ID Q7KTI7_DROME Unreviewed; 1499 AA. AC Q7KTI7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 2. DT 25-OCT-2017, entry version 145. DE SubName: Full=PDGF-and VEGF-receptor related, isoform N {ECO:0000313|EMBL:AAS64657.2}; DE EC=2.7.10.- {ECO:0000313|EMBL:AAS64657.2}; DE EC=2.7.10.1 {ECO:0000313|EMBL:AAS64657.2}; GN Name=Pvr {ECO:0000313|EMBL:AAS64657.2, GN ECO:0000313|FlyBase:FBgn0032006}; GN Synonyms=8222 {ECO:0000313|EMBL:AAS64657.2}, CG8222 GN {ECO:0000313|EMBL:AAS64657.2, ECO:0000313|FlyBase:FBgn0032006}, GN CT24332 {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 stai {ECO:0000313|EMBL:AAS64657.2}, Vegf GN {ECO:0000313|EMBL:AAS64657.2}, VEGFR {ECO:0000313|EMBL:AAS64657.2}, GN Vegfr {ECO:0000313|EMBL:AAS64657.2}, VEGFR-A GN {ECO:0000313|EMBL:AAS64657.2}, Vegfr-b {ECO:0000313|EMBL:AAS64657.2}, GN Vegfr-c {ECO:0000313|EMBL:AAS64657.2}, VGR1 GN {ECO:0000313|EMBL:AAS64657.2}, Vgr1 {ECO:0000313|EMBL:AAS64657.2}, GN vgr1 {ECO:0000313|EMBL:AAS64657.2}; GN ORFNames=Dmel_CG8222 {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:RESEARCH0084.1-RESEARCH0084.20(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 -!- 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 UniGene; Dm.4698; -. DR PaxDb; Q7KTI7; -. 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; ENSGT00760000118923; -. DR OrthoDB; EOG091G01TL; -. DR Reactome; R-DME-1257604; PIP3 activates AKT signaling. DR Reactome; R-DME-1433557; Signaling by SCF-KIT. DR Reactome; R-DME-1433559; Regulation of KIT signaling. DR Reactome; R-DME-3928663; EPHA-mediated growth cone collapse. DR Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-DME-5673001; RAF/MAP kinase cascade. DR Reactome; R-DME-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR GenomeRNAi; 34127; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0032006; -. DR ExpressionAtlas; Q7KTI7; differential. DR Genevisible; Q7KTI7; DM. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004713; F:protein tyrosine kinase activity; NAS:FlyBase. DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:FlyBase. DR GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; ISS:FlyBase. DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase. DR GO; GO:0061327; P:anterior Malpighian tubule development; IMP:FlyBase. DR GO; GO:0019730; P:antimicrobial humoral response; IMP:FlyBase. DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase. DR GO; GO:0030031; P:cell projection assembly; IMP:FlyBase. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase. DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:FlyBase. DR GO; GO:0007516; P:hemocyte development; IMP:FlyBase. DR GO; GO:0035099; P:hemocyte migration; IMP:FlyBase. DR GO; GO:0035172; P:hemocyte proliferation; TAS: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:0043066; P:negative regulation of apoptotic process; IMP:FlyBase. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:FlyBase. DR GO; GO:0006468; P:protein phosphorylation; NAS:FlyBase. DR GO; GO:0045610; P:regulation of hemocyte differentiation; IMP:FlyBase. DR GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase. DR GO; GO:0038202; P:TORC1 signaling; IMP:FlyBase. 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; -; 7. 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. 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; 5. DR SUPFAM; SSF56112; SSF56112; 2. 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:SAAS00708816}; KW Complete proteome {ECO:0000313|Proteomes:UP000000803}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00803457}; KW Immunoglobulin domain {ECO:0000256|SAAS:SAAS00941986}; KW Kinase {ECO:0000256|SAAS:SAAS00708717}; KW Membrane {ECO:0000256|SAAS:SAAS00602125, ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00708656}; 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:SAAS00457685}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transferase {ECO:0000256|SAAS:SAAS00708727, 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 {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}. 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 //