PI3K1_SOYBN
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 03-AUG-2022, entry version 127.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.GLYMA04G10090.1; -.
DR GeneID; 547983; -.
DR KEGG; gmx:547983; -.
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..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
