ID B3M0A8_DROAN Unreviewed; 1099 AA.
AC B3M0A8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDV43114.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:EDV43114.1, ECO:0000313|EMBL:KPU80091.1};
DE SubName: Full=Uncharacterized protein, isoform B {ECO:0000313|EMBL:KPU80091.1};
GN Name=Dana\GF18327 {ECO:0000313|EMBL:EDV43114.1};
GN Synonyms=dana_GLEANR_19585 {ECO:0000313|EMBL:EDV43114.1}, Pi3K92E
GN {ECO:0000313|EMBL:EDV43114.1};
GN ORFNames=GF18327 {ECO:0000313|EMBL:EDV43114.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV43114.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV43114.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV43114.1}, and Tucson
RC 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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).
RN [2] {ECO:0000313|EMBL:EDV43114.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV43114.1};
RX PubMed=18057021; DOI=10.1093/bioinformatics/btm542;
RA Zimin A.V., Smith D.R., Sutton G., Yorke J.A.;
RT "Assembly reconciliation.";
RL Bioinformatics 24:42-45(2008).
RN [3] {ECO:0000313|EMBL:EDV43114.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV43114.1};
RG FlyBase;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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DR EMBL; CH902617; EDV43114.1; -; Genomic_DNA.
DR EMBL; CH902617; KPU80091.1; -; Genomic_DNA.
DR RefSeq; XP_001954553.1; XM_001954517.2.
DR RefSeq; XP_014766891.1; XM_014911405.1.
DR AlphaFoldDB; B3M0A8; -.
DR STRING; 7217.B3M0A8; -.
DR EnsemblMetazoa; FBtr0123027; FBpp0121519; FBgn0095345.
DR EnsemblMetazoa; FBtr0381731; FBpp0342001; FBgn0095345.
DR GeneID; 6501103; -.
DR KEGG; dan:6501103; -.
DR eggNOG; KOG0904; Eukaryota.
DR HOGENOM; CLU_002191_1_3_1; -.
DR OMA; KGCKQHV; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000007801; 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; 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:UP000007801};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDV43114.1}.
FT DOMAIN 50..138
FT /note="PI3K-ABD"
FT /evidence="ECO:0000259|PROSITE:PS51544"
FT DOMAIN 223..313
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 353..521
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 557..734
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 801..1082
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
SQ SEQUENCE 1099 AA; 127758 MW; 89E06ED398985EE4 CRC64;
MNQAFIMERP CMDSMVALDH MQLVNYQDQI DGMEQELNSR FSVDLWRNEW PEIVNLICML
PNGFLTVLTT QSTTTISDIK EKLVQIAKQM PLGFLIKKAC DYQVYGLSTF NIEPYIDETK
RICEVQPYFG LLRLSDRTDD TSFSSDYELA KLVSGMIGKS FDHHRTLGTP EIDDFRLNMT
QICDSIEMER SVYTWQQWLL YEYPLRLANS TKMPLLIRER HPTRTFLIVV KNENDPSTFT
LSVSEQDTPL SLTESSLQKM NRSQMKMYDR ASDYILKVSG RDEYLFGDYP LIQFLYIQEM
LSDTAVPNVV LQSIYRLEPY INHNNDQNMV PRRLPPKKRP AILPKTPTSL WDMGNYFQFT
LHSIGNVNYD KSRALKVGVH VGLFHGEQKL CAQRSADAPN SGSDTFLFND LVMSFDIQMR
NLPRMTRLCI VIFEVTKMSR SKKSSNNKDN SLKDVSYNKN PLAWVNTTLF DYKDNLRTGS
QTLYTWTYAD DIQSDEVFHP LGTIESNPRK EECALLHLTF HGNGTGCVRY PTEDAVLQYA
ADRAAASLRE SQLQQPQQLA EKPLKVLKDL LANYSGLDKI YEMVDQDRNA IWERRNDIMR
ELPEELSILL HCVYWKERDD VADIWYLLKQ WPLISIERSL ELLDYAYPDP AVRRFAIRCL
QYLKDEDLLL YLLQLVQAIK HESYLESDLV VFLLERALRN QRIGHYFFWH LRSEMQSPSM
QTRFGLLLEV YLKGCKHHVA PLRRQLQVLE KLKHSSVIAK KGSKEKVKSL LQDFLRDQRN
TGIFQNILNP LNPSFRCSGV SPDKCKVMDS KMRPLWVVFE NADKTSNEVS IIFKNGDDLR
QDMLTLQMLR VMDQLWKRDG MDFRMNIYNC ISMEQRLGMI EVVRDAETIA NIQKEKGMFS
ATAAFKKGSL FSWLKEHNPN SLSKAINEFT LSCAGYCVAT YVLGVADRHS DNIMVKKNGQ
LFHIDFGHIL GHFKEKFGVK RERVPFVLTH DFVYVINNGC NDREAKEFCH FQDLCERAFL
ALRKHGCLIL SLFSMMISTG LPELSSEKDL NYLRETLVLD YTEEKAREHF RGKFKEALAN
SWKTSLNWAS HNFSKNNKQ
//
