ID   PI3K1_SOYBN             Reviewed;         814 AA.
AC   P42347;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Phosphatidylinositol 3-kinase, root isoform;
DE            Short=PI3-kinase;
DE            Short=PI3K;
DE            Short=PtdIns-3-kinase;
DE            EC=2.7.1.137;
DE   AltName: Full=SPI3K-5;
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Prize; TISSUE=Root;
RX   PubMed=7937816; DOI=10.1073/pnas.91.20.9617;
RA   Hong Z., Verma D.P.S.;
RT   "A phosphatidylinositol 3-kinase is induced during soybean nodule
RT   organogenesis and is associated with membrane proliferation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:9617-9621(1994).
CC   -!- FUNCTION: Associated with membrane proliferation.
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   -!- INDUCTION: Repressed during nodule organogenesis and reinduced in
CC       mature nodules.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00880}.
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DR   EMBL; L27265; AAA83995.1; -; mRNA.
DR   PIR; T07761; T07761.
DR   RefSeq; NP_001236955.1; NM_001250026.2.
DR   AlphaFoldDB; P42347; -.
DR   SMR; P42347; -.
DR   STRING; 3847.P42347; -.
DR   PaxDb; 3847-GLYMA04G10090-1; -.
DR   GeneID; 547983; -.
DR   KEGG; gmx:547983; -.
DR   eggNOG; KOG0906; Eukaryota.
DR   InParanoid; P42347; -.
DR   OrthoDB; 10350at2759; -.
DR   BRENDA; 2.7.1.137; 2483.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central.
DR   GO; GO:0034271; C:phosphatidylinositol 3-kinase complex, class III, type I; IBA:GO_Central.
DR   GO; GO:0034272; C:phosphatidylinositol 3-kinase complex, class III, type II; IBA:GO_Central.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; 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   CDD; cd08397; C2_PI3K_class_III; 1.
DR   CDD; cd00870; PI3Ka_III; 1.
DR   CDD; cd00896; PI3Kc_III; 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; IPR011162; MHC_I/II-like_Ag-recog.
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; IPR008290; PI3K_Vps34.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR   SMART; SM00142; PI3K_C2; 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; SSF54452; MHC antigen-recognition domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-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; PS51545; PIK_HELICAL; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..814
FT                   /note="Phosphatidylinositol 3-kinase, root isoform"
FT                   /id="PRO_0000088820"
FT   DOMAIN          14..177
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT   DOMAIN          274..449
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          533..799
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          539..545
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          668..676
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          687..708
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ   SEQUENCE   814 AA;  93282 MW;  5B13A7DE16FFA0AD CRC64;
     MTGNEFRFFL SCDISVPVTF RVERLEGNLP LPNPKSPDLE TNAPTENRTK ELFVECALYI
     DGAPFGLPTR TRLESSGPSY CWNELITLTT KYRDLTAQSQ LTFTVWDLSH GEGLIGGATI
     LLFNNKKQLK TGKQKLRLWA GKEADGTFPT STPGKVPRHE RGELERLEKL VNKYERGQIQ
     RVDWLDRLTF KTMERIKERE SLKNGSSHLY LVVDFCSFEH RVVFQESGAN FLFPSPIAST
     NDIVVVWDPE VGKINPSEHK QLKLARSLTR GVIDRDLKPS SNERKSIQRI LKYPPTRTLS
     GDERQLLWKF RFSLMSEKRA LTKFLRCVEW SDVQEAKQAL ELMGKWEMID VCDALELLSP
     VFESEEVRAY AVSVLERADD EELQCYLLQL VQALRFERSD KSRLSHFLVQ RALRNIELAS
     FLRWYVAVEL YDPAYAKRFY CTYEILEENM MKIAAGVNGE EDGFKQWQSL VRQTELTAQL
     CSITREVRNV RGNTQKKIEK LRQLLSGLLS ELTYFDEPIR SPLAPGVLIA GIVPSESSIF
     KSALHPLRLS FRTANGGTCK IIFKKGDDLR QDQLVVQMVS LMDRLLKLEN LDLHLTPYKV
     LATGQDEGML EFIPSRSLAQ ILSENRSIIS YLQKFHPDDH GPFGITATCL ETFIKSCAGY
     SVITYILGIG DRHLDNLLLR NDGGLFHVDF GFILGRDPKP FPPPMKLCKE MVEAMGGAES
     QYYTRFKSYC CEAYNILRKS SNLILNLFYL MAGSNIPDIA SDPEKGILKL QEKFRLDLDD
     EASIHFFQDL INESVSALFP QMVETIHRWA QYWR
//