ID Q7KTI7_DROME Unreviewed; 1499 AA. AC Q7KTI7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 2. DT 31-JUL-2019, entry version 162. DE RecName: Full=Receptor protein-tyrosine kinase {ECO:0000256|SAAS:SAAS00293071}; DE EC=2.7.10.1 {ECO:0000256|SAAS:SAAS00293071}; GN Name=Pvr {ECO:0000313|EMBL:AAS64657.2, GN ECO:0000313|FlyBase:FBgn0032006}; GN Synonyms=8222 {ECO:0000313|EMBL:AAS64657.2}, CT24332 GN {ECO:0000313|EMBL:AAS64657.2}, Dmel\CG8222 GN {ECO:0000313|EMBL:AAS64657.2}, DmVEGFR {ECO:0000313|EMBL:AAS64657.2}, GN PVR {ECO:0000313|EMBL:AAS64657.2}, PvR {ECO:0000313|EMBL:AAS64657.2}, GN pvr {ECO:0000313|EMBL:AAS64657.2}, stai {ECO:0000313|EMBL:AAS64657.2}, GN Vegf {ECO:0000313|EMBL:AAS64657.2}, VEGFR GN {ECO:0000313|EMBL:AAS64657.2}, Vegfr {ECO:0000313|EMBL:AAS64657.2}, GN VEGFR-A {ECO:0000313|EMBL:AAS64657.2}, Vegfr-b GN {ECO:0000313|EMBL:AAS64657.2}, Vegfr-c {ECO:0000313|EMBL:AAS64657.2}, GN VGR1 {ECO:0000313|EMBL:AAS64657.2}, Vgr1 GN {ECO:0000313|EMBL:AAS64657.2}, vgr1 {ECO:0000313|EMBL:AAS64657.2}; GN ORFNames=CG8222 {ECO:0000313|EMBL:AAS64657.2, GN ECO:0000313|FlyBase:FBgn0032006}, Dmel_CG8222 GN {ECO:0000313|EMBL:AAS64657.2}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803}; RN [1] {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.H., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., RA Abril J.F., Agbayani A., An H.J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., WoodageT, Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., RA Yeh R.F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [2] {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537568; RA Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A., RA Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A., RA George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R., RA Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J., RA Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C., RA Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.; RT "Finishing a whole-genome shotgun: release 3 of the Drosophila RT melanogaster euchromatic genome sequence."; RL Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002). RN [3] {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803} RP GENOME REANNOTATION. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfied E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537573; RA Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., RA Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., RA Ashburner M., Celniker S.E.; RT "The transposable elements of the Drosophila melanogaster euchromatin: RT a genomics perspective."; RL Genome Biol. 3:RESEARCH0084-RESEARCH0084(2002). RN [5] {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=12537574; RA Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., RA Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., RA Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., RA Karpen G.H.; RT "Heterochromatic sequences in a Drosophila whole-genome shotgun RT assembly."; RL Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002). RN [6] {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=16110336; DOI=10.1371/journal.pcbi.0010022; RA Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., RA Ashburner M., Anxolabehere D.; RT "Combined evidence annotation of transposable elements in genome RT sequences."; RL PLoS Comput. Biol. 1:166-175(2005). RN [7] {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569856; DOI=10.1126/science.1139815; RA Smith C.D., Shu S., Mungall C.J., Karpen G.H.; RT "The Release 5.1 annotation of Drosophila melanogaster RT heterochromatin."; RL Science 316:1586-1591(2007). RN [8] {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|Proteomes:UP000000803} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803}; RX PubMed=17569867; DOI=10.1126/science.1139816; RA Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M., RA Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A., RA Dimitri P., Karpen G.H., Celniker S.E.; RT "Sequence finishing and mapping of Drosophila melanogaster RT heterochromatin."; RL Science 316:1625-1628(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L- CC tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, CC Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; CC EC=2.7.10.1; Evidence={ECO:0000256|SAAS:SAAS01173575}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. {ECO:0000256|SAAS:SAAS00602168}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE014134; AAS64657.2; -; Genomic_DNA. DR RefSeq; NP_995647.2; NM_205925.3. DR PRIDE; Q7KTI7; -. DR EnsemblMetazoa; FBtr0332417; FBpp0304690; FBgn0032006. DR GeneID; 34127; -. DR UCSC; CG8222-RF; d. melanogaster. DR CTD; 5817; -. DR FlyBase; FBgn0032006; Pvr. DR eggNOG; KOG0200; Eukaryota. DR eggNOG; COG0515; LUCA. DR GeneTree; ENSGT00940000173194; -. DR GenomeRNAi; 34127; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0032006; Expressed in 31 organ(s), highest expression level in embryonic/larval hemocyte (Drosophila). DR ExpressionAtlas; Q7KTI7; differential. DR Genevisible; Q7KTI7; DM. