PI5K2_ARATH
ID PI5K2_ARATH Reviewed; 754 AA.
AC Q8L796; Q9CA20;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase 2 {ECO:0000303|PubMed:19903693};
DE Short=AtPIP5K2 {ECO:0000303|PubMed:19903693};
DE EC=2.7.1.68 {ECO:0000305|PubMed:19903693};
DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase 2;
DE AltName: Full=Diphosphoinositide kinase 2;
DE AltName: Full=PtdIns(4)P-5-kinase 2 {ECO:0000303|PubMed:19903693};
GN Name=PIP5K2; OrderedLocusNames=At1g77740; ORFNames=T32E8.7;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12226484; DOI=10.1104/pp.004770;
RA Mueller-Roeber B., Pical C.;
RT "Inositol phospholipid metabolism in Arabidopsis. Characterized and
RT putative isoforms of inositol phospholipid kinase and phosphoinositide-
RT specific phospholipase C.";
RL Plant Physiol. 130:22-46(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH
RP RABE1A; TUFA; RABE1C; RABE1D AND RABE1E, AND INDUCTION.
RX PubMed=19903693; DOI=10.1242/jcs.053488;
RA Camacho L., Smertenko A.P., Perez-Gomez J., Hussey P.J., Moore I.;
RT "Arabidopsis Rab-E GTPases exhibit a novel interaction with a plasma-
RT membrane phosphatidylinositol-4-phosphate 5-kinase.";
RL J. Cell Sci. 122:4383-4392(2009).
CC -!- FUNCTION: Possesses phosphatidylinositol (PtdIns) phosphate kinase
CC activity (Probable). Phosphorylates PtdIns(4)P and PtdIns(3)P in vitro
CC (PubMed:19903693). Doesn't phosphorylate PtdIns(5)P nor PtdIns(3,4)P2
CC in vitro (PubMed:19903693). Does not exhibit phosphatidylinositol
CC kinase activity in vitro (PubMed:19903693).
CC {ECO:0000269|PubMed:19903693, ECO:0000305|PubMed:19903693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC Evidence={ECO:0000305|PubMed:19903693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14426;
CC Evidence={ECO:0000305|PubMed:19903693};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:13609,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57923,
CC ChEBI:CHEBI:58088, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:19903693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13610;
CC Evidence={ECO:0000305|PubMed:19903693};
CC -!- ACTIVITY REGULATION: Activated by binding to RABE1D.
CC -!- SUBUNIT: Interacts with RABE1A, TUFA, RABE1C, RABE1D and RABE1E.
CC {ECO:0000269|PubMed:19903693}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19903693}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8L796-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8L796-2; Sequence=VSP_015946;
CC -!- MISCELLANEOUS: Plants overexpressing PI5K2 exhibit severe dwarfism and
CC are enriched in the plasma membrane of the root meristem.
CC {ECO:0000305|PubMed:19903693}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
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; AC012193; AAG51623.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36015.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59859.1; -; Genomic_DNA.
DR EMBL; AY136391; AAM97057.1; -; mRNA.
DR EMBL; BT002112; AAN72123.1; -; mRNA.
DR PIR; C96807; C96807.
DR RefSeq; NP_001319397.1; NM_001334792.1. [Q8L796-1]
DR RefSeq; NP_177897.1; NM_106423.2. [Q8L796-1]
DR AlphaFoldDB; Q8L796; -.
DR SMR; Q8L796; -.
DR BioGRID; 29329; 1.
DR STRING; 3702.AT1G77740.1; -.
DR iPTMnet; Q8L796; -.
DR PaxDb; Q8L796; -.
DR PRIDE; Q8L796; -.
DR ProteomicsDB; 236735; -. [Q8L796-1]
DR EnsemblPlants; AT1G77740.1; AT1G77740.1; AT1G77740. [Q8L796-1]
DR EnsemblPlants; AT1G77740.2; AT1G77740.2; AT1G77740. [Q8L796-1]
DR GeneID; 844110; -.
