ID B4H483_DROPE Unreviewed; 1478 AA.
AC B4H483;
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=GL20824 {ECO:0000313|EMBL:EDW31198.1};
DE Flags: Fragment;
GN Name=Dper\GL20824 {ECO:0000313|EMBL:EDW31198.1};
GN ORFNames=Dper_GL20824 {ECO:0000313|EMBL:EDW31198.1};
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:EDW31198.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658,
CC ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18374;
CC Evidence={ECO:0000256|ARBA:ARBA00029297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:12709, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC EC=2.7.1.137; Evidence={ECO:0000256|ARBA:ARBA00023985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12710;
CC Evidence={ECO:0000256|ARBA:ARBA00023985};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC ProRule:PRU00879}.
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DR EMBL; CH479208; EDW31198.1; -; Genomic_DNA.
DR RefSeq; XP_002025662.1; XM_002025626.1.
DR SMR; B4H483; -.
DR STRING; 7234.B4H483; -.
DR EnsemblMetazoa; FBtr0186439; FBpp0184931; FBgn0158419.
DR GeneID; 6600653; -.
DR KEGG; dpe:6600653; -.
DR eggNOG; KOG0905; Eukaryota.
DR HOGENOM; CLU_002191_0_0_1; -.
DR OMA; QMAAGFR; -.
DR OrthoDB; 10350at2759; -.
DR PhylomeDB; B4H483; -.
DR Proteomes; UP000008744; Unassembled WGS sequence.
DR GO; GO:0010008; C:endosome membrane; IEA:EnsemblMetazoa.
DR GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:EnsemblMetazoa.
DR GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0017124; F:SH3 domain binding; IEA:EnsemblMetazoa.
DR GO; GO:0031267; F:small GTPase binding; IEA:EnsemblMetazoa.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:EnsemblMetazoa.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04012; C2A_PI3K_class_II; 1.
DR CDD; cd08381; C2B_PI3K_class_II; 1.
DR CDD; cd00869; PI3Ka_II; 1.
DR CDD; cd05166; PI3Kc_II; 1.
DR CDD; cd06884; PX_PI3K_C2_68D; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
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 Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000008; C2_dom.
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; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048:SF14; LD28067P; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF00792; PI3K_C2; 1.
DR Pfam; PF00794; PI3K_rbd; 1.
DR Pfam; PF00613; PI3Ka; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00142; PI3K_C2; 1.
DR SMART; SM00144; PI3K_rbd; 1.
DR SMART; SM00145; PI3Ka; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS51547; C2_PI3K; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51546; PI3K_RBD; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000008744};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 154..262
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 450..622
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 630..808
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 897..1172
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1210..1326
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1350..1469
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 37..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EDW31198.1"
SQ SEQUENCE 1478 AA; 166905 MW; 0025A00BCB2797B0 CRC64;
CTSTCLIGWR QDYLASRRLS AASLCQAEAP VEERLRLSEN GSGSVSPPPP LPPRNQQLYE
SAQVQAALTA SKPYQPTALT DSYTSSIPAR VVLDRRKTCT RLYELISDQR TDDPELLEFY
HMVKQLRSRY PHDDAPTNVG HVVAAEFNYH YMMDTSIKVI VHPALNTLQQ HALSTSAAAA
EGQVKGYGTP VTFTCDIDSV VAQVVAQALA SLEGQVKGSV TDYVVKPIGL LEWLAPTSRL
SQLESVHNSF QLEKDVHLGL CLSTASNMQA IARSERDDVN DADLQPEQLF PNEVVPIVTY
DNMMILIETL EMEIDKLESA ADPPPPASGR SVVSCSGVVQ AVKAICALLG SIDTLDIARC
VSDLKRVCED AQTKYAAGSG ASNPEIVSDY GDYAQVTMRP RSLLEQIKVK CNILRDAVQE
LVELYANVFR VAFSVKSLDY ATTPIPISCV SKPIVVSINC LHRPPPNWKY DDYSLCVQLV
YGTRLLSKPN VLSCSNDTSG GLFPRLNFSA WLTFEQHPIC TLPREARVTF VLYGKQAASE
NEPNSEPNGE RRQVTTELGW CSIQLFDFKR AMICGPYLLS VWPPTTDKML GPAPARGCHP
HPDFCPVLSI EVPPYGGRIE FPEHQEVPKP APHYDFASLD ANLQEELLDT AELGYTGATE
RREVFWEKRL YLQNYPNALP KVLHAAHSWD YANLIDLHAL LHSWAPLSPL QALELLLPRY
PDAKVREKAV EWISKMPNDQ LVDFLPQLVQ SLKHDTYEGS AMARFLLAKC LESPRFAHHM
YWLLVHSLPD DPHNSIGAAM VDQEYDECQI TQARYYRRSK MMLRALMAIC GEKMLQRFMY
QHRMCQKLTT IAESVKESKE SMRQKSLAAG MDEVHQDLLD KPTCLPLGPE LEVTGVAVRN
CSYFNSNTLP LKITFVGPDA ESLPAIFKCG DDLQQDQLTI QLIRIMNKMW LAERLDLKMV
TFNCVPTGYK SGMIELVSEA ETLRKIQVEC GLTGSFKDRP IAEWLGKQNP SPLEYQSAVR
NFTLSCAGYS VATYVLGICD RHNDNIMLKT SGHLFHIDFG KFLGDAQMFG NFKRDRTPFV
LTSDMAYVIN GGDKPSTDFH YFVDLCCRAF NIVRKNADLL LHTLAHMATA GMPGVNSNAV
TYVRRALLPS QSNPEAAATF AKMIQSSLKS WFTQFNFFLH NLAQMRFTAD EGTGELLSFV
PRKYTMQQDG RLKIVKVVRF QKHYSMEKFY MYILQVTRHG QPDPTHLFRS YREFTEFHQK
LCMHFPLVKL HSLPAGVHVG RSNIKSVAEK RLPLIQLFLK SLFDAAEEIA HSDLVYTFFH
PLLRDQQEAK LEMPKMKEDK RKPSRDNPNE IGQIRLSLQY QRGVLTVMIH HAKGLPMIQG
GQEPNTYVKC YLKPDPKKET KRKTKVVRKT CVPSFMETLE YRMPLNIIQE RRLQVTIWTH
DTLQENELLG GFELDLSKHD LRQELCDWHR LGSVPRNG
//
