ID B3M4C4_DROAN Unreviewed; 1862 AA.
AC B3M4C4;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDV39394.1};
DE EC=2.7.1.- {ECO:0000313|EMBL:EDV39394.1, ECO:0000313|EMBL:KPU78034.1};
DE SubName: Full=Uncharacterized protein, isoform D {ECO:0000313|EMBL:KPU78034.1};
DE SubName: Full=Uncharacterized protein, isoform E {ECO:0000313|EMBL:KPU78035.1};
GN Name=Dana\GF24513 {ECO:0000313|EMBL:EDV39394.1};
GN Synonyms=dana_GLEANR_9228 {ECO:0000313|EMBL:EDV39394.1};
GN ORFNames=GF24513 {ECO:0000313|EMBL:EDV39394.1};
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:EDV39394.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV39394.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV39394.1}, 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:EDV39394.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV39394.1};
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:EDV39394.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TSC#14024-0371.13 {ECO:0000313|EMBL:EDV39394.1};
RG FlyBase;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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; CH902618; EDV39394.1; -; Genomic_DNA.
DR EMBL; CH902618; KPU78034.1; -; Genomic_DNA.
DR EMBL; CH902618; KPU78035.1; -; Genomic_DNA.
DR RefSeq; XP_001956588.1; XM_001956552.2.
DR RefSeq; XP_014765079.1; XM_014909593.1.
DR RefSeq; XP_014765080.1; XM_014909594.1.
DR SMR; B3M4C4; -.
DR STRING; 7217.B3M4C4; -.
DR EnsemblMetazoa; FBtr0129213; FBpp0127705; FBgn0101507.
DR EnsemblMetazoa; FBtr0390666; FBpp0350180; FBgn0101507.
DR EnsemblMetazoa; FBtr0391311; FBpp0350768; FBgn0101507.
DR GeneID; 6507145; -.
DR KEGG; dan:6507145; -.
DR eggNOG; KOG0905; Eukaryota.
DR HOGENOM; CLU_002191_0_1_1; -.
DR OMA; QMAAGFR; -.
DR OrthoDB; 10350at2759; -.
DR Proteomes; UP000007801; 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:UP000007801};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDV39394.1}.
FT DOMAIN 546..652
FT /note="PI3K-RBD"
FT /evidence="ECO:0000259|PROSITE:PS51546"
FT DOMAIN 835..1007
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000259|PROSITE:PS51547"
FT DOMAIN 1018..1193
FT /note="PIK helical"
FT /evidence="ECO:0000259|PROSITE:PS51545"
FT DOMAIN 1282..1557
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 1595..1711
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 1735..1854
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 36..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1862 AA; 208951 MW; 84E7739FFCAE6C13 CRC64;
MSNQAQIDYD KQFQDDLAKA TALSLEQQAL DDYRRHKKYG TGYRPSSSTA TPAAASAREY
HVAQRSQSVN QGRRHSEVHP TLAAPVSLER SRTPPAQGTD NDLICFASPT SKQPENDSPF
GRLIEDLQRI QTTNPQSAMV PVGPVAAASV PAPYGFVPPS PHVQPPPYGM VGAPAGGMQL
VPYQAPGAQQ QRPLNNEELQ RLYSLPAQMA QMQVVPVAQP NTIYYYPGAV VTPPVVPGSA
AYMPPQYPAQ SYRYGGGFTH MDLSQPRPSP APSVSSQPSS HVAPPQNSQN PANGVALKAR
RQVPSTASIS SSSNGQRSGS DLIDLNQDEY SRVSVLEAFD PLLNENTGND SASDCTSYYA
EYDPFDFLYS GDAGTQYSDP MYEAVNRWDK SAATVSPNVN VIGWRQDFLS QPSTSSAAYQ
TDNVAQPLEE ELRLSENGSG SMSPPPPLPP RNQHSLEYPG VPSKPNQSTP FTDSYTSSIP
AHVVLDRRKT CTRLYEVISE QRSDDPELLE FYHMVKQLRA RYPHDDAPTN VGHVVATEFD
YHYMMNTSIK VIVHPALNTL QPHALSASMA KEQVKGYGMP VTFTCDIDSV VAQVVAQALA
SLEGQVRGTV TDYAVKPIGL LEWLAPTSKL SQLECVHNSF QLEKDVHLGL CLSTTANMQA
IARTERDDEH DADLLPEQLL PNEVVQTITY DSMMILIETL ETEIDKLESA ADGAPSRSVL
SCSGVVQAVK AICALLGSID TLDIARCVAD LKRICEEAQT KYLAGASNPE IVSDYGDYAQ
VTLRPRSLLE QIKVKCNGLR DAVQELVELY ANVFRVAFSV KTPDYSTTPI PISCVSKPIV
VSINCLHRPP PNWKYEDYSL CVQLVYGTRL LSKPHVLSCS NDTSGGLFPR LNFSAWLTFE
QHPICTLPRE ARLTIVLYGK QAASEGEPNT DQNGERRQVT TELGWCSIQL FDFKRVMICG
PYLLSVWPPT TDKMLGPAPA RGCHPHPDYC PVLSIEVPPY GGRIEFPEHQ EIPKPAPHYD
FASLDANLQE ELLDTAELGY SGATDRREVF WEKRLYLQKY PNALPKVLHA AHSWDYANLI
DLHALLHSWA PLSPLQALEL LLPRYPDAKV REKAVEWISK MPNDQLVDFL PQLVQSLKHD
TYEGSAMARF LLAKCLESPR FAHHMYWLLV HSLPDDPHNS IGAAMVDQEY DESQVTQARY
YRRNKMMLRA LMAICGEKML QRFMYQHRMC QKLTKIAESV KEAKESMRQK CLAAGMDEVH
QDLLEKPTCL PLGPELEVTG VSVRNCSYFN SNTLPLKINF VGPDAESLPA IFKCGDDLQQ
DQLTIQLIRI MNKMWLAERL DLKMVTFNCV PTGYKSGMIE LVNEAETLRK IQVEYGLTGS
FKDRPIAEWL GKQNPSPLEY QSAVRNFTLS CAGYSVATYV LGICDRHNDN IMLKTSGHLF
HIDFGKFLGD AQMFGNFKRD RTPFVLTSDM AYVINGGDKP TIDFHYFVDY CCRAFNIVRK
NADLLLHTLA HMATAGMPGV NSNAVTYVRR ALLPSQSNPE AAATFAKMIQ SSLKSWFTQF
NFFLHNLAQI RFTPEEGSGE LLSFVPRKYT MQQDGRLKIV KVVCFQKHYS MEKFYMYILE
VTRHGQPVPT HLFRSYREFT EFHEKLCLHF PLVKLHSLPA GVHVGRSNIK SVAEKRLPLI
QRFLKSLFDA SEEIAHSELV YTFFHPLLRD QQEAKLEMPK IKEVKRQPSR DNPNEIGQIR
LSLQYQRGVL TVMIHHAKGL PMLQGGQEPN TYVKCYLKPD PKKETKRKTK VVRKTCVPSF
METLEYRMPL NIIQERRLQV TVWSHDTLQE NELLGGFELD LSKHDLRQEL CDWHRLGTVP
RN
//
