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PI3K2_SOYBN
ID   PI3K2_SOYBN             Reviewed;         812 AA.
AC   P42348;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Phosphatidylinositol 3-kinase, nodule isoform;
DE            Short=PI3-kinase;
DE            Short=PI3K;
DE            Short=PtdIns-3-kinase;
DE            EC=2.7.1.137;
DE   AltName: Full=SPI3K-1;
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 nodule;
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: Highly expressed in young root nodules in parallel with
CC       membrane proliferation but is repressed in mature nodules.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00880}.
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DR   EMBL; L29770; AAA64468.1; -; mRNA.
DR   PIR; T07745; T07745.
DR   RefSeq; NP_001242315.1; NM_001255386.1.
DR   AlphaFoldDB; P42348; -.
DR   SMR; P42348; -.
DR   STRING; 3847.GLYMA06G10090.1; -.
DR   PRIDE; P42348; -.
DR   GeneID; 100778348; -.
DR   KEGG; gmx:100778348; -.
DR   eggNOG; KOG0906; Eukaryota.
DR   OrthoDB; 204282at2759; -.
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:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
DR   GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR   GO; GO:0030242; P:autophagy of peroxisome; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; 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   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; 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; PTHR10048; 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; SSF48371; 1.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF54452; SSF54452; 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; PS51545; PIK_HELICAL; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..812
FT                   /note="Phosphatidylinositol 3-kinase, nodule isoform"
FT                   /id="PRO_0000088821"
FT   DOMAIN          14..175
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00880"
FT   DOMAIN          272..447
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT   DOMAIN          531..797
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          537..543
FT                   /note="G-loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          666..674
FT                   /note="Catalytic loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT   REGION          685..706
FT                   /note="Activation loop"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
SQ   SEQUENCE   812 AA;  93002 MW;  94C5A922AF198A4B CRC64;
     MTGNEFRFFL SCDISVPVTF RVERLEGNLP LPKSPDLENN APTDNRTTEL FVECALYIDG
     APFGLPMRTR LESLGPSYCW NELITLTTKY RDLTAQSQLT FTVWDLSHGE GLIGGATILL
     FNNKKQLKTG KQKLRLWAGK EADGTFPTST PGKVPRHERG ELERLEKLVN KYERGQIQRV
     DWLDRLTFKT MERIKERESL KNGSSHMYLV VDFCSFEHRV VFQESGANFL FPSPIASTND
     IVVVWDPEVG KINPSEHKQL KLARSLTRGV IDRDLKPSSN ERKSIQRILK YPPTRTLSGD
     ERQLLWKFRF SLMSEKRALT KFLRCVEWSD VQEAKQALEL MGKWEMIDVC DALELLSPVF
     ESEEVRAYAV SVLERADDEE LQCYLLQLVQ ALRFERSAKS RLSHFLIQCA LRNIELASFL
     RWYVAVELYD PAYAKRFYCT YEILEENMMK IAAGVNGEED GFKQWQSLVR QTELTAQLCS
     ITREVSNVRG NTQKKIEKLR QLLSGLLSEL TYFDEPIRSP LAPGVLITGI VPSESSIFKS
     ALHPLRLTFR AANGGTCKII FKKGDDIRQD QLVVQMVSLM DRLLKLENLD LHLTPYKVLA
     TGQDEGMLEF IPSRSLAQIL SENRSIISYL QKFHPDDHGP FGITATCLET FIKSCAGYSV
     ITYILGIGDR HLDNLLLRND GGLFHVDFGF ILGRDPKPFP PPMKLCKEMV EAMGGAESQY
     YTRFKSYCCE AYHILRKSSN LILNLFYLMA GSNIPDIASD PEKGILKLQE KFRLDLDDEA
     SIHFFQDLIN ESVSALFPQM VETIHRWAQY WR
 
 
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