PI3K1_DICDI
ID PI3K1_DICDI Reviewed; 1571 AA.
AC P54673; Q54XS5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Phosphatidylinositol 3-kinase 1;
DE Short=PI3-kinase;
DE Short=PI3K;
DE Short=PtdIns-3-kinase;
DE EC=2.7.1.137;
GN Name=pikA; Synonyms=pik1; ORFNames=DDB_G0278727;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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:PRU00877, ECO:0000255|PROSITE-ProRule:PRU00879,
CC ECO:0000255|PROSITE-ProRule:PRU00880}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85721.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23476; AAA85721.1; ALT_FRAME; mRNA.
DR EMBL; AAFI02000024; EAL67965.1; -; Genomic_DNA.
DR PIR; T18272; T18272.
DR RefSeq; XP_641955.1; XM_636863.1.
DR AlphaFoldDB; P54673; -.
DR SMR; P54673; -.
DR STRING; 44689.DDB0214949; -.
DR PaxDb; P54673; -.
DR PRIDE; P54673; -.
DR EnsemblProtists; EAL67965; EAL67965; DDB_G0278727.
DR GeneID; 8621687; -.
DR KEGG; ddi:DDB_G0278727; -.
DR dictyBase; DDB_G0278727; pikA.
DR eggNOG; KOG0904; Eukaryota.
DR HOGENOM; CLU_245488_0_0_1; -.
DR InParanoid; P54673; -.
DR OMA; FMNLFAM; -.
DR PhylomeDB; P54673; -.
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:P54673; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:dictyBase.
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; IDA:dictyBase.
DR GO; GO:0031143; C:pseudopodium; TAS:dictyBase.
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:0030295; F:protein kinase activator activity; IGI:dictyBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:dictyBase.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:dictyBase.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; TAS:dictyBase.
DR GO; GO:0019954; P:asexual reproduction; IMP: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:0006935; P:chemotaxis; IMP:dictyBase.
DR GO; GO:0043327; P:chemotaxis to cAMP; IGI:dictyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:dictyBase.
DR GO; GO:0044351; P:macropinocytosis; IMP:dictyBase.
DR GO; GO:0030011; P:maintenance of cell polarity; IGI:dictyBase.
DR GO; GO:0050919; P:negative chemotaxis; IGI:dictyBase.
DR GO; GO:0001845; P:phagolysosome assembly; IGI:dictyBase.
DR GO; GO:0090382; P:phagosome maturation; IGI:dictyBase.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IGI:dictyBase.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IGI:dictyBase.
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; IGI:dictyBase.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1905303; P:positive regulation of macropinocytosis; IGI:dictyBase.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IGI:dictyBase.
DR GO; GO:0031269; P:pseudopodium assembly; IGI:dictyBase.
DR GO; GO:0045761; P:regulation of adenylate cyclase activity; IMP:dictyBase.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IGI:dictyBase.
DR GO; GO:0050920; P:regulation of chemotaxis; IGI:dictyBase.
DR GO; GO:1900027; P:regulation of ruffle assembly; IMP:dictyBase.
DR GO; GO:0009617; P:response to bacterium; IMP:dictyBase.
DR GO; GO:0031000; P:response to caffeine; IDA:dictyBase.
DR GO; GO:0051591; P:response to cAMP; IGI: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; IPR003113; PI3K_ABD.
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; 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; 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; PS51544; PI3K_ABD; 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; Transferase.
