN SKLCMSEIRK MENVTGTKER
     NQKNDIAVRT NGDQASCVTK LLKFTLIKTS SNMIMLKWEP FWPSDFRDLL GFMVLYKETL
     YRNVTEFDGQ DACGSNSWAI ADVDPPQRST EGKKADDPGY LIRPLKPWTL YAIMVKTQLS
     TSDEQQVNGA KSKIIYVRTD ASKPSVPLDP ISSSNSSSQI ILKWKPPTNP NGNITHYRVI
     CRKQSEDSDL YKFDYCLQGM KLPSRTPTPT VRMNRSGTTQ TSPPGRCCAC PKTDYQLKKE
     QEEIEYRKTF ENYLHNEVFE SRPSRRRRSV GVANATLPSF FLPAAPGLAF GSTTVPPEDE
     EGSKVELKVS SKESTVISNL HHFTSYKIEI IACNKVKDVE QCSLASLVSA RTMPEEKADD
     IPGTVTHEIV AAEPPYVLIK WDSPRSPNGL IILYEVYYRK VEDTEDLTAC VSRPAYLKSG
     GTKLSLMHPG NYSVRVRATS LAGNGSFTET TYFYMPNSDP GLIWIVMGPV ICFILLLFIG
     GGVFVILKKR QTEGPTGPLI ASSNPEYIST NDVYIPDEWE VPRDKITVLR ELGQGSFGMV
     YEGIAKDIIK GDPDTQVAVK TVNESASLRE RIEFLNEASV MKAFNCHHVV RLLGVVSKGQ
     PTLVVMELMT HGDLKSYLRG LRPDSENNPT GRSPPTLKEM IQMAAEISDG MAYLNAKKFV
     HRDLAARNCM VAEDFTVKIG DFGMTRDIYE TDYYRKGGKG LLPVRWMAPE SLKDGVFTAH
     SDCWSFGVVL WEITTLAEQP YQGLSNEQVL KFVMDGGYLD RPDNCPERMH SLMQMCWQYN
     PKMRPLFQEI IEMLREDLHP SFHDFSFFYS EENKVPETEE YDLDLDNMES IPLDPSSYSQ
     REESLGRDSG PSAARRGNYE EHVPYTHMNG GKKNGRILSL PRSSPS
//
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