ID B4II96_DROSE Unreviewed; 1088 AA.
AC B4II96;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=GM23175 {ECO:0000313|EMBL:EDW49640.1};
GN Name=Dsec\GM23175 {ECO:0000313|EMBL:EDW49640.1};
GN ORFNames=Dsec_GM23175 {ECO:0000313|EMBL:EDW49640.1};
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN [1] {ECO:0000313|EMBL:EDW49640.1, ECO:0000313|Proteomes:UP000001292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25
RC {ECO:0000313|Proteomes:UP000001292};
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; CH480842; EDW49640.1; -; Genomic_DNA.
DR RefSeq; XP_002043456.1; XM_002043420.1.
DR AlphaFoldDB; B4II96; -.
DR STRING; 7238.B4II96; -.
DR EnsemblMetazoa; FBtr0206160; FBpp0204652; FBgn0178042.
DR GeneID; 6619237; -.
DR KEGG; dse:6619237; -.
DR HOGENOM; CLU_002191_1_3_1; -.
DR OMA; KGCKQHV; -.
DR OrthoDB; 10350at2759; -.
DR PhylomeDB; B4II96; -.
DR Proteomes; UP000001292; 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: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:UniProtKB-UniRule.
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:0042127; P:regulation of cell population proliferation; 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; cd08693; C2_PI3K_class_I_beta_delta; 1.
DR CDD; cd00872; PI3Ka_I; 1.
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:UP000001292};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 41..129
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 214..304
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 344..512
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 544..721
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 788..1071
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1088 AA; 126945 MW; E17DEB348B9DE132 CRC64;
MNMMDNRALA YVAHQPKYET PPEEAEPPCM RFSVNLWKNE MLNWVDLICL LPNGFLIELR
VNPANTIQVI KVEMVNQAKQ MPLGYVIKEA CEYQVYGIST FNIEPYTDET KRLSEVQPYF
GILSLGERTD TTSFSSDYEL TKMVNGMIGT TFDHNRTHGS PEIDDFRLYM TQTCDNIELE
RSVYTWQQRL LYEHPLRLAN STKMPELIRE RHPTRTFLIV VKNENDQSTF TLSVNEQDTP
FSLTESTLQK MNRSQMKMND RTSDYILKVS GRDEYLLGDY PLIQFLYIQE MLSDSAVPNV
VLQSVYRLES YINHHNEQAM VTKRLPPKKQ TVHPQKAISS LWDMGNYFQL TLHSISNVNF
DKTRALKVGV HVCLYHGDKK LCAQRSTDSP NGNFDTFLFN DLVMDFDIQM RNLPRMTRLC
IVIFEVTKMS RSKKSSNNKD IALKDVPYNK NPLAWVNTTI FDHKDILRTG RHTLYTWTYA
DDIQSVEVFH PLGTIEPNPR KEECALVDLT FHSSGTGTVR YPSEEVVLQY AAEREQTNRL
QRQLAGPEKP IKELKDLVAN YTGLDKIYEM VDQDRNAIWE RRNDILREIP EELSILLHCV
YWKERDDVAD MWYLLKQWPL ISIERSLELL DYAYPDPAVR RFAIRCLHFL KDEDLLLYLL
QLVQAIKHES YLESDLVVFL LERALRNQRI GHYFFWHLRS EMQTPSMQTR FGLLLEVYLK
GCKHHVAPLR KQLHVLEKLK QGSLIAKKGS KEKVKTMLQD FLRDQRNSGV FQNIQNPLNP
SFRCSGVTPD RCKVMDSKMR PLWVVFENAD VNASDVHIIF KNGDDLRQDM LTLQMLRVMD
QLWKRDGMDF RMNIYNCISM EKSLGMIEVV RHAETIANIQ KEKGMFSATS PFKKGSLLSW
LKEHNKPADK LNKAINEFTL SCAGYCVATY VLGVADRHSD NIMVKRNGQL FHIDFGHILG
HFKEKLGVRR ERVPFVLTHD FVYVINKGFN DRESKEFCHF QELCERAFLV LRKHGCLILS
LFSMMISTGL PELSSEKDLD YLRETLVLDY TEEKAREHFR AKFSEALANS WKTSLNWASH
NFSKNNKQ
//
