GenomeNet

Database: UniProt/TrEMBL
Entry: B4LWM3_DROVI
LinkDB: B4LWM3_DROVI
Original site: B4LWM3_DROVI 
ID   B4LWM3_DROVI            Unreviewed;      1076 AA.
AC   B4LWM3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDW67688.1};
DE            EC=2.7.1.- {ECO:0000313|EMBL:EDW67688.1, ECO:0000313|EMBL:KRF83413.1};
DE   SubName: Full=Uncharacterized protein, isoform B {ECO:0000313|EMBL:KRF83413.1};
DE   SubName: Full=Uncharacterized protein, isoform C {ECO:0000313|EMBL:KRF83414.1};
GN   Name=Dvir\GJ24290 {ECO:0000313|EMBL:EDW67688.1};
GN   ORFNames=Dvir_GJ24290 {ECO:0000313|EMBL:EDW67688.1};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW67688.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW67688.1, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW67688.1}, and Tucson
RC   15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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:EDW67688.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW67688.1};
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:EDW67688.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=TSC#15010-1051.87 {ECO:0000313|EMBL:EDW67688.1};
RG   FlyBase;
RL   Submitted (JUN-2008) 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; CH940650; EDW67688.1; -; Genomic_DNA.
DR   EMBL; CH940650; KRF83413.1; -; Genomic_DNA.
DR   EMBL; CH940650; KRF83414.1; -; Genomic_DNA.
DR   RefSeq; XP_002054168.1; XM_002054132.2.
DR   RefSeq; XP_015027598.1; XM_015172112.1.
DR   RefSeq; XP_015027599.1; XM_015172113.1.
DR   AlphaFoldDB; B4LWM3; -.
DR   SMR; B4LWM3; -.
DR   STRING; 7244.B4LWM3; -.
DR   EnsemblMetazoa; FBtr0240215; FBpp0238707; FBgn0211370.
DR   EnsemblMetazoa; FBtr0438903; FBpp0395617; FBgn0211370.
DR   EnsemblMetazoa; FBtr0444918; FBpp0401219; FBgn0211370.
DR   GeneID; 6629966; -.
DR   KEGG; dvi:6629966; -.
DR   eggNOG; KOG0904; Eukaryota.
DR   HOGENOM; CLU_002191_1_3_1; -.
DR   InParanoid; B4LWM3; -.
DR   OMA; KGCKQHV; -.
DR   OrthoDB; 10350at2759; -.
DR   Proteomes; UP000008792; 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; 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:UP000008792};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDW67688.1}.
FT   DOMAIN          25..113
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          198..288
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          331..499
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          532..709
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          776..1059
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1076 AA;  124905 MW;  EF9CB6B427E3B476 CRC64;
     MADMTFSKDK YMCSRFAIDL WKYDPPDVVH LTCLMPNGLM LYLVAKSTAT IREVKVEMVT
     QAKCGPLGYL IKDACDYLVY GISHYTIEPY TDETKRLFEV QPYFGLLSLG ERTDTTTFSS
     DYELTKMVTD IIGKSFDHQN TQGTPEVDHF RTKVALICDN IKIERSKYSW QQRLLYEHPL
     RLANSTTMPE LIRQRHPSSA FLIAVKNEND QSTFTLSVVE NDTPLSLIDS TLQKMNRSQM
     KMNDRAADYI LKVSGRDEYL FGDHPLIQFL YIQEALSDAA VPNVVLQSVL RLESYINHYS
     EQSLGLKSPP KPDRQTTATL HKPITMLWDL EEVNFTLTLH GVTNVNFDRA RAFKVGVHVG
     LYHGKRKLCA QRSVDASSCG SSQDFQFDDN VMEFDIQMRN LPRMTRLCIV VFEVTKMSRS
     KKSSNNSSTL KDVFYNNNPL AWVNTTLFDY KNQLRKGRQT LYTWTYADDI QSDDVFYPLG
     TVESNPRKDG CAMVHLTFHQ GANDSSNEDV CYPSEEEVLQ YAEDRANRDK QQPIADPEKT
     LLGVLLANYS GKDKIYEMVD QDRNTIWERK NDILREFPED LPVLLHCVYW KDRDDVADIW
     YLLKQWPLIS IERSLELLDY AFPDPAVRGF AIKCLHNLKD EDLLLYLLQL VQAIRHESYL
     ENDLVIFLLE RALRNQRIGH YFFWHLRSEM QTPCMQTRFG LLLEAYLKGC KQHVKPLRKQ
     LEVLEKLKQG SVIAKKGSKE KVRNVLQKFL RNEHNNGVFQ NIQNPLNPSF RCSRVTPDKC
     KVMDSKMRPL WVVFENVDQT ANDVYIIFKN GDDLRQDMLT LQMLRVMDQL WKREGLDLRM
     NIYNCISMEQ RLGMIEVVRH SETIANIQKE KGMFSATSPF KKGSLYSWLK EHNKAPEKLN
     KAINEFTLSC AGYCVATYVL GVADRHSDNI MVKRNGQLFH IDFGHILGHF KEKFGVRRER
     VPFVLTHDFV YVINKGCIDR EAKEFCYFQT LCERAFLILR KHGCLILSLF SMMISTGLPE
     LSSEKDLNYL RETLVLDYTE ENARKHFQAK FSEALANSWK TSLNWASHNF SKNNKQ
//
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