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Database: UniProt/TrEMBL
Entry: B4GZD0_DROPE
LinkDB: B4GZD0_DROPE
Original site: B4GZD0_DROPE 
ID   B4GZD0_DROPE            Unreviewed;      1103 AA.
AC   B4GZD0;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 110.
DE   SubName: Full=GL27142 {ECO:0000313|EMBL:EDW28148.1};
GN   Name=Dper\GL27142 {ECO:0000313|EMBL:EDW28148.1};
GN   ORFNames=Dper_GL27142 {ECO:0000313|EMBL:EDW28148.1};
OS   Drosophila persimilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744};
RN   [1] {ECO:0000313|EMBL:EDW28148.1, ECO:0000313|Proteomes:UP000008744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSH-3 / Tucson 14011-0111.49
RC   {ECO:0000313|Proteomes:UP000008744};
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   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00879}.
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DR   EMBL; CH479198; EDW28148.1; -; Genomic_DNA.
DR   RefSeq; XP_002023945.1; XM_002023909.1.
DR   AlphaFoldDB; B4GZD0; -.
DR   SMR; B4GZD0; -.
DR   STRING; 7234.B4GZD0; -.
DR   EnsemblMetazoa; FBtr0192757; FBpp0191249; FBgn0164723.
DR   GeneID; 6598691; -.
DR   KEGG; dpe:6598691; -.
DR   eggNOG; KOG0904; Eukaryota.
DR   HOGENOM; CLU_002191_1_3_1; -.
DR   OMA; CVEWNDH; -.
DR   OrthoDB; 10350at2759; -.
DR   PhylomeDB; B4GZD0; -.
DR   Proteomes; UP000008744; Unassembled WGS sequence.
DR   GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; IEA:EnsemblMetazoa.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0046934; F:1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:EnsemblMetazoa.
DR   GO; GO:0035212; P:cell competition in a multicellular organism; IEA:EnsemblMetazoa.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:EnsemblMetazoa.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0055115; P:entry into diapause; IEA:EnsemblMetazoa.
DR   GO; GO:0036099; P:female germ-line stem cell population maintenance; IEA:EnsemblMetazoa.
DR   GO; GO:0030707; P:follicle cell of egg chamber development; IEA:EnsemblMetazoa.
DR   GO; GO:0042593; P:glucose homeostasis; IEA:EnsemblMetazoa.
DR   GO; GO:0035099; P:hemocyte migration; IEA:EnsemblMetazoa.
DR   GO; GO:0002168; P:instar larval development; IEA:EnsemblMetazoa.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IEA:EnsemblMetazoa.
DR   GO; GO:0036335; P:intestinal stem cell homeostasis; IEA:EnsemblMetazoa.
DR   GO; GO:0030536; P:larval feeding behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0055088; P:lipid homeostasis; IEA:EnsemblMetazoa.
DR   GO; GO:0048542; P:lymph gland development; IEA:EnsemblMetazoa.
DR   GO; GO:0007552; P:metamorphosis; IEA:EnsemblMetazoa.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:EnsemblMetazoa.
DR   GO; GO:0010507; P:negative regulation of autophagy; IEA:EnsemblMetazoa.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IEA:EnsemblMetazoa.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:1903688; P:positive regulation of border follicle cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0030307; P:positive regulation of cell growth; IEA:EnsemblMetazoa.
DR   GO; GO:0045793; P:positive regulation of cell size; IEA:EnsemblMetazoa.
DR   GO; GO:0042691; P:positive regulation of crystal cell differentiation; IEA:EnsemblMetazoa.
DR   GO; GO:0045572; P:positive regulation of imaginal disc growth; IEA:EnsemblMetazoa.
DR   GO; GO:0035205; P:positive regulation of lamellocyte differentiation; IEA:EnsemblMetazoa.
DR   GO; GO:0010884; P:positive regulation of lipid storage; IEA:EnsemblMetazoa.
DR   GO; GO:1904801; P:positive regulation of neuron remodeling; IEA:EnsemblMetazoa.
DR   GO; GO:0046622; P:positive regulation of organ growth; IEA:EnsemblMetazoa.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:EnsemblMetazoa.