DR Gramene; AT1G77740.1; AT1G77740.1; AT1G77740. [Q8L796-1]
DR Gramene; AT1G77740.2; AT1G77740.2; AT1G77740. [Q8L796-1]
DR KEGG; ath:AT1G77740; -.
DR Araport; AT1G77740; -.
DR TAIR; locus:2203211; AT1G77740.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_4_1; -.
DR InParanoid; Q8L796; -.
DR OMA; GRYTSKP; -.
DR PhylomeDB; Q8L796; -.
DR BioCyc; ARA:AT1G77740-MON; -.
DR PRO; PR:Q8L796; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L796; baseline and differential.
DR Genevisible; Q8L796; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:RHEA.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003006; P:developmental process involved in reproduction; IMP:TAIR.
DR GO; GO:0010311; P:lateral root formation; IMP:TAIR.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR Gene3D; 3.30.800.10; -; 1.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR017163; PIno-4-P-5_kinase_pln.
DR InterPro; IPR023610; PInositol-4-P-5-kinase.
DR InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR PANTHER; PTHR23086; PTHR23086; 1.
DR Pfam; PF02493; MORN; 7.
DR Pfam; PF01504; PIP5K; 1.
DR PIRSF; PIRSF037274; PIP5K_plant_prd; 1.
DR SMART; SM00698; MORN; 7.
DR SMART; SM00330; PIPKc; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transferase.
FT CHAIN 1..754
FT /note="Phosphatidylinositol 4-phosphate 5-kinase 2"
FT /id="PRO_0000185474"
FT REPEAT 82..104
FT /note="MORN 1"
FT REPEAT 105..127
FT /note="MORN 2"
FT REPEAT 128..150
FT /note="MORN 3"
FT REPEAT 151..173
FT /note="MORN 4"
FT REPEAT 174..196
FT /note="MORN 5"
FT REPEAT 197..219
FT /note="MORN 6"
FT REPEAT 220..242
FT /note="MORN 7"
FT DOMAIN 351..750
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 54..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..731
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..436
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_015946"
SQ SEQUENCE 754 AA; 86345 MW; 5F861AA47EEC0B33 CRC64;
MMREPLVSEE EEEEATEVLL VEKTKLCKRR GDEEKTEERR DDLLLLALTP MVRSKSQGTT
RRVTPTPPPV DVEKPLPNGD LYMGTFSGGF PNGSGKYLWK DGCMYEGEWK RGKASGKGKF
SWPSGATYEG EFKSGRMEGS GTFVGVDGDT YRGSWVADRK QGHGQKRYAN GDYYEGTWRR
NLQDGRGRYV WMNGNQYTGE WRNGVICGKG VLAWPNGNRY EGQWENGVPK GSGVFTWADG
SSWIGSWNES SNLMRNFFDG IEKNELIVAT RKRSSVDSGA GSLTGEKIFP RICIWESDGE
AGDITCDIVD NVEASVIYRD RISIDKDGFR QFRKNPCCFS GEAKKPGETI SKGHKKYDLM
LNLQHGIRYS VGKHASVVRD LKQSDFDPSE KFWTRFPPEG SKTTPPHLSV DFRWKDYCPL
VFRRLRELFT VDPADYMLAI CGNDALRELS SPGKSGSFFY LTQDDRFMIK TVKKSEVKVL
LRMLPSYYKH VCQYENTLVT RFYGVHCIKP VGGQKTRFIV MGNLFCSEYR IQRRFDLKGS
SHGRYTSKPE GEIDETTTLK DLDLNFAFRL QRNWYQELMT QIKRDCEFLE AERIMDYSLL
VGVHFRDDNT GDKMGLSPFV LRSGKIESYQ SEKFMRGCRF LEAELQDMDR ILAGRKPLIR
LGANMPARAE RMARRSDYDQ YSSGGTNYQS HGEVYEVVLY FGIIDILQDY DISKKIEHAY
KSLQADPASI SAVDPKLYSR RFRDFISRIF IEDG
