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Database: UniProt
Entry: A0A0L7R7T2_9HYME
LinkDB: A0A0L7R7T2_9HYME
Original site: A0A0L7R7T2_9HYME 
ID   A0A0L7R7T2_9HYME        Unreviewed;      2495 AA.
AC   A0A0L7R7T2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Tyrosine-protein kinase receptor {ECO:0000256|RuleBase:RU000312};
DE            EC=2.7.10.1 {ECO:0000256|RuleBase:RU000312};
GN   ORFNames=WH47_12364 {ECO:0000313|EMBL:KOC66937.1};
OS   Habropoda laboriosa.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Habropoda.
OX   NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC66937.1, ECO:0000313|Proteomes:UP000053825};
RN   [1] {ECO:0000313|EMBL:KOC66937.1, ECO:0000313|Proteomes:UP000053825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0110345459 {ECO:0000313|EMBL:KOC66937.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Habropoda laboriosa.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; KQ414637; KOC66937.1; -; Genomic_DNA.
DR   STRING; 597456.A0A0L7R7T2; -.
DR   Proteomes; UP000053825; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0022008; P:neurogenesis; IEA:UniProt.
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; 7.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR   PANTHER; PTHR24416:SF527; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ROS; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF00041; fn3; 5.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00135; LY; 5.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 5.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF63825; YWTD domain; 3.
DR   PROSITE; PS50853; FN3; 7.
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|PROSITE-ProRule:PRU10141};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kinase {ECO:0000313|EMBL:KOC66937.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|RuleBase:RU000312};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000312};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW   Transferase {ECO:0000313|EMBL:KOC66937.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000312};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1809..1832
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..118
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          124..216
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          501..600
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          989..1089
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1493..1596
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1597..1693
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1697..1798
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1893..2162
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          2195..2219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2266..2345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2363..2410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2266..2282
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2283..2317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2318..2345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2363..2383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2384..2410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1926
