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Database: UniProt
Entry: A0A340XMY7_LIPVE
LinkDB: A0A340XMY7_LIPVE
Original site: A0A340XMY7_LIPVE 
ID   A0A340XMY7_LIPVE        Unreviewed;      1370 AA.
AC   A0A340XMY7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN   Name=INSR {ECO:0000313|RefSeq:XP_007460649.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007460649.1};
RN   [1] {ECO:0000313|RefSeq:XP_007460649.1}
RP   IDENTIFICATION.
RG   RefSeq;
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   RefSeq; XP_007460649.1; XM_007460587.1.
DR   GeneID; 103085622; -.
DR   CTD; 3643; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000265300; 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; 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; 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; 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};
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:UP000265300};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1370
FT                   /note="Tyrosine-protein kinase receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016394070"
FT   TRANSMEM        946..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          624..726
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          841..935
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1011..1286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          765..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1315..1370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..780
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1315..1329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1147
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         1021
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1045
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1092..1098
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1151..1152
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1370 AA;  154838 MW;  739488A195284992 CRC64;
     MGAGGGRGAA AVPLLVAVAA LLVGAAGHLY PGEVCPGMDI RNNLTRLHEL ANCSVIEGHL
     QILLMFKTRP EDFRDLSFPK LIMITDYLLL FRVYGLESLK DLFPNLTVIR GSRLFFNYAL
     VIFEMVHLKE LGLYNLMNIT RGSVRIEKNN ELCYLATIDW SRILDSVEDN YIVLNKDDNE
     ECGDICPGAA KGKTNCPATV INGQFVERCW THSHCQKVCP TICKSHGCTA EGLCCHSECL
     GNCSEPDDPT KCVACRNFFL DGRCVETCPP PYYHFQDWRC VNFSFCQDLH NKCKNSRRQG
     CHQYVIHNNK CIPECPSGYT MNSSNLMCTP CLGPCPKVCH LLEGEKTIDS VTSAQELRGC
     TIINGSLIIN IRGGNNLAAE LEANLGLIEE ISGYLKIRRS YALVSLSFFR KLRLIRGETL
     EIGNYSFYAL DNQNLRQLWD WSKHNLTITQ GKLFFHYNPK LCLSEIHKME EVSGTKGRQE
     RNDIALKTNG DQASCENELL KFSYIRTSYD KILLKWEPYW PPDFRDLLGF MLFYKEAPYQ
     NVTEFDGQDA CGSNSWTVVD IDPPMRSNDP KSQNHPGWLM RGLKPWTQYA IFVKTLVTFS
     DERRTYGAKS DIIYVQTDAT NPSVPLDPIS VSNSSSQIIL KWKPPSDPNG NITHYLVFWE
     RQEEDGELYE LDYCLKGLKL PSRTWSPPFE SEGSQKHNQS EYEESAGECC SCPKTDSQIL
     KELEESSFRK TFEDYLHNVV FIPRPSRKRR ALGDVGNVTA AVPTIPAFPN TSSTSAPTSS
     EEHRPFEKVV NKESLVISGL RHFTGYRIEL QACNQDSPEE RCSVAAYVSA RTMPEAKADD
     IVGPVTHEIF ENNVVHLMWQ EPKEPNGLIV LYEVSYRRYG EEELHLCVSR RHFALERGCR
     LRGLPPGNYS VRVRATSLAG NGSWTEATYF YVTDYLDVPS NIAKIIIGPL IFVFLFSVVI
     GSIYLFLRKR QPDGPLGPLY ASSNPEYLSA SDVFPCSVYV PDEWEVPREK ITLLRELGQG
     SFGMVYEGNA RDIVKGEAET RVAVKTVNES ASLRERIEFL NEASVMKGFT CHHVVRLLGV
     VSKGQPTLVV MELMAHGDLK SYLRSLRPEA ENNPGRPPPT LQEMIQMAAE IADGMAYLNA
     KKFVHRDLAA RNCMVAHDFT VKIGDFGMTR DIYETDYYRK GGKGLLPVRW MAPESLKDGV
     FTTSSDMWSF GVVLWEITSL AEQPYQGLSN EQVLKFVMDG GFLDQPDNCP ERVTDLMRMC
     WQFNPKMRPT FLEIVDLLKD ELHPSFPEVS FFHSEENKVP ESEELEMEFE DMESVPLDRS
     SHAQREEAGG RDGGSALGLK RNYQEHIPYT HMNGGKKNGR ILTLPRSNPS
//
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