PI3K2_DICDI
ID PI3K2_DICDI Reviewed; 1857 AA.
AC P54674; Q54RJ8;
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 2;
DE Short=PI3-kinase;
DE Short=PI3K;
DE Short=PtdIns-3-kinase;
DE EC=2.7.1.137;
GN Name=pikB; Synonyms=pik2; ORFNames=DDB_G0283081;
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:PRU00879, ECO:0000255|PROSITE-ProRule:PRU00880}.
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DR EMBL; U23477; AAA85722.1; -; mRNA.
DR EMBL; AAFI02000050; EAL65869.1; -; Genomic_DNA.
DR PIR; T18273; T18273.
DR RefSeq; XP_639238.1; XM_634146.1.
DR AlphaFoldDB; P54674; -.
DR SMR; P54674; -.
DR STRING; 44689.DDB0191474; -.
DR PaxDb; P54674; -.
DR PRIDE; P54674; -.
DR EnsemblProtists; EAL65869; EAL65869; DDB_G0283081.
DR GeneID; 8623924; -.
DR KEGG; ddi:DDB_G0283081; -.
DR dictyBase; DDB_G0283081; pikB.
DR eggNOG; KOG0904; Eukaryota.
DR HOGENOM; CLU_236743_0_0_1; -.
DR InParanoid; P54674; -.
DR OMA; KENIWRQ; -.
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:P54674; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005938; C:cell cortex; IDA:dictyBase.
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:0044354; C:macropinosome; IDA: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; IDA: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: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:0051591; P:response to cAMP; IGI:dictyBase.
DR GO; GO:0051602; P:response to electrical stimulus; 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; Transferase.
FT CHAIN 1..1857
FT /note="Phosphatidylinositol 3-kinase 2"
FT /id="PRO_0000088823"
FT DOMAIN 821..934
FT /note="PI3K-RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00879"
FT DOMAIN 1099..1271
FT /note="C2 PI3K-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT DOMAIN 1326..1503
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 1568..1845
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1580
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1711..1719
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 1730..1756
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 8..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 14
FT /note="S -> P (in Ref. 1; AAA85722)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="S -> C (in Ref. 1; AAA85722)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="D -> V (in Ref. 1; AAA85722)"
FT /evidence="ECO:0000305"
FT CONFLICT 1014
FT /note="S -> SN (in Ref. 1; AAA85722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1857 AA; 203822 MW; 750336008B288443 CRC64;
MKMSEGIISP LSLSSESSEQ QQAAIRKFSN GSNGSGGGGG SNLSVNSSNS GSNNSIRKSS
TLMYNGPLPS INDGKELLLE NSKPKVVELV NTFNHKPLST IHSVHNEIPP PAIEKEKKEI
INTISNSGVT KYMTALEILD STINTPLNRS RSGSIGSKPI CNNLTSSSSS SSTTATTPSP
TTTSNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNTTST TTTTTSILIS
SSPPPSSSSS SSSNDEQFNN NNNNNNSNSG GSSRMITSKS QIKPLIVTSN TAATTTTTTT
TNTSAPTTPT NRVQSSLDDL LFNLPTIPSN VPTVNGGPKI SAVPKKVSSS KLLIPPSSNV
SSSSNITLSL SSSSPSSSSS SSTSTVVPIV QLSSSNSTNS PSTSLPTTPR LSQPTTSYTQ
LIPSQQQQQP TESNSSSNTN TTTTSSSSSS SSSSLTISSP QPSNNSIRIS AFGRSSTQFT
ISSNGIPSSP GQVSNKDYNN IGNLSNSSGE RVKNKQYSML NISKKTILDE SDISSSPRSI
GSPNSIRASI SSQLPPSLSS IGGGGGGGSG PNVVSNKPLV VKKPSTSEHI KKENIWRQTM
IPLTKEDHIK VVFEGIPGKR VIQKFLIDKT PIEIKSKFFE DLKDGDLLNG LTQLPSLIPE
HYELKVLSVN STISNETLPL RRQTLMQACN ISRLFPKLHL ILKSESTTIL DGASTTTTTT
TTTTTTTANQ SSNIITKSNS SLDLTINNSN EIIDVKGHIQ AELEIFELIG TSFTRVLDQG
QEVVSFRRDF AQFRLSNFTS TRNDLSQMIY VSSEPLPLTI PNKITIMVLL PGDGKIIKRV
DCCPNSSVGD VKKEIFKKFA MIDRVHTQGK TQDDFVLKVT GFREYILCIH ELGNLTSRQR
FYPTGSGGDF SLMDYDYIRQ CVGKNQTVEL SLTNNSILSL NQVSEKVSFI DKILETSDFD
DYDEDLDSIN SNSFDDLKQS IQQQQQQQIQ TVINIKETNK ENKDSNKENK DSSSNNNNNN
NNNNNNNNNN NNNNNNNNNN NGNNNGNNSN NNSNSNISRG SIDSEGNGSG SGNGSEQPTL
IGVQNFSLPN NSKLPINIVK RLFRVNIAGL RNLNFNNNED ARNKFADGKN NQPNVFVMAE
LYYGGELLTN PVFTPIAQLA SYGDGSVEFP NWEKGIAFTI PIRYLPRAAR ASFTVYVTTI
SEALESQMDE VVSKSIPIGW SNCLLMNHKG MLRMGPTAFR LWDDGRRANP IGTCVDNQAA
KQPIILLVEF ESFIRPIVYV DTALQSMMVN DSSSISSNGV ESPSIVSFSS SAASSSPLPS
SPLPSPVGLK KLDLDEARRL KALMDSDPLV QLSAEDKKLV YGYRHIYKSK PKALAKFLLS
VNWIDPDQVT DAYRQMNDWA LLKPVQALEI LDAKFADEHV RNFAIKIINS FSDAEFSDFL
LQLTQVLKYE PYHNSDLTHI LIQRALSNRS RIGHFFFWFL KSEMHTPEIE ERYGLLLEGY
LRSCGTHRQD LIKQNQVLKS LHTVAMAVKQ TNGSSERKKV LMEGLSKIKF PDTFQLPLDP
RWEAKGLIID KCRYMDSKKL PLWLVFENVE PHAKPLTVIF KVGDDLRQDI LTLQVLRIMD
KFWKNSGMDL RLQPYKCIAT GDGIGMLEVV LNANTIANIN KDAGGTGALL EEKTLVNWLK
ECNKTEAEYN KAVETFILSC AGYVVATYVM GIGDRHSDNI MITKLGHLFH IDFGHFLGNY
KKKYGFKRER APFIFTPQYM AIVGGKDSEN FKRFVTTCCS AYNILRKNTD LFINLFQLML
STGIPELQVA EDIDYLRKAL APGLSDEEAA EEFTKNISVA LNTKTVLLND IFHGWAH
