PI3K3_DICDI
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 03-AUG-2022, entry version 145.
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 (Slime mold).
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.DDB0185203; -.
DR PaxDb; P54675; -.
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 Reactome; R-DDI-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:P54675; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; 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:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0032060; P:bleb assembly; IGI:dictyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IGI:dictyBase.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; 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 GO; GO:0050920; P:regulation of chemotaxis; IGI:dictyBase.
DR GO; GO:0009617; P:response to bacterium; IMP:dictyBase.
DR CDD; cd00891; PI3Kc; 1.
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; IPR000341; PI3K_Ras-bd_dom.
DR InterPro; IPR035448; PI3Kc.
DR InterPro; IPR015433; PI_Kinase.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR10048; PTHR10048; 2.
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; SSF48371; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF54236; SSF54236; 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; 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
