ID Q8UW85_PAROL Unreviewed; 1368 AA.
AC Q8UW85;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN Name=fIR-2 {ECO:0000313|EMBL:BAB83668.1};
OS Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC Paralichthys.
OX NCBI_TaxID=8255 {ECO:0000313|EMBL:BAB83668.1};
RN [1] {ECO:0000313|EMBL:BAB83668.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12010644; DOI=10.1677/joe.0.1730365;
RA Nakao N., Tanaka M., Higashimoto Y., Nakashima K.;
RT "Molecular cloning, identification and characterization of four distinct
RT receptor subtypes for insulin and IGF-I in Japanese flounder, Paralichthys
RT olivaceus.";
RL J. Endocrinol. 173:365-375(2002).
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 EMBL; AB065097; BAB83668.1; -; mRNA.
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: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; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000620-
KW 2}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000620-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU000312};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1368
FT /note="Tyrosine-protein kinase receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004315650"
FT TRANSMEM 943..969
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 626..726
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 1312..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 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; 155167 MW; FE11BC92086DE38B CRC64;
MVSRTEPVMC PRTLCFVLTA VCFMVSCHRA TGEICVSKDI RNNVTNMQTL ENCTVIEGHL
KILLMFRTKP EDFHGLSFPK LRVVTDYLLL FRVYGLESFR DLFPNLTVIR GNNLFFNYAL
VVFEMLQLRE IGLHSLMNIT RGAVRIEKNP DLCYLSTLDW SKILDSVEDN YIIANKNDRE
CGDVCPGAAL GKTTCQTTTI NGHFSERCWT QKHCQKMCPV QCKHRACTKD DQCCHDQCLG
GCLQPNSASH CVACRGLQLE GNCVDRCPEN HFTFKGWRCV TFAFCQDLHN KCKREKERAK
NPDCHEYVIH NGACVADCPS GYTTVNSSSL NCMPCAGLCP KVCMGLKTVD SVTAAQALKG
CTVLNGSLVI NLRGGNNIAA ELEASLGQLE EITGYLTVRR SYALVSLSFF RKLRVIRGEE
QEIGNYSFYA LDNQNLRQLW DWSKHKLTIL QGRMFFLYNS KLCMSEIRRW EEVTGTKDRQ
QKMDIATKTN GDQASCENHP LKFTQIRTMS DKIMVKWEAF WPSDYRDLLG FMVLYKEAPF
RNVTEFDGQD ACGSNSWVIA DVDPPRRAPD GEKNQLEPGH LILPLKPWTQ YAIMVKSQLS
ASDEHQVHGA KSEIIYVRTN STQPSVPLDA ISSSNSSSQI ILKWKPPNDP NGNITHYLVF
CQRQPEASEL YKFDYCQKGM KLPSRVPTQV DSDEEHKWNQ TEEQGSGTRV CACPKTEKEL
KKEKEDSEYR KTFENYLHNE VFEIKRSRQR RAAIDIANRT YFSHTTAPSL PEGTHIPDDE
DTFESTKTVV TVHAKESTVI SNLRHFTSYQ IEIHACNHPK DPERCSMASY VSARTMPEDK
ADDIVGPISS EVTENSVHIT WLEPAAPNGM IILYEVNYKR LGDTEELHYC VSRNMFKVNR
GCKLKVMHPG NYTVRIRATS LAGNGSWTEP TYFYVQDASD PLYIVKIVIG PVICFILLLF
VTVTGFVFFK KNQTQGPSGP IYASSNPEYL SANDVYEEDE WEVAREKIAI LRELGQGTFG
MVYEGNAKDI IKGESETRVA VKTVNESASL RERIEFLNEA SVMKAFSCHH VVRLLGVVSK
GQPTLVVMEL MTHGDLKSFL RSLRPDAENN PGRPPPTLKE MIQMAAEIAD GMAYLNAKKF
VHRDLAARNC MVANDLTVKI GDFGMTRDIY ETDYYRKGGK GLLSVRWMAP ESLKDGVFTA
HSDCWSFGVV LWEISTLAEQ PYQGLSNEQV LKFVMDGGYL DRPDNCADRI HNLMQMCWQY
NPKMRPAFQE IIEMLREDLH PSFQELSFFY SEENKPPVSE DFDLDMENME SIPLDPSSYS
QREQCLDRDE GSSMGLRGSY EEHHIPFTHM NGGKTNGRIL GLPRSSPS
//
