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   27-MAR-2024, entry version 142.
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}.
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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.Q8L796; -.
DR   iPTMnet; Q8L796; -.
DR   PaxDb; 3702-AT1G77740-1; -.
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; AT1G77740; PIP5K2.
DR   eggNOG; KOG0229; Eukaryota.
DR   HOGENOM; CLU_004312_6_4_1; -.
DR   InParanoid; Q8L796; -.
DR   OMA; YSIGKHA; -.
DR   OrthoDB; 340426at2759; -.
DR   PhylomeDB; Q8L796; -.
DR   BioCyc; ARA:AT1G77740-MONOMER; -.
DR   PRO; PR:Q8L796; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8L796; baseline and differential.
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:0046488; P:phosphatidylinositol metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009958; P:positive gravitropism; IMP:TAIR.
DR   CDD; cd17302; PIPKc_AtPIP5K_like; 1.
DR   Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR   Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 4.
DR   Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR017163; PIno-4-P-5_kinase_pln.
DR   InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR   InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR   InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR   InterPro; IPR023610; PInositol-4/5-P-5/4-kinase.
DR   PANTHER; PTHR23086:SF140; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 2; 1.
DR   PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 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   SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 1.
DR   SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR   PROSITE; PS51455; PIPK; 1.
DR   Genevisible; Q8L796; AT.
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
//