PI3K_ARATH
ID PI3K_ARATH Reviewed; 814 AA.
AC P42339; O22695;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Phosphatidylinositol 3-kinase VPS34 {ECO:0000303|PubMed:7972072};
DE EC=2.7.1.137;
DE AltName: Full=PI3-kinase VPS34 {ECO:0000303|PubMed:7972072};
DE Short=AtVPS34 {ECO:0000303|PubMed:7972072};
DE Short=PI3K VPS34 {ECO:0000303|PubMed:7972072};
DE AltName: Full=PtdIns-3-kinase VSP34 {ECO:0000303|PubMed:7972072};
GN Name=VPS34 {ECO:0000303|PubMed:7972072};
GN OrderedLocusNames=At1g60490 {ECO:0000312|Araport:AT1G60490};
GN ORFNames=F8A5.4 {ECO:0000312|EMBL:AAB71971.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Seedling;
RX PubMed=7972072; DOI=10.1073/pnas.91.24.11398;
RA Welters P., Takegawa K., Emr S.D., Chrispeels M.J.;
RT "AtVPS34, a phosphatidylinositol 3-kinase of Arabidopsis thaliana, is an
RT essential protein with homology to a calcium-dependent lipid binding
RT domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11398-11402(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP INTERACTION WITH VPS15.
RC STRAIN=cv. Columbia;
RX PubMed=22361507; DOI=10.1016/j.jgg.2012.01.002;
RA Wang W.-Y., Zhang L., Xing S., Ma Z., Liu J., Gu H., Qin G., Qu L.-J.;
RT "Arabidopsis AtVPS15 plays essential roles in pollen germination possibly
RT by interacting with AtVPS34.";
RL J. Genet. Genomics 39:81-92(2012).
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 -!- SUBUNIT: Interacts with VPS15. {ECO:0000269|PubMed:22361507}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00880}.
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DR EMBL; U10669; AAA83427.1; -; mRNA.
DR EMBL; AC002292; AAB71971.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33693.1; -; Genomic_DNA.
DR EMBL; BT000878; AAN41278.1; -; mRNA.
DR PIR; B96630; B96630.
DR RefSeq; NP_176251.1; NM_104735.4.
DR AlphaFoldDB; P42339; -.
DR SMR; P42339; -.
DR BioGRID; 27568; 1.
DR IntAct; P42339; 2.
DR STRING; 3702.AT1G60490.1; -.
DR PaxDb; P42339; -.
DR PRIDE; P42339; -.
DR ProteomicsDB; 226176; -.
DR EnsemblPlants; AT1G60490.1; AT1G60490.1; AT1G60490.
DR GeneID; 842344; -.
DR Gramene; AT1G60490.1; AT1G60490.1; AT1G60490.
DR KEGG; ath:AT1G60490; -.
DR Araport; AT1G60490; -.
DR TAIR; locus:2036546; AT1G60490.
DR eggNOG; KOG0906; Eukaryota.
DR HOGENOM; CLU_004869_0_0_1; -.
DR InParanoid; P42339; -.
DR OMA; GRQKCKI; -.
DR OrthoDB; 204282at2759; -.
DR PhylomeDB; P42339; -.
DR BioCyc; ARA:AT1G60490-MON; -.
DR BRENDA; 2.7.1.137; 399.
DR PRO; PR:P42339; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42339; baseline and differential.
DR Genevisible; P42339; AT.
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; IDA:TAIR.
DR GO; GO:0055046; P:microgametogenesis; IMP:TAIR.
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 GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
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; 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; 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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..814
FT /note="Phosphatidylinositol 3-kinase VPS34"
FT /id="PRO_0000088819"
FT DOMAIN 25..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 532..799
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 538..544
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"
FT CONFLICT 37
FT /note="S -> A (in Ref. 1; AAA83427)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..453
FT /note="KL -> NW (in Ref. 1; AAA83427)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="G -> R (in Ref. 1; AAA83427)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 93328 MW; 0A09926196E08D3E CRC64;
MGANEFRFFL SCDINSPVTF RIEKLDGNLP VKKSSDSGVV SIAEEKKPEL YIECALYIDG
APFGLPMRTR LKTTGPPYCW NELITLSSKY RDLTAHSQLA ITVWDVSCGK TEGLIGGATV
LLFNSKMQMK SGKQKLRLWQ GKEADGSFPT STPGKVPRHE RGELERLEKL MNKYERGQIQ
SIDWLDRLML KSLDTIKEQE STKHGSSHLF VVIDFCSFEH RVVFQESGAN LFITAPIGST
NEFVTVWDTE LGKTNPSENK QLKLARSLDR GIIDRDLKPS NIERKSIQRV LKYPPTRTLS
GDERQLLWKF RFSLMSEKRA LTKFLRCVEW SDVQEAKQAI QLMYKWEMID VCDALELLSP
LFESEEVRAY AVSVLERADD EELQCYLLQL VQALRFERSD RSCLSQFLVQ RALQNIELAS
FLRWYVAVEL HDHVYAKRFY STYELLEENI IKLPPGVNGE DGYQLWQSLV RQTELTAQLC
SITREVRNVR GNTQKKIEKL RQLLGGLLSE LTYFEEPIRS PLTPNVLIKG IVAGESSLFK
SALHPLRLTF RTPEEGGSCK LIFKKGDDLR QDQLVVQMVW LMDRLLKLEN LDLCLTPYKV
LATGHDEGML EFIPSRSLAQ ILSEHRSITS YLQKFHPDEH APFGITATCL DTFIKSCAGY
SVITYILGIG DRHLDNLLLT DDGRLFHVDF AFILGRDPKP FPPPMKLCKE MVEAMGGAES
QYYTRFKSYC CEAYNILRKS SNLILNLFHL MAGSTIPDIA SDPEKGILKL QEKFRLDMDD
EACIHFFQDL INESVSALFP QMVETIHRWA QYWR