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 27-MAR-2024, entry version 137.
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.P42348; -.
DR PaxDb; 3847-GLYMA06G10090-1; -.
DR GeneID; 100778348; -.
DR KEGG; gmx:100778348; -.
DR eggNOG; KOG0906; Eukaryota.
DR InParanoid; P42348; -.
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..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
//
