PI5K1_ARATH
ID PI5K1_ARATH Reviewed; 752 AA.
AC Q56YP2; O22503; O82120; Q9LM65;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase 1;
DE Short=AtPIP5K1;
DE EC=2.7.1.68;
DE AltName: Full=1-phosphatidylinositol 4-phosphate kinase 1;
DE AltName: Full=Diphosphoinositide kinase 1;
DE AltName: Full=PtdIns(4)P-5-kinase 1;
GN Name=PIP5K1; Synonyms=P5K1; OrderedLocusNames=At1g21980; ORFNames=F2E2.1;
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 STRAIN=cv. Columbia;
RA Satterlee J.S., Sussman M.R.;
RT "An Arabidopsis phosphatidylinositol-4-phosphate 5-kinase homolog with
RT seven novel repeats rich in aromatic and glycine residues.";
RL (er) Plant Gene Register PGR97-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9753781; DOI=10.1046/j.1365-313x.1998.00227.x;
RA Mikami K., Katagiri T., Iuchi S., Yamaguchi-Shinozaki K., Shinozaki K.;
RT "A gene encoding phosphatidylinositol-4-phosphate 5-kinase is induced by
RT water stress and abscisic acid in Arabidopsis thaliana.";
RL Plant J. 15:563-568(1998).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=11672432; DOI=10.1042/0264-6021:3590583;
RA Westergren T., Dove S.K., Sommarin M., Pical C.;
RT "AtPIP5K1, an Arabidopsis thaliana phosphatidylinositol phosphate kinase,
RT synthesizes PtdIns(3,4)P(2) and PtdIns(4,5)P(2) in vitro and is inhibited
RT by phosphorylation.";
RL Biochem. J. 359:583-589(2001).
RN [7]
RP CHARACTERIZATION, AND TISSUE SPECIFICITY.
RX PubMed=11489170; DOI=10.1046/j.1365-313x.2001.01051.x;
RA Elge S., Brearley C., Xia H.J., Kehr J., Xue H.W., Mueller-Roeber B.;
RT "An Arabidopsis inositol phospholipid kinase strongly expressed in
RT procambial cells: synthesis of PtdIns(4,5)P2 and PtdIns(3,4,5)P3 in insect
RT cells by 5-phosphorylation of precursors.";
RL Plant J. 26:561-571(2001).
RN [8]
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).
CC -!- FUNCTION: Catalyzes the synthesis of phosphatidylinositol 4,5-
CC bisphosphate and phosphatidylinositol 3,4-bisphosphate.
CC {ECO:0000269|PubMed:11672432}.
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 -!- TISSUE SPECIFICITY: Expressed in the whole plant, preferentially in
CC roots. Strongly expressed in meristematic tissues, namely procambial
CC cell layers. {ECO:0000269|PubMed:11489170, ECO:0000269|PubMed:9753781}.
CC -!- INDUCTION: By abscisic acid (ABA), drought and salt treatment.
CC {ECO:0000269|PubMed:9753781}.
CC -!- PTM: Phosphorylation inactivates the enzyme.
CC {ECO:0000269|PubMed:11672432}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86542.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA33501.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF019380; AAB82658.1; -; mRNA.
DR EMBL; AB005902; BAA33501.1; ALT_FRAME; mRNA.
DR EMBL; AC069252; AAF86542.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30181.1; -; Genomic_DNA.
DR EMBL; AK221279; BAD93975.1; -; mRNA.
DR PIR; T51821; T51821.
DR RefSeq; NP_173617.1; NM_102047.4.
DR AlphaFoldDB; Q56YP2; -.
DR SMR; Q56YP2; -.
DR BioGRID; 24040; 7.
DR STRING; 3702.AT1G21980.1; -.
DR iPTMnet; Q56YP2; -.
DR PaxDb; Q56YP2; -.
DR PRIDE; Q56YP2; -.
DR ProteomicsDB; 234910; -.
DR EnsemblPlants; AT1G21980.1; AT1G21980.1; AT1G21980.
DR GeneID; 838801; -.