DR   GO; GO:0045615; P:positive regulation of plasmatocyte differentiation; IEA:EnsemblMetazoa.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:EnsemblMetazoa.
DR   GO; GO:0050773; P:regulation of dendrite development; IEA:EnsemblMetazoa.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:EnsemblMetazoa.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:EnsemblMetazoa.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:EnsemblMetazoa.
DR   GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IEA:EnsemblMetazoa.
DR   GO; GO:0051823; P:regulation of synapse structural plasticity; IEA:EnsemblMetazoa.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblMetazoa.
DR   GO; GO:0060074; P:synapse maturation; IEA:EnsemblMetazoa.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:EnsemblMetazoa.
DR   CDD; cd05165; PI3Kc_I; 1.
DR   Gene3D; 3.10.20.770; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR002420; PI3K-type_C2_dom.
DR   InterPro; IPR003113; PI3K_ABD.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   PANTHER; PTHR10048:SF118; PI-3 KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF02192; PI3K_p85B; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00143; PI3K_p85B; 1.
DR   SMART; SM00144; PI3K_rbd; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS51547; C2_PI3K; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51544; PI3K_ABD; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008744};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          54..142
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          227..317
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          357..525
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          559..736
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          803..1086
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1103 AA;  127822 MW;  57F8A3189F2FD8BF CRC64;
     MNRTASVSHN YAACLLDNRQ ASYADLTYPG CDMPPTEYAP SDMRFSINLW KNDPPDYVDL
     ICMIPNGTLL MMKAPSSTTI REIKVEVVKM AKQNCLGYMI KDACDYQFYG ISVFNIEPYT
     DETKRLCEVQ PHFGLLSLGD RTDATSFSSD YELTKMVSGM IGNSFDHHRT QGTPEIDDFR
     RSMTDLCESI EVERSQFTWQ QRLLYEHPLR LAGSVDMPEL IRQRHPTSAF LIVVKNENDQ
     STFTLSVMEK DTPFSLIEST LQKMNRSQMK MNDRAGDYIL KVSGRDEYLF GDHPLIQFLY
     IQEALSDSAV PNVVLQSVIR MESYINHHNE QSMGLKRAPK KDRSVVLHKA PTSLWDLGNY
     FQLTLHSISN VNYDKTRAFR VGVDVGLYHG EHKLCSQRSI DAPNGSSDTF LFNDQIMDFD
     IQMRNLPRMT RLCIVIFEVT KLSRSKKSSN NKDNAQKDVS YNKNPLAWVN TTLLDYKAHL
     RTGRQVLYTW TYADDIQSDE VFHPLGTIEP NPRKEECALV HVTFHSSGAE SVRYPCENTV
     LQYAADRALA SLREKQQQPA EPEKPLKDLK ELVANYTGLD KIYEMVDQDR NAIWERRNDV
     LRELPEQLPI LLHCVYWKER DDVADIWYLL KRWPLISVER SLELLDYAYP DPAVRRFAIK
     CLQILKDDDL LLYLLQLVQA IKHESYLESD LVVLLLERAL RNQRIGHYFF WHLRSEMQTP
     SMQTRFGLLL EVYLKGCKHH VAPLRKQLQV LDKLKQVSVL AKKGSKEKVK TMLQDFLRDQ
     RNTGVFQNIQ NPLNPSFRCS GVSPDQCKVM DSKMRPLWVV FENADLNSND VYIIFKNGDD
     LRQDMLTLQM LRVMDKLWKR DGMDFRMNIY NCISMEQRLG MIEVVRHAET IANIQKEKGM
     FSATSPFKKG SLYSWLKEHN KPADKLNKAI NEFTLSCAGY CVATYVLGVA DRHSDNIMVK
     RNGQLFHIDF GHILGHFKEK FGVRRERVPF VLTHDFVYVI NKGCNDREAK EFCHFQELCE
     HAFLTLRKHG CLILSLFSMM ISTGLPELSS EKDLNYLRDT LVLDYTEEKA REHFRAKFSE
     ALANSWKTSL NWASHNFSKN NKQ
//
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