ITPK1_MAIZE
ID ITPK1_MAIZE Reviewed; 342 AA.
AC Q84Y01;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase 1 {ECO:0000303|PubMed:12586875};
DE Short=ZmIpk {ECO:0000303|PubMed:12586875};
DE EC=2.7.1.134 {ECO:0000269|PubMed:12586875};
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 1 {ECO:0000303|PubMed:12586875};
DE Short=Inositol-triphosphate 5/6-kinase 1 {ECO:0000303|PubMed:12586875};
DE Short=Ins(1,3,4)P(3) 5/6-kinase 1 {ECO:0000303|PubMed:12586875};
DE EC=2.7.1.159 {ECO:0000269|PubMed:12586875};
DE AltName: Full=Low phytic acid protein 2 {ECO:0000303|PubMed:12586875};
GN Name=ITPK1 {ECO:0000303|PubMed:12586875};
GN Synonyms=LPA2 {ECO:0000303|PubMed:12586875};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=12586875; DOI=10.1104/pp.014258;
RA Shi J., Wang H., Wu Y., Hazebroek J., Meeley R.B., Ertl D.S.;
RT "The maize low-phytic acid mutant lpa2 is caused by mutation in an inositol
RT phosphate kinase gene.";
RL Plant Physiol. 131:507-515(2003).
CC -!- FUNCTION: Kinase that can phosphorylate various inositol polyphosphate
CC such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3 and participates in phytic acid
CC biosynthesis in developing seeds. Phosphorylates Ins(3,4,5,6)P4 at
CC position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to have
CC regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma
CC membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5 is
CC not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form
CC Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6)
CC pathway. Also able to phosphorylate Ins(3,5,6)P3 but not Ins(1,4,5)P3,
CC Ins(2,4,5)P3, Ins(1,3,4,6)P4 nor Ins(1,3,5,6)P4. Has higher specific
CC activity on Ins(3,4,5,6)P4 than Ins(1,3,4)P3 and Ins(3,5,6)P3. Can also
CC could use Ins(1,2,5,6)P4 as a substrate. {ECO:0000269|PubMed:12586875}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-
CC inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216;
CC EC=2.7.1.134; Evidence={ECO:0000269|PubMed:12586875};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159;
CC Evidence={ECO:0000269|PubMed:12586875};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660,
CC ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159;
CC Evidence={ECO:0000269|PubMed:12586875};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:Q13572};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q13572}.
CC -!- TISSUE SPECIFICITY: Expressed in the embryo of 15 day after
CC pollination. Expressed in kernels at earlier stages but at very low
CC levels. Expression in the embryo peaks at 15 days after pollination and
CC then declines. No expression is detected from endosperm and vegetative
CC tissues. {ECO:0000269|PubMed:12586875}.
CC -!- DISRUPTION PHENOTYPE: Plants display reduced phytic acid content in
CC seeds. {ECO:0000269|PubMed:12586875}.
CC -!- SIMILARITY: Belongs to the ITPK1 family. {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; AY172635; AAO17299.1; -; mRNA.
DR RefSeq; NP_001105901.1; NM_001112431.1.
DR AlphaFoldDB; Q84Y01; -.
DR SMR; Q84Y01; -.
DR STRING; 4577.GRMZM2G456626_P01; -.
DR PaxDb; Q84Y01; -.
DR EnsemblPlants; Zm00001eb024800_T001; Zm00001eb024800_P001; Zm00001eb024800.
DR GeneID; 732818; -.
DR Gramene; Zm00001eb024800_T001; Zm00001eb024800_P001; Zm00001eb024800.
DR KEGG; zma:732818; -.
DR MaizeGDB; 301214; -.
DR eggNOG; ENOG502QQS1; Eukaryota.
DR HOGENOM; CLU_041857_0_0_1; -.
DR OMA; CKPLIAY; -.
DR OrthoDB; 1116241at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q84Y01; baseline and differential.
DR Genevisible; Q84Y01; ZM.
DR GO; GO:0005524; F:ATP binding; IC:AgBase.
DR GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IDA:UniProtKB.
DR GO; GO:0000825; F:inositol tetrakisphosphate 6-kinase activity; IDA:AgBase.
DR GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; TAS:AgBase.
DR GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IDA:UniProtKB.
DR GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0048316; P:seed development; IMP:AgBase.
DR InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
DR InterPro; IPR040464; InsP(3)kin_ATP-grasp.
DR InterPro; IPR041429; ITPK1_N.
DR PANTHER; PTHR14217; PTHR14217; 1.
DR Pfam; PF05770; Ins134_P3_kin; 1.
DR Pfam; PF17927; Ins134_P3_kin_N; 1.
DR PIRSF; PIRSF038186; ITPK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..342
FT /note="Inositol-tetrakisphosphate 1-kinase 1"
FT /id="PRO_0000220843"
FT DOMAIN 116..332
FT /note="ATP-grasp"
FT /evidence="ECO:0000255"
FT BINDING 28
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 70
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 166
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 187..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 198
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 299
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
SQ SEQUENCE 342 AA; 37313 MW; F24DEB3FEBEE6F3C CRC64;
MASDAAAEPS SGVTHPPRYV IGYALAPKKQ QSFIQPSLVA QAASRGMDLV PVDASQPLAE
QGPFHLLIHK LYGDDWRAQL VAFAARHPAV PIVDPPHAID RLHNRISMLQ VVSELDHAAD
QDSTFGIPSQ VVVYDAAALA DFGLLAALRF PLIAKPLVAD GTAKSHKMSL VYHREGLGKL
RPPLVLQEFV NHGGVIFKVY VVGGHVTCVK RRSLPDVSPE DDASAQGSVS FSQVSNLPTE
RTAEEYYGEK SLEDAVVPPA AFINQIAGGL RRALGLQLFN FDMIRDVRAG DRYLVIDINY
FPGYAKMPGY ETVLTDFFWE MVHKDGVGNQ QEEKGANHVV VK
