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Database: UniProt
Entry: A0A3Q2C9Y3_CYPVA
LinkDB: A0A3Q2C9Y3_CYPVA
Original site: A0A3Q2C9Y3_CYPVA 
ID   A0A3Q2C9Y3_CYPVA        Unreviewed;      1416 AA.
AC   A0A3Q2C9Y3;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000001583.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000001583.1}
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   RefSeq; XP_015234188.1; XM_015378702.1.
DR   STRING; 28743.ENSCVAP00000001583; -.
DR   Ensembl; ENSCVAT00000013181.1; ENSCVAP00000001583.1; ENSCVAG00000002588.1.
DR   GeneID; 107087242; -.
DR   CTD; 245701; -.
DR   GeneTree; ENSGT00940000156682; -.
DR   OMA; HRCWHHR; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000265020; 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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd00064; FU; 1.
DR   CDD; cd05032; PTKc_InsR_like; 1.
DR   CDD; cd00185; TNFRSF; 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; 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:SF106; INSULIN-LIKE GROWTH FACTOR 1 RECEPTOR; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00757; Furin-like; 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; 3.
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}; Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   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:UP000265020};
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..1416
FT                   /note="Tyrosine-protein kinase receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018593989"
FT   TRANSMEM        937..961
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          488..606
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          610..709
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          833..929
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1002..1275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1305..1381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1395..1416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1136
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-1"
FT   BINDING         1012
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1036
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         1083..1089
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1140..1141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
FT   BINDING         1154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000620-2"
SQ   SEQUENCE   1416 AA;  160167 MW;  A2F95BE4541EF22B CRC64;
     MNVGAGTSMG SLTLFWGLLL FVSSICVRPI HGEICSPSID IRNDISEFKR LENCTVLEGY
     LQIVLINEKT SNINQEVFRT LSFPKLTVIT DYLLLFRVPG LDSLSKLFPN LSVIRGLNLF
     FGNALVIYEM NNLKDIGLYN LMNITRGTVQ IEKNGELCYL DSVDWSLIMD SYVNNIITRN
     KEPKECDDIC PGIMEDNPIC RTTSFKDNKD YRCWTSNHCQ KVCPPQCKLA CTDKGECCHS
     QCLGGCSEPN NDMACSACIH YNHDGRCVPD CPDGTFMFEG WRCITMTECS EVHLPNDNLF
     VIHNRECMSD CPSGFKRSSN ETDRHCTACN GLCDKYCRGT VIDSVDAAQS LKECTVIEGN
     LVINIRSGIN IASELETFMG LIQTVTGYVR IRHSHSLSSL SFLKSLRYIN GQDLIDNMYS
     FSAVNNQNLQ SLWNWTQHNL TIQAGRIFFR GNPKLCMSEI HAMWEKTGIT VKPEEADYRY
     NGDRASCESD VLKFKSNITT SHTITLTWER YQVPDHGDLI SFIVYYQESP FQNITQFDGQ
     DGCGSNTWHM VDVDLPHDQN DPKFTLQHLK PWTQYAIYVK ATTLQMKDEH ISGAKSDIIY
     IRTRPSLPSM PNDPRAYANS STKLVVKWSP PVFPNGNQIY YLVRWQRQPE DREFYHHDYC
     SKDLKLPIRS PSLGPLEEKD NPNPPKVTLP GETKGLCCTC QKTAEEKERE KHDRYFLKVF
     ENFLHNTIFL PRPPDRRRRD LFGLANHTQF HDDGQGNITL GSGENSTDGI PPVNEYPFND
     DRTSAEYLEI PNLRPFTTYL IEIHACNEQL GFNCSVGAFV FSRTKPAAKA DDIPGKVIYE
     MCDNTDGCVV LHWPQPLMPN GLILMYEIKY RLGNEPEKHK CVSRRQYHEY KGFRLTILSP
     GNYSARVRAT SLAGNGSWTE SISFYVPPPK REDFATLYLV ILVPIIVTLL IASLTTVLIF
     INKKRNNNRL GNGVLYASVN PEYISAAEMY TPDEWEVARE KITMHKELGQ GSFGMVYEGT
     AKGVVKDEPE TRVAIKTVNE SASMRERIEF LNEASVMKEF NCHHVVRLLG VVSQGQPTLV
     IMELMTRGDL KSHLRSVRNE NTNSQTLPPL KKMIQMTGEI ADGMAYLNAN KFVHRDLAAR
     NCMVAEDFTV KIGDFGMTRD IYETDYYRKG GKGLLPVRWM SPESLKDGVF TTMSDVWSFG
     VVLWEITTLA EQPYQGMSNE QVLRFVMEGG LLEKPDNCPD MLFELMRMCW QYNPKMRPSF
     QEIINSIKDD LDPHFREVSF FYSEENKPPD MEELDMEVEN MENIPLDPVS TRQPPTAAVP
     PSGCMGSRSP PPSQQLSPLQ GPSTPLLGSV SHSPPGPLAT ALTSSGHGSD KHSEHALANG
     PVVVLQPNFD ELEPYAHMNG GRKNERALPL PQSSAC
//
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