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:FlyBase. DR GO; GO:0038085; F:vascular endothelial growth factor binding; IBA:GO_Central. DR GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; IBA:GO_Central. DR GO; GO:0061327; P:anterior Malpighian tubule development; IMP:FlyBase. DR GO; GO:0019730; P:antimicrobial humoral response; IMP:FlyBase. DR GO; GO:0030031; P:cell projection assembly; IMP:FlyBase. DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase. DR GO; GO:0030097; P:hemopoiesis; IEP:FlyBase. DR GO; GO:0048803; P:imaginal disc-derived male genitalia morphogenesis; IMP:FlyBase. DR GO; GO:0045087; P:innate immune response; IMP:FlyBase. DR GO; GO:0036335; P:intestinal stem cell homeostasis; IMP:FlyBase. DR GO; GO:0035167; P:larval lymph gland hemopoiesis; IGI:FlyBase. DR GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase. DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISS:FlyBase. DR GO; GO:0007419; P:ventral cord development; IMP:FlyBase. DR Gene3D; 2.60.40.10; -; 6. 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; IPR013106; Ig_V-set. 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 Pfam; PF07679; I-set; 2. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 7. DR SMART; SM00408; IGc2; 4. DR SUPFAM; SSF48726; SSF48726; 4. DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level; KW ATP-binding {ECO:0000256|SAAS:SAAS00600564}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Disulfide bond {ECO:0000256|SAAS:SAAS01150976}; KW Immunoglobulin domain {ECO:0000256|SAAS:SAAS00941986}; KW Kinase {ECO:0000256|SAAS:SAAS00601152}; KW Membrane {ECO:0000256|SAAS:SAAS00602125, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00600689}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q7KTI7}; KW Receptor {ECO:0000256|SAAS:SAAS00600436, ECO:0000313|EMBL:AAS64657.2}; KW Reference proteome {ECO:0000313|Proteomes:UP000000803}; KW Repeat {ECO:0000256|SAAS:SAAS00295312}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|SAAS:SAAS00601608, KW ECO:0000313|EMBL:AAS64657.2}; KW Transmembrane {ECO:0000256|SAAS:SAAS00600943, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00602683, KW ECO:0000256|SAM:Phobius}; KW Tyrosine-protein kinase {ECO:0000256|SAAS:SAAS00293420}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 1499 Receptor protein-tyrosine kinase. FT {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004290881. FT TRANSMEM 782 803 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 260 355 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 468 566 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 577 673 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 679 772 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 857 1271 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT REGION 1008 1045 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 1341 1387 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 1427 1499 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 1008 1022 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 1031 1045 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 1346 1381 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 1477 1492 Polar. {ECO:0000256|SAM:MobiDB-lite}. SQ SEQUENCE 1499 AA; 168872 MW; 4F0DE90513697B13 CRC64; MAMLPRLILL PLLLILRISW SDAVPLQQFS PDPDDSIENC GGENGAPLMT PCKSAIILDA QTSTTLKCED DEPMSWWTSQ SQYVHVKSFD NTEDPARPFG TSLHLIEVTA DYVAAYYCVK TSKFSQIAKE EQSDEAMIEL VNQGYASSIY VYVNDPDTKL VDSHNVVTAR QYTDVVIPCK PAMPDTEVLL ETSNGEMHSS KSVGRYDPQR GFTIEIRSIV DGGDYYCRPN PPFPHNEEEM TSIEVRFIGN GHIDNGKPLP KPVIRSSVEH HVFTDTNFTL DCEQSAYVES VYGMEWFTPS RDENRIFASQ SRTDPKTRNS THQTGRSTLT VLNAQPSDTG LYKCVTTDNS NQNVQRATYR IKVLKQNESY LNVGEPSGHY NVQEYANRTI QMTANFEGFP TPSFSWFKPD GTEVRQSENN FKILSTELST MLQVLNAQLQ DSGTYVLRGS NSFGVVQREY NVSVMDAPAL KMSDAYVQVG SVARLECTVR SYPPAIVTFF FRPCSLEPQW PTCSVLNQNF SFQTRPRPGK LSVERIYEVS FLPTEPGILT CIAQNIIDGK ERRTLTKAHV LLGNISENMT IYGFDKDHKI AKEDNVNFTC EALAYHFDGN LKWFINGEDL KESDSVHIET SHTKYSYKST VHITTISDRD RGTYECRAYH NDKDAVYSSR EIDLYVHDPS APQWTNGGQE GHSKIKRKLS QTLELECAST AVPVAIVRWF KDDKEVTESK LRHIIEKESK LLITHLYPGD EGVYKCVVEN RLDRIERSFT VVISDLPGIS MAWVWFGVIL FLILIGLCVF LAVRYQKEHK RHLALKAAGL ANFEEGAVGH INPDLTLDEQ AELLPYNREF EFPRENLKLG KQLGAGAFGV VLKGEAKGIR REEPTTTVAV KMVKATADNE VVRALVSELK IMVHLGQHLN VVNLLGAVTK NIAKRELMVI VEYCRFGNIQ NFLLRNRKCF INQINPDTDH IDPSIMTQRM SDNYELHRDT NGGGLKYANV GFPIHSYINE PHNNNTQPPT HRRNSDNDPR SGTRAGRTGS GTATYSYDRQ MDTCATVMTT VPEDDQIMSN NSVQPAWRSN YKTDSTEAMT VTTVDLISWA FQVARGMDYL SSKKVLHGDL AARNILLCED NVVKICDFGL ARSMYRGDNY KKSENGKLPI KWLALESLSD HVFSTYSDVW SYGIVLWEMF SLAKVPYPGI DPNQELFNKL NDGYRMEKPK FANQELYEIM LECWRKNPES RPLFAELEKR FANMLGEDVA SHYLDLNNPY MQSNIEYMKK QSTDYLALMG SPDELAPAAP RYVNGHIVPD IRIEELPDDY MEMSRDSDPD ACTAIFSPTR LEGESSDFPD FSSETTFNFP GARQSPTLSN NLNSGSSKPL RKKNGMPTVD VADQAPEEIP MLHRSSTGSD GSPEQGRRFN QALKQQYVTP TPSPRHHVET KLNGEPSENY VNMKPPRKNI PGKTTTGGGG AAAGASTEAF SNPSYQPLST VNEKEQRRY //