DR Gramene; AT1G21980.1; AT1G21980.1; AT1G21980.
DR KEGG; ath:AT1G21980; -.
DR Araport; AT1G21980; -.
DR TAIR; locus:2201108; AT1G21980.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_4_1; -.
DR InParanoid; Q56YP2; -.
DR OMA; YSIGKHA; -.
DR OrthoDB; 212718at2759; -.
DR PhylomeDB; Q56YP2; -.
DR BioCyc; ARA:AT1G21980-MON; -.
DR BRENDA; 2.7.1.68; 399.
DR PRO; PR:Q56YP2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q56YP2; baseline and differential.
DR Genevisible; Q56YP2; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:TAIR.
DR GO; GO:0051015; F:actin filament binding; IDA:TAIR.
DR GO; GO:0003785; F:actin monomer binding; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016307; F:phosphatidylinositol phosphate kinase activity; IDA:TAIR.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Stress response; Transferase.
FT CHAIN 1..752
FT /note="Phosphatidylinositol 4-phosphate 5-kinase 1"
FT /id="PRO_0000185473"
FT REPEAT 81..103
FT /note="MORN 1"
FT REPEAT 104..126
FT /note="MORN 2"
FT REPEAT 127..149
FT /note="MORN 3"
FT REPEAT 150..172
FT /note="MORN 4"
FT REPEAT 173..195
FT /note="MORN 5"
FT REPEAT 196..218
FT /note="MORN 6"
FT REPEAT 219..241
FT /note="MORN 7"
FT DOMAIN 349..748
FT /note="PIPK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00781"
FT REGION 708..729
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT CONFLICT 182
FT /note="Q -> P (in Ref. 1; AAB82658)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="G -> S (in Ref. 1; AAB82658)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="S -> I (in Ref. 2; BAA33501)"
FT /evidence="ECO:0000305"
FT CONFLICT 416
FT /note="C -> Y (in Ref. 2; BAA33501)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="V -> M (in Ref. 2; BAA33501)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="F -> L (in Ref. 2; BAA33501)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="E -> D (in Ref. 2; BAA33501)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="H -> P (in Ref. 2; BAA33501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 752 AA; 85945 MW; 8A9E7D10A32CBF53 CRC64;
MSDSEEDEEE EEASEVILSS VVQKKKKKNL RFGEEVERRD GLVLLAQSTP MVRSRSQGTT
RRVTPTPLVD VEKPLPNGDL YIGSFSGGFP HGSGKYLWKD GCMYEGDWKR GKASGKGKFS
WPSGATYEGE FKSGRMEGFG TFTGADGDTY RGTWVADRKH GHGQKRYANG DFYEGTWRRN
LQDGRGRYVW RNGNQYTGEW RSGVISGKGL LVWPNGNRYE GLWENGIPKG NGVFTWSDGS
SCVGAWNESN IMRSFFNGVE KNDLIVGNRK RSSVDSGAGS LGGEKVFPRI CIWESDGEAG
DITCDIIDNV EASMIYRDRI SVDRDGFRQF KKNPCWFNGE AKKPGQTISK GHKKYDLMLN
LQLGIRYSVG KHASIVRDLK QTDFDPKEKF WTRFPPEGTK TTPPHQSVDF RWKDYCPLVF
RRLRELFQVD PAKYMLAICG NDALRELSSP GKSGSFFYLT QDDRFMIKTV KKSEVKVLLR
MLPSYYKHVC QYENSLVTRF YGVHCVKPVG GQKTRFIVMG NLFCSEYRIQ RRFDLKGSSH
GRSTAKPEGE IDETTTLKDL DLNFSFRLQR NWYQELMKQI KRDCEFLEAE RIMDYSLLVG
VHFRDDNTGE KMGLSPFVLR SGRIDSYQNE KFMRGCRFLE AELQDMDRIL AGRKPSIRLG
ANMPAKAERM ARRSDFDQYS SGGASYPSHG EMYEVVLYFG VIDILQDYDI TKKIEHAYKS
LQADPASISA VDPKLYSKRF RDFISRIFIE EG
