ID   PI3K3_DICDI             Reviewed;        1697 AA.
AC   P54675; Q553Z1; Q869X9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Phosphatidylinositol 3-kinase 3;
DE            Short=PI3-kinase;
DE            Short=PI3K;
DE            Short=PtdIns-3-kinase;
DE            EC=2.7.1.137;
GN   Name=pikC; Synonyms=pik3; ORFNames=DDB_G0275011;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 113-1697.
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).
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:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
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DR   EMBL; AAFI02000013; EAL69786.1; -; Genomic_DNA.
DR   EMBL; U23478; AAA85723.1; -; mRNA.
DR   PIR; T18274; T18274.
DR   RefSeq; XP_643820.1; XM_638728.1.
DR   AlphaFoldDB; P54675; -.
DR   SMR; P54675; -.
DR   STRING; 44689.P54675; -.
DR   PaxDb; 44689-DDB0185203; -.
DR   EnsemblProtists; EAL69786; EAL69786; DDB_G0275011.
DR   GeneID; 8619867; -.
DR   KEGG; ddi:DDB_G0275011; -.
DR   dictyBase; DDB_G0275011; pikC.
DR   eggNOG; KOG0905; Eukaryota.
DR   HOGENOM; CLU_240995_0_0_1; -.
DR   InParanoid; P54675; -.
DR   OMA; LHAHEIF; -.
DR   PhylomeDB; P54675; -.
DR   BRENDA; 2.7.1.137; 1939.
DR   Reactome; R-DDI-114604; GPVI-mediated activation cascade.
DR   Reactome; R-DDI-1660499; Synthesis of PIPs at the plasma membrane.
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-392451; G beta:gamma signalling through PI3Kgamma.
DR   PRO; PR:P54675; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR   GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR   GO; GO:0032060; P:bleb assembly; IGI:dictyBase.
DR   GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IBA:GO_Central.
DR   GO; GO:0036092; P:phosphatidylinositol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0050920; P:regulation of chemotaxis; IGI:dictyBase.
DR   GO; GO:0009617; P:response to bacterium; IMP:dictyBase.
DR   CDD; cd08380; C2_PI3K_like; 1.
DR   CDD; cd00872; PI3Ka_I; 1.
DR   CDD; cd00891; PI3Kc; 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; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR000341; PI3K_Ras-bd_dom.
DR   InterPro; IPR035448; PI3Kc.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048:SF48; PHOSPHATIDYLINOSITOL 3-KINASE 3; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 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   SMART; SM00142; PI3K_C2; 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; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW   Transferase.
FT   CHAIN           1..1697
FT                   /note="Phosphatidylinositol 3-kinase 3"
FT                   /id="PRO_0000088824"
FT   DOMAIN          737..823
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT   DOMAIN          888..1036
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT   DOMAIN          1060..1238
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          1304..1581
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REPEAT          1622..1626
FT                   /note="1"
FT   REPEAT          1627..1631
FT                   /note="2"
FT   REPEAT          1632..1636
FT                   /note="3"
FT   REPEAT          1642..1646