FT CHAIN 1..1571
FT /note="Phosphatidylinositol 3-kinase 1"
FT /id="PRO_0000088822"
FT DOMAIN 530..627
FT /note="PI3K-ABD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00877"
FT DOMAIN 700..789
FT /note="PI3K-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT DOMAIN 851..1020
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 1040..1216
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 1280..1558
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1292
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1424..1432
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1443..1469
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 1..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 749
FT /note="D -> H (in Ref. 1; AAA85721)"
FT /evidence="ECO:0000305"
FT CONFLICT 1494
FT /note="A -> G (in Ref. 1; AAA85721)"
FT /evidence="ECO:0000305"
FT CONFLICT 1540
FT /note="E -> A (in Ref. 1; AAA85721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1571 AA; 178472 MW; 9550F58C0E822C9F CRC64;
MNSIESSSND SNEINKNSNK NNTHLNSNYN NIYKNNSTSS NNNNNHNNIE IIGIDNNKNN
NKNNNDNNNN NNNIDKKRKD SKNKQNQEIN QEMSENKKIY NSNDSNCSSG SSSGGHVNNG
HHILIEENER LEHENQEIQE IYKQKGMEFQ KKDLRFGYDV NSNNNNNNGG GSSSGSSSGG
SDESASNQPI IRTRNREGSI LNLKKQGLVK EISQRFQTPD TASYTRPNAN NISIKDKISI
LKKEQERRKQ DSEVQQREKV IVLSADSSNI QIYHPSVLIE KMNSKLDTEE KPATTTTTTT
TTSTSISTST PTTTTTTTTN TSTTNDITIK PKTSPTKNNE ERSQSPITTP KQPVEEIVKK
VSTPKSNNTS KKTSSDTTPT GKTTKKDKKD KKDKSRDSGN LVIVNNTNNT SSNNNNNNNN
NNNNETIIKR RGRVLVTPSS DLKKNIQIYF TIPINPPVNK TNKPNQLLSN TSQQFLKTLI
SNEIPIDCKI NDINDTDAFS DLSASASSSS FITKSSQSLL NVQSLRVKAI KTSFNILFLM
PNQSKKILQV KGSDTIENLK ERIISDYLFN NNSNNNNNNC KYGADSYLIL DFNDNPMERS
LVLNKSDYIL DKRAQGLIPK LKVIEKSTIL DSDPSDELSP SEYEIIRKLI PGTDTWRGEE
VEYFRRVTSR LRYEALPLIK GSIQSTLLVR LSPLPIPIVG NKILISIFLP ITQVTKTLDL
ELNETADQFT NRLFTKNYSK HLPNVNSNDF ILKVVGSSDF IHGPHDIRTF ESIRNHIIQG
TKPQLTLIQR PKPELDPQPF KPRFDYPPEL IIDHSCSNAI NCNNNNTNST NNNNINFDNW
DQITHISIRE IKKPFRVKVM GSTRIPLSCI KDIDSSSVIV SISLYHGIEC FSKAFTQPII
PPPFAFLAET LSVDWCEWLV FTNIDYSNLP VDARLSISVY SANETVDDVE EIKNLDEATK
KLTPIGWINV MITDFKYQLR QGMVELSLWP SDFSNPLGTC SNNPSSSQSV GLTLEFEEFN
LPVLFPRKTK FSTSVSVIEQ PPTNINSNEM REFFEQITAL DPLSDLKQEK YNQLWTLRHY
SILFPQVLPR LMLSVPWTQA TAVDEAISLL DRWPKLKPYE SLELLDAKHA NRKVREFAVT
CLEDLSEDEL LDILLQLVQV LKYEPFHDSK LSRFLLRKAI LNRNIGHSFF WYLKSDLHDS
NLSERFGILL ESYLYACGAH RIELLKQMEV INNLTEVAKK IKPLKDQDRR EFMIKEFESL
EWPKRFHLTL NPRFESNGLI INKSKYMDSK KLPLRLSFTN TDMNADPIEV IFKAGDDLRQ
DMLTLQMIRL MDKLWQKEGL DLKLSPYGCI STGDMIGMIE VVLNSETTAK IQKSEGGGAA
SAFKLDPLAN WILQHNKSDM EYQKAVDTFI LSCAGYCVAT YVLGIGDRHN DNLMVTKGGR
LFHIDFGHFL GNYKKKFGFK RERAPFVFTP DFCYVMGGKE SFKFSQFVNY CCTAYNIVRK
NAKLFMNLFA MMVSTGIPEL QSMEDLNYLK ESFSIELSDE KAREKFVALI HESLATKTTQ
LNNFFHHLAH A
