PI3K4_DICDI
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 03-AUG-2022, entry version 136.
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 (Slime mold).
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.DDB0219939; -.
DR PaxDb; P54676; -.
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; GRQKCKI; -.
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:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; 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 Gene3D; 1.10.1070.11; -; 1.
DR Gene3D; 1.25.40.70; -; 1.
DR Gene3D; 2.60.40.150; -; 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; PTHR10048; 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; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 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