FT                   /note="4"
FT   REPEAT          1647..1651
FT                   /note="5"
FT   REGION          57..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          310..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..428
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1310..1316
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1447..1455
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1466..1492
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          1609..1697
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1622..1651
FT                   /note="5 X 5 AA approximate repeats"
FT   REGION          1659..1672
FT                   /note="7 X 2 AA tandem repeats of K-E"
FT   COMPBIAS        244..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1609..1628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1629..1697
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        1159
FT                   /note="A -> T (in Ref. 3; AAA85723)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1175
FT                   /note="M -> L (in Ref. 3; AAA85723)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1697 AA;  192942 MW;  C5442DC2C3202E32 CRC64;
     MRQIVTGVIH QTTQSQQIPN VINSNQIQFS NEPMVVGSIE DFDIDSEVPP LAINLQRSIN
     NNNNNNNNNN NNNNNNNNNN NNNNNNNTQP CTTVFLDRDS CVNVKATIDL LKEQLEFTIK
     DLIDFKENYD KLESTEQFKQ WSNLIKNIKE NSLNNSNIYL TIPTTQNLIN NNNNNNNNNN
     NNNNNNNNNN NNNNNNVIIP SASTENKEEN DNNNSNNNNN INLSPDSSIT KDINITENKI
     TEIKTTETKE TSTGTSPLEK SPSKGFIISP KKPEEENEIE GETINNIAIT NYTQGPSMLT
     LMKKKLENIK KNNNNNNNNG NGNNNSNNNN SNSNNNNNGI SPSSSPPSHL NGNNNNNNSN
     NTNSNNTTNA TTNSVGFSIT MTNSNSLSVS KRMNKFKSWT SSKPTSSSIG FASSPQNNGK
     PLNISGSSRF FTSRQDSKID LLKSPSSSPP TQSDIFNENN NNNNNNNNNN NNNNNNNNNN
     NNNNNNNNNN EELINNNNNN NNDENYKIEE TEESLKELLE KEKLENEERE KILKERNEID
     NLKKKNHLSK GYFMRACNAS NDDGLEEEDI PLQDEHWETN VIVLLPCRHH VKVPGSSSSS
     IDSIRQLAWA SGKMQGHLNL EKDEKFFTLR WCNKDVVFDQ DTPLGHLIQY NLNYNNPTQK
     PTNIKLELVL EDELCKERLV DLQSLEINNG RPSIWKSHID DVLSFNRKLR ELAMLAKPQS
     NVPAARLTPY PPPKTIPEFF VIRVHLFKNQ TKSLRCANNH TAFSLMTILS EKLKNTTPFD
     PTQYRFLITG INQYVDPNVP LLSVEYIVEK IKRKGEIDLT MVELLSLGLI IQQQQQQQQQ
     QQQQQQQQQI ENIDDENILK LNNGILNVLS KIEKPIREKD NCISSLTVTE NLQVRLLHAH
     EIFASKASEI IGTDSPSIQL FIEAAVYFGG ELLATQSSKL VSFQDTVVWN EWVNIPLAVS
     NIPNGARMCL GLNARYRGDI FNIGWVGHRL FDSKGILNTF APFSLLLWPG KINPIGTCVD
     NLESKDQAII IAFEFKDYVV PKTIHYEDDL IELISKDENG NELPVVTMEE MDRVEQIILQ
     DPLYSLNKEE RLLIWKSRYF CHTKPQALSK LLQSVEWTNY KQVGEAFQLL KIWPTLSAVD
     ALELLDPKFA DCVEIREYAV KCLDQMSDYE LEIYMLQLVQ AIKHDVFHNS VLSLFLIGRV
     WQNMQVLGHP FFWHLRADID NQEVCERFRV LSSGFLRYAP TQLMESFKRE ITTLRILENL
     AKRVKEVPYE KRKQYVENNL REEQSFPTEL FVPFDPSIRI LNIIPEKCKS MDSAKVPLWV
     TFKNADPFAP PLQMIAKTGD DLRQDILTLQ LLRLMDHMWK SQDLDLHMTI YRCIATGMGT
     GLIEVVPNSE TAARIQAGAG GVSGAFKQTP IANWLKNHNQ TENSYQKAVS KFTLSCAGYC
     VATYVLGIGD RHNDNIMVDI HGHLFHIDFG HFLGNFKTFA GFQREKAPFV LTPDFVYVIG
     GKDSPNFAFF VDICCKAFNI IRSNAHVFIN MFELMLSTGI PELRSENDIV YLRDKFRLDL
     TDAEASEYFK KLIHESIGTL TTTINFAIHI MAHRKNLVSG NSAPKIGSAS SLNLNKNKPS
     SQSKLDLSRS DLSRSDSSRS DSSRLDLSRS DKKNNKDNKE KEKEKEKEKE KENNDNNDKD
     NNNNSNNDTE KENSIDK
//