ID   PI3K4_DICDI             Reviewed;         816 AA.
AC   P54676; Q54HA2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Phosphatidylinositol 3-kinase VPS34-like;
DE            Short=PI3-kinase;
DE            Short=PI3K;
DE            Short=PtdIns-3-kinase;
DE            EC=2.7.1.137;
GN   Name=pikE; Synonyms=pik5; ORFNames=DDB_G0289601;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AX3;
RX   PubMed=7565716; DOI=10.1128/mcb.15.10.5645;
RA   Zhou K., Takegawa K., Emr S.D., Firtel R.A.;
RT   "A phosphatidylinositol (PI) kinase gene family in Dictyostelium
RT   discoideum: biological roles of putative mammalian p110 and yeast Vps34p PI
RT   3-kinase homologs during growth and development.";
RL   Mol. Cell. Biol. 15:5645-5656(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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;
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00880}.
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DR   EMBL; U23480; AAA85726.1; -; Genomic_DNA.
DR   EMBL; AAFI02000147; EAL62618.1; -; Genomic_DNA.
DR   PIR; A59003; A59003.
DR   RefSeq; XP_636122.1; XM_631030.1.
DR   AlphaFoldDB; P54676; -.
DR   SMR; P54676; -.
DR   STRING; 44689.P54676; -.
DR   PaxDb; 44689-DDB0219939; -.
DR   EnsemblProtists; EAL62618; EAL62618; DDB_G0289601.
DR   GeneID; 8627225; -.
DR   KEGG; ddi:DDB_G0289601; -.
DR   dictyBase; DDB_G0289601; pikE.
DR   eggNOG; KOG0906; Eukaryota.
DR   HOGENOM; CLU_004869_0_0_1; -.
DR   InParanoid; P54676; -.
DR   OMA; LHKFAQY; -.
DR   PhylomeDB; P54676; -.
DR   BRENDA; 2.7.1.137; 1939.
DR   Reactome; R-DDI-1632852; Macroautophagy.
DR   Reactome; R-DDI-1660514; Synthesis of PIPs at the Golgi membrane.
DR   Reactome; R-DDI-1660516; Synthesis of PIPs at the early endosome membrane.
DR   Reactome; R-DDI-1660517; Synthesis of PIPs at the late endosome membrane.
DR   Reactome; R-DDI-5668599; RHO GTPases Activate NADPH Oxidases.
DR   PRO; PR:P54676; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR   GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd08397; C2_PI3K_class_III; 1.
DR   CDD; cd00870; PI3Ka_III; 1.
DR   CDD; cd00896; PI3Kc_III; 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; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR008290; PI3K_Vps34.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR   SMART; SM00142; PI3K_C2; 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   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; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..816
FT                   /note="Phosphatidylinositol 3-kinase VPS34-like"
FT                   /id="PRO_0000088825"
FT   DOMAIN          39..186
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT   DOMAIN          275..460
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          532..800
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          538..544
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          669..677
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          688..709
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   CONFLICT        4
FT                   /note="S -> T (in Ref. 1; AAA85726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        13
FT                   /note="R -> S (in Ref. 1; AAA85726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44..46
FT                   /note="EKK -> DDP (in Ref. 1; AAA85726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        289..290
FT                   /note="LT -> NS (in Ref. 1; AAA85726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        382
FT                   /note="K -> P (in Ref. 1; AAA85726)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        565
FT                   /note="G -> N (in Ref. 1; AAA85726)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   816 AA;  94748 MW;  DC6637F485FD6975 CRC64;
     MKVSKDFKFY YSRDIPIKYK IKLCTLEGKR NKENAPETVD KWIEKKYLKY SSLYRDTTID
     LYITCTLYSD GKQLSTSEHT SYNPFSVSNK WDETIIFPLK HQDLPFDTMI VITIWDIYSP
     MKKVPIGGTS FNIFGMNKIE RKGKHKLLIW QDREGDGEKE TTTPGQIQGK DEQYRLEKLK
     KKYDRKLINH CQWLDKFSLN EIERLSRASE SLNKNQIYLT IELPEFELPI LFKQQNCPLY
     IPLSQTQKKS LVLINDIEMD EHPSEQKYHR LNLYDHKDLK PNSTELKGLT DILKQPPNTK
     VTSKEALLIW RFRYYLTNNK KALTKFLRCV EWSESHQKNE ALSIMPKWDP IDIADSLELL
     SSAFTHKNTI MVRRYAVEIL KKADDEELLY YLLQLVQATK YEQFDGNPSD SPLISFLFER
     SNKNFILGSH FYWYLTVDSV LKSSIFCSHY KTLQELYFRQ LDHTDAQRVN AQNKFISRLS
     LLSVELKAMN ITREKKIEKL RIMLAEGEYK DLSDFQPIRL PVNPDIEIIG IVPEKSNIYK
     SAKSPLGLKL RTTKGEEYGV IFKTGDDLRQ DQLIIQLISL MDRLLKKENL DLKLTPYKVL
     ATAEEDGIVE MVNPSEAMAS VLSKYDGDIL KFFKTHNPDA DSPYGIAPEV MDTFVKSCAG
     YCVITYILGI GDRHLDNLLL TPNGKLFHID FGYILGKDPK ILPPPMKLCK EMVLGMGGEN
     SKHYEKFKQL CCEAYNILRK SSHLILNLFA LMVDASIPSI SDDKEKSILK VQEKLQLELT
     DQEASNSLLQ LLNDSVTALF PVIIEMAHKW LQYWKA
//