ID A0A0Q9WN23_DROVI Unreviewed; 1509 AA.
AC A0A0Q9WN23;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
GN Name=Dvir\GJ20603 {ECO:0000313|EMBL:KRF81861.1};
GN ORFNames=Dvir_GJ20603 {ECO:0000313|EMBL:KRF81861.1};
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF81861.1, ECO:0000313|Proteomes:UP000008792};
RN [1] {ECO:0000313|EMBL:KRF81861.1, ECO:0000313|Proteomes:UP000008792}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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};
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DR EMBL; CH940649; KRF81861.1; -; Genomic_DNA.
DR RefSeq; XP_015028632.1; XM_015173146.1.
DR EnsemblMetazoa; FBtr0443284; FBpp0399693; FBgn0207742.
DR GeneID; 6628383; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000008792; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProt.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0022008; P:neurogenesis; IEA:UniProt.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 PANTHER; PTHR24416:SF600; PDGF-AND VEGF-RECEPTOR RELATED, ISOFORM J; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000615; TyrPK_CSF1-R; 3.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000615-3};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000615-3};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1509
FT /note="receptor protein-tyrosine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006386935"
FT TRANSMEM 788..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 259..352
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 465..569
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 583..679
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 688..778
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 863..1268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1019..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1123
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-1"
FT BINDING 897
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT BINDING 1128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
FT BINDING 1141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000615-3"
SQ SEQUENCE 1509 AA; 170108 MW; FB6F6536E867B4A5 CRC64;
MRKLLYVLFG LIGISIFDRL EALPRPQNDF EDNDILYNCG GEMGVPLITP CKDSLKLDAG
TSYTLQCEAS EPIDWWHGHY GHKLSETFDN IGDPQRPYGI RLTLDEVSVE NVGAYYCIKS
SLGLDPNNWT EETLIELVNN NEASTIYVFV NDKSNLLAPL EPIIQARQYS EVIIPCKPAM
PETEVLLTFN SDTFSSETAA RYDPKRGFVI EIRSVTDGGE YYCEPKIPSP DNEEESTIIV
VRFIGNGHID KATDRLNKPI INSTSRGHVY EGQTFQLVCE LSAPYGVSYD MHWVVPDKVD
KFRYNYTEAL FDERAKNTTH RVGRSKLTVT DARLTDKGAY KCVVSDSFRN MEYASYRMHV
MQPNSSYLKV SEPSNHYTVH EHVNRTIQMT ANFEGFPQPT FKWYKPNGIE VWDTEQNFQI
LATETSTTLK ILNAQLEDSG SYVLKGTNGI DVKQLSFNVS VISGPVLSMG DVYVVAGQEA
HLNCSVKSFP QAVVTFLFKP CSLKPRWPSC ELASQNFSSE TVQEEYQYKT NTRPGLLSVE
SIHEAIFTPD KPGIIICVAQ NQIDNKLVTS QTRAHVLLGT IAENISISGM DPNRKIAKGD
QESFTCAALA YHFDGNLEWY LDGELISEGP DVELETNSTE YSYTKTLKFH AIADKDRGTY
ECRARYINDP DKYDSREITV YVHDPKAPQW SYTNLNAKSK IERNLGDSLI LECKSKAVPQ
AKVSWYKDDV ELFETNRTHL VEDGTKLLIP HLYPKHDGIY RCVVANRLGS IENSVTVVIA
NIPGVSKLWI WVGAIFFGVL IALCAFLAVR YREERKNHLA LKSAGLANFE EGDVAQINPA
LSLDEQAELL PYNREFEFPR DKLKLGKQLG AGAFGVVLKG EAEGIRSDEP VSTVAVKMVK
RTADAEVVRA LVSELKIMVH LGQHLNVVNL LGAVTKNIAK RELMVIVEYC RFGNIQNFLL
RNRKCFINQI NPINDRIDPS IMTQRISDNF DLHRDVGGGL KYVNVGFPNH PYINHVNNNY
THTHRRNSDN DPRSGTRAGR TVTGGSTYDR QLDTCATEAT VMTTVPEDEH IMSNNSIQPA
WRSNYKTDST EAMTVTTIDL VSWAFQVARG MYYLSSKKVL HGDLAARNIL LCEDNVVKIC
DFGLARSMYR GDNYKKSESG KLPIKWLALE SLSDHVFSTY SDVWSFGIVL WEFFSLSKVP
YPGIDPNQEL FNKLNDGYRM EKPPYANQEL YEIMLECWRK SPESRPLFHV LERRLANMLG
EDVANHYLDL NDPYMRSNTE YMKNRPTDYL SLMGSPDEFA PAAPRYVNGH IVPDIRIEAS
PDDYLQMNAE NNTAIFSPTR PKGDANQSTE FADLPAIETN ETSFTFPDTR TVVGQHSPTL
ANNMDSSAHK PLRRKNGMPT VDAADQAPEE IPMLHRTSTS DGERSPEQAR RFPQALKQQY
VTPTPSPRHH IETTLNGSGE NYVNVKPPRK NLVNKSAPGG NSSSSSTDAF SNPSYQPLTV
VNEKQERRY
//
