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Database: UniProt
Entry: A0A6J2YJE0_SITOR
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ID   A0A6J2YJE0_SITOR        Unreviewed;      1062 AA.
AC   A0A6J2YJE0;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   28-JAN-2026, entry version 27.
DE   RecName: Full=phosphatidylinositol 3-kinase {ECO:0000256|ARBA:ARBA00012073};
DE            EC=2.7.1.137 {ECO:0000256|ARBA:ARBA00012073};
GN   Name=LOC115888539 {ECO:0000313|RefSeq:XP_030764148.1};
OS   Sitophilus oryzae (Rice weevil) (Curculio oryzae).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Curculionidae; Dryophthorinae; Sitophilus.
OX   NCBI_TaxID=7048 {ECO:0000313|Proteomes:UP000504635, ECO:0000313|RefSeq:XP_030764148.1};
RN   [1] {ECO:0000313|RefSeq:XP_030764148.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_030764148.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00001498};
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00880}.
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DR   RefSeq; XP_030764148.1; XM_030908288.1.
DR   AlphaFoldDB; A0A6J2YJE0; -.
DR   GeneID; 115888539; -.
DR   OrthoDB; 67688at2759; -.
DR   Proteomes; UP000504635; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035005; F:1-phosphatidylinositol-4-phosphate 3-kinase activity; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0032060; P:bleb assembly; IEA:UniProtKB-ARBA.
DR   GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:TreeGrafter.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:TreeGrafter.
DR   GO; GO:0050920; P:regulation of chemotaxis; IEA:UniProtKB-ARBA.
DR   CDD; cd05165; PI3Kc_I; 1.
DR   FunFam; 1.10.1070.11:FF:000001; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit; 1.
DR   FunFam; 3.30.1010.10:FF:000008; Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma; 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; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 2.
DR   Gene3D; 3.30.1010.10; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 4; 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; IPR015433; PI3/4_kinase.
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; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   PANTHER; PTHR10048:SF118; PI-3 KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF02192; PI3K_p85B; 1.
DR   Pfam; PF00794; PI3K_rbd; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00143; PI3K_p85B; 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; PS51544; PI3K_ABD; 1.
DR   PROSITE; PS51546; PI3K_RBD; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000504635};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          19..108
FT                   /note="PI3K-ABD"
FT                   /evidence="ECO:0000259|PROSITE:PS51544"
FT   DOMAIN          185..283
FT                   /note="PI3K-RBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51546"
FT   DOMAIN          325..492
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          518..695
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          760..1045
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1062 AA;  122817 MW;  0AD3B5D1A089605E CRC64;
     MVPIPAEYMP DFWSLLSTEC PIVELTCLLP NGIIVLLKVN HNATLAEIKE DLWEEASRFP
     LYGKLHDISV YTFKIINSMA EEEELNDDLR KLCDIKPTGG VLIISECRGN SVDHSVNVAI
     GHLIGKGLQE FDALNSNEIN DFRFKMRKMG DEISEKRNQG TWLDKLQYQF PPRLSQSDDV
     KFKGIKCICV ETKCEYEIAE FERESLQSTF KLNVLPTTKP IELMEMILSK RANLNIKNES
     VTEYILKICG RDEYLVGDFS IIEFQYIQDC LLQDIIPSFL SVHINRILDN DYDYVDILEA
     RKNKTVFNST NTLRKKKNIE STWNISDNYT ITLCTASKLN CDTKKSTEIG IQVGLFHGGK
     PLCQPVKTEE RLVSEKCEVE FNVDLELDIE VWHIPRNAKL CFVIYESNKY FKGTKSRKPK
     EVKDSQINPI AWANTTVFDF KGYLRTGAMT LYLWTYAEDI MSDDVLHPLG TVVSNPNKEY
     CTALTLIFKS YGSDQNYTYP ALETVINYGN SLQEINNSIL ETLTDETKES FLRLINDMDN
     FYDIYDQDRE TIWSHRKFWI KHTPELFPKL LLCIDWNKRE DVSQAIVLTR ECPKLPIEKA
     LELLDYAYAD QVVRSFAVQC LQDMSDEDLL LYLLQLVQAI KHELYLDCDL VNFLIKRALD
     NQKIGHYLFW HLRSEMQVAS VSVRFGLILE AYCRGSQEHI PVLQRQLKSI EKLKQCSEIV
     RNRRDKEKAK AALKEYIVNN SAKDIVRSPL DPSYRCNGIK IEKCRVMDSK MKPLWIVYEN
     YDRYGEDVYL IFKNGDDLRQ DMLTLQMLKI MDKLWKREGL DLRMNPYNCI SLEPRVGMIQ
     VVLNAETIAN IQKEKNSFAP TASFRKGSIL AWLKDHNTTE AALNKAIKEF TLSCAGYCVA
     TYVLGIGDRH SDNIMVKKTG QLFHIDFGHI LGHFKEKFGI KRERVPFVLT HDFVFVINKG
     QKTQQETPTE FKEFQDNCEK AFMILRKHGN LILSLFAMMI STGLPELSSE KDLQYLRETL
     VLSKTDEEAK AHFRAKFDEA LSNSWKTSLN WASHNIAKNN KG
//
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