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   2495 AA;  280834 MW;  7971A0ECD42C5CA2 CRC64;
     MDVIFVSIIP AEIGIPPAPA LVADSLTATS LRLEWKGIDI ERRGGGISYL VQWRYEELAE
     TWQYCRNQSW GEDDQILVEN LQPYTKYRFR VALLLKSSQH NPEPIVSAPS VVIRTLAAGL
     PTSAPVIVRA VAVDSCRASV SWEPGPFPNG PLLSYVLRLQ GADHSQLKDI AASENTDHYM
     FQNLEPNKNY SISVTMRNGV GEGPPAVTHV VTTPEPAVKD TQQPILILGG QHVVMKQDAD
     MLDDPSVVYE NTSIIKGVAI HVASAQLFIS DSLGYVYRTS ITKRTKPMVI LSPSQANFKP
     LSLSVDWLNL HLYILGEVKH ATTVWQIARC NLDGRGLTVA VAGFLTRPTH IEVDPYNGYL
     FWVTRGGLYR LDLADISNGV KHEVQPYLIL EDAHLGAFTV DHTNFRLLVP HHIQNTVISV
     SLDGREVLDL RSNTQQPKFK NVVSLAMANG LFYWTNGEEV LIEGYHSGQN RYFHNAYPDR
     SNGSFVSVNV LMDASQPVPV PVNPPTGVQA VLGVERAKVS WQAPHLLGGQ GKGAWQNWSY
     ELEIKDESTG ETIHQKDIAG SSHTVHNLRE KSEYSIKAAA YTSAGRGPWS TEFRGRTLRD
     GSHASILWSA NEGLLRSDVT GENIDTLIYK ASLKEPETDY HIVDVSWYKD ILYIVGNNSA
     LYRYNITNHQ KMKMNIHSVG SVAVDWISKK LYWANPKQQI ITRANLNGSQ QEPMSILAIV
     KELMIDSLEA YLYWSTGHAV EVARLNGQDR RYYHSDEIFN GKQVMGLTLD TENRYVYWIV
     RSYESGSIVY RAPTSEKIPM THKIMPEKVS ALQHPNMQGP LCYFSEHLLW LQDDRNAVIG
     DLSGQNTAII NGITLSGLHM VAIMDPALHQ YPKNLSSETV VVLPNAVNYS SIRVEGTWRN
     FNISWDPVEN INYGTVFYEV KFADYINTNS NPEITTETSM PYNNSEQILP YSVLEVTVKA
     FTYWETAHHT RKILRSPQSI PSQPTNSRAF IEFHKEPLSE NVDIFAIFRW DQPEFTNGLI
     TGYTVMCWFK EDHVPIQFCD HKSLIPSTLL EHTVQDLLPN TTYYFQVSAH TEIGAGPYTD
     LINVSTIYEN PVPQLLVATM DAVRISDLDQ EVNYTITRHI AVEVTYMAAE NKIYWINEMQ
     ELVTSDLNGA NATKMLTLNN SALSITIDWV ARHLYWSESS YRENGGRVMK LDLTMWHDGI
     LKYENIIASS RRIVNLDILP STGSLYWIEL TKKDGGIIMQ SDLNGRAIQP FFNHIDDCSC
     PYRPSVIPVM TIDSTNYQKP VMYWISMEGH LNIADIDGCA CSLIVSAGFN KGLPPTSLTV
     DKMNIYWSNI AEDQIYFVNK KYPDDGEIKH FYLPSVRSIK ALGKSLQTYP ITNCLIPHQV
     SYNVEEVKKT ANSITVRLPQ PVPQFGCETY SLPTTLYTIY VSQCLENDPN MCEDSDRTKF
     QTYEEEYEIK DLKPFTKYRL KLALSNYYAD LESMSLEFGS GVVLRTEAGA PTAPENVTVE
     ALTPTLAVVY WMPPKILNAA AVRYEVHWRL VRLINGARQK GEQFIKGTER TTDGRFFTML
     EPWLPDQEYL VFVRAYPAHV NDVYSESPGQ VVKMYPEPNN LTLTGVSVNG LNVTWVPTIN
     LTIRYTLEYK DVAVENWQVA NDSKMVNEKL TYFIKKLQPR TLYKFRLILR YPNYKLDFVW
     PTDGRFTFQT LGDVPSAPGM PTVTKLRNSV YQLNWEPAQA HGSQITLYRV EGMKINEINE
     QIDSSENASW KLFYNGTDNY WIITGDMDDK YRFRVKARNA YGFGGWSRSS PIIDLTETTG
     GILAAQQHLG LVLGLSVPVI TIMLICFCYF LCLYRQRKED KKAVLPPLVS DVELATLREI
     PRGNFVQSNA LYASTLQNDP DDSTLPKIRR EQITLAKFLG SGAFGEVFQG NAKDLERPGV
     TPVAIKTLRK GASAQEKTEF LQEARLMSHF RHKHVLRLLG VCLDTDPPLL VLELMEAGDL
     LSYLRASRSL QTSDLHALRL QDLLAMCEDV ARGCRYLEEL HFVHRDLACR NCLVSARDRE
     NRVVKIGDFG LARDIYKNDY YRKEGEGLLP VRWMAPESLV DGVFTSQSDV WAFGVLMWEI
     TSLGQQPYPA RTNLEVLHHV RAGGRLPKPM NCPPGLHQLM LRCWSAADAR PSFKACLEHI
     VSLRSTIEDA PLSPVHAGHY LARRGVSNMA YFADENQNHN NSGNSWKSSS SEGSRDMQPF
     LQNSHNATLT LQSGEVPKYL ELLADNEDII PRENSTNGYE VPRSIHISDQ NLANTNKVGT
     NSDAKRDNLH PESTLQEQKD NPGDTKEQSE KKCDKRSSIS SLNLPERKRA SITSMTDKCN
     TLDSSKLTNP TIKAILKRDS FTSLTDQRKN KRNATERRGS EISLEGRSTS SLSSNISLAP
     PTRPSSSLIS SQNVLPLKNS VIGGDSTLND GNVTKNTLPK IQRTHSNLQN GKANIPLVIN
     SALLNLLRQT PVVEDSNNIV TYTNINTDAV RVNGS
//
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