ID W5M9H7_LEPOC Unreviewed; 1365 AA.
AC W5M9H7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005036.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005036.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; AHAT01011134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01011135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015220966.1; XM_015365480.1.
DR STRING; 7918.ENSLOCP00000005036; -.
DR Ensembl; ENSLOCT00000005044.1; ENSLOCP00000005036.1; ENSLOCG00000004179.1.
DR GeneID; 102696537; -.
DR KEGG; loc:102696537; -.
DR CTD; 245700; -.
DR eggNOG; KOG4258; Eukaryota.
DR GeneTree; ENSGT00940000155404; -.
DR HOGENOM; CLU_000288_166_0_1; -.
DR InParanoid; W5M9H7; -.
DR OMA; FFILCTC; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000018468; Linkage group LG19.
DR Bgee; ENSLOCG00000004179; Expressed in zone of skin and 11 other cell types or tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005899; C:insulin receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005009; F:insulin receptor activity; IBA:GO_Central.
DR GO; GO:0043560; F:insulin receptor substrate binding; IBA:GO_Central.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:InterPro.
DR GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000018468};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1365
FT /note="Tyrosine-protein kinase receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004865737"
FT TRANSMEM 945..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 612..713
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 834..936
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1006..1281
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 669..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1142
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 1146..1147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT BINDING 1160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ SEQUENCE 1365 AA; 154008 MW; 5F1F4E9DCC5CAF2F CRC64;
MRLDTPVVAF VTFICVLSNC GISDGEICKS MDIRNNITHL HAIENCTVIE GHLKILLMFK
TKPEDFRGLR FPKLTMITDY LLLFRVYGLE SLRDLFPNLT VVRGTNLFFN YALVLFEMLQ
LKEIGLHSLM NITRGAVRIE KNPDLCYLST LDWSKILDSV EDNYIVSNKD DRECGDVCPG
TAKGKTSCPQ TIFNGHFSER CWTQDHCQRT CPSSCKHRAC TKEGQCCHDE CLGSCTAPND
PRKCVACRRY LHQGACVDNC PAGSYIFEGW RCVSFKFCQD LHNKCKQGTG CDEYVIHNGE
CIPECPSGYT TMNSTMLNCT PCAGLCPKVC TGVKTVDSVT AAQALRGCTI LNGSLVINIR
GGNNIAAELE ANLGQLEEIT GYLKIRRSYA LVSLSFLRKL KLIRGEVLES GNFSFYALDN
QNLRQLWDWS KHNMTILQGR MFFHFNSKLC MSEIRKMEEV TGTKGRDIKN DISMKTNGDQ
ASCETQVLKF TQIRTLSDKI IIKWEPFWPP DYRDLLGFMV LYKEAPYRNV TEFDGQDACG
SNSWVIADVD PPPRASDGRD QVEPGHLIHP LKPWTQYAIF VKTLLSASDE HQVHGAKSEI
IYVRTNATKP SVPLDPISSS NSSSQIMLKW KPPTDANGNI THYLVFCQQQ PEASDLYKFD
YCQKGMKLPS RAPTHQDTEE AQKWNQTDEP GQSGRCCSCP KTETQLKREA EESEYRKTFE
NYLHNEVFEI RTSSAGLETN EDRPSRRRRS LGAVANSTIQ RFFTTPSTLP NASTTRGPEE
EEGAKVVLTV HAKESAVISS LRHFTSYQIE IHACNHPTDP SRCSMAAYVS ARTMPEDKAD
DIVGQVTHEV LTNTVHIRWQ EPKSPNGMII LYEVNYKRLG DSEELHHCVS RKSYSVDQGC
KLRVLHPGNY SVRIRATSLA GNGSWTEPTY FYVQDPRDPS SVMKIAIGSV ICIVLILVVA
GAVFMVVRKK QTEGPTGPLY ASSNPEYLSA NDVYVPDEWE VPREKIDVLR ELGQGSFGMV
YEGIAKEIVK GEPETRVAVK TVNESASLRE RIEFLNEASV MKSFSCHHVV RLLGVVSKGQ
PTLVVMELMT HGDLKSYLRS LRPDAENNPG RPPPTLKEMI QMAAEIADGM AYLNAKKFVH
RDLAARNCMV AEDFTVKIGD FGMTRDIYET DYYRKGGKGL LPVRWMAPES LKDGVFTAHS
DCWSFGVVLW EISTLAEQPY QGLSNEQVLK FVMDGGYLDR PDNCAERLHN LMQMCWQYNP
KMRPTFHEII EMLKDDLHPS FQEVSFFYSE ENKPPETEEF DMDFENMESI PLDPSSYSQR
EESLGRDNGP SMGLRGNYEE HVPYTHMNGG KKNGRILSLP RSSPS
//
