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Inositol-tetrakisphosphate 1-kinase 1 (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase 1) (Inositol-triphosphate 5/6-kinase 1) (Ins(1,3,4)P(3) 5/6-kinase 1) (EC 2.7.1.159) (Low phytic acid protein 2) (ZmIpk)

 ITPK1_MAIZE             Reviewed;         342 AA.
Q84Y01;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
10-OCT-2018, entry version 86.
RecName: Full=Inositol-tetrakisphosphate 1-kinase 1;
EC=2.7.1.134;
AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 1;
Short=Inositol-triphosphate 5/6-kinase 1;
Short=Ins(1,3,4)P(3) 5/6-kinase 1;
EC=2.7.1.159;
AltName: Full=Low phytic acid protein 2;
AltName: Full=ZmIpk;
Name=ITPK1; Synonyms=LPA2;
Zea mays (Maize).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae;
PACMAD clade; Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae;
Zea.
NCBI_TaxID=4577;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=12586875; DOI=10.1104/pp.014258;
Shi J., Wang H., Wu Y., Hazebroek J., Meeley R.B., Ertl D.S.;
"The maize low-phytic acid mutant lpa2 is caused by mutation in an
inositol phosphate kinase gene.";
Plant Physiol. 131:507-515(2003).
-!- FUNCTION: Kinase that can phosphorylate various inositol
polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3 and
participates in phytic acid biosynthesis in developing seeds.
Phosphorylates Ins(3,4,5,6)P4 at position 1 to form
Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory
importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma
membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5
is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form
Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate
(InsP6) pathway. Also able to phosphorylate Ins(3,5,6)P3 but not
Ins(1,4,5)P3, Ins(2,4,5)P3, Ins(1,3,4,6)P4 nor Ins(1,3,5,6)P4. Has
higher specific activity on Ins(3,4,5,6)P4 than Ins(1,3,4)P3 and
Ins(3,5,6)P3. Can also could use Ins(1,2,5,6)P4 as a substrate.
{ECO:0000269|PubMed:12586875}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 3,4,5,6-
tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-
pentakisphosphate.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4-trisphosphate =
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4-trisphosphate =
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in the embryo of 15 day after
pollination. Expressed in kernels at earlier stages but at very
low levels. Expression in the embryo peaks at 15 days after
pollination and then declines. No expression is detected from
endosperm and vegetative tissues. {ECO:0000269|PubMed:12586875}.
-!- DISRUPTION PHENOTYPE: Plants display reduced phytic acid content
in seeds. {ECO:0000269|PubMed:12586875}.
-!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
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EMBL; AY172635; AAO17299.1; -; mRNA.
RefSeq; NP_001105901.1; NM_001112431.1.
UniGene; Zm.13384; -.
ProteinModelPortal; Q84Y01; -.
SMR; Q84Y01; -.
STRING; 4577.GRMZM2G456626_P01; -.
PaxDb; Q84Y01; -.
PRIDE; Q84Y01; -.
EnsemblPlants; Zm00001d030083_T001; Zm00001d030083_P001; Zm00001d030083.
GeneID; 732818; -.
Gramene; Zm00001d030083_T001; Zm00001d030083_P001; Zm00001d030083.
KEGG; zma:732818; -.
MaizeGDB; 301214; -.
eggNOG; ENOG410IHA6; Eukaryota.
eggNOG; ENOG4110KIK; LUCA.
HOGENOM; HOG000220790; -.
KO; K00913; -.
OMA; MQDERIC; -.
OrthoDB; EOG09360FFG; -.
Proteomes; UP000007305; Chromosome 1.
ExpressionAtlas; Q84Y01; baseline and differential.
Genevisible; Q84Y01; ZM.
GO; GO:0005829; C:cytosol; IEA:EnsemblPlants.
GO; GO:0005524; F:ATP binding; IC:AgBase.
GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IDA:UniProtKB.
GO; GO:0000825; F:inositol tetrakisphosphate 6-kinase activity; IDA:AgBase.
GO; GO:0051717; F:inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity; TAS:AgBase.
GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IDA:UniProtKB.
GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0052746; P:inositol phosphorylation; IEA:EnsemblPlants.
GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:UniProtKB.
GO; GO:0048316; P:seed development; IMP:AgBase.
InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
PANTHER; PTHR14217; PTHR14217; 1.
Pfam; PF05770; Ins134_P3_kin; 1.
PIRSF; PIRSF038186; ITPK; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Reference proteome; Transferase.
CHAIN 1 342 Inositol-tetrakisphosphate 1-kinase 1.
/FTId=PRO_0000220843.
DOMAIN 116 332 ATP-grasp.
NP_BIND 187 198 ATP. {ECO:0000250|UniProtKB:Q13572}.
METAL 282 282 Magnesium 1.
{ECO:0000250|UniProtKB:Q13572}.
METAL 297 297 Magnesium 1.
{ECO:0000250|UniProtKB:Q13572}.
METAL 297 297 Magnesium 2.
{ECO:0000250|UniProtKB:Q13572}.
METAL 299 299 Magnesium 2.
{ECO:0000250|UniProtKB:Q13572}.
BINDING 28 28 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250|UniProtKB:Q9XYQ1}.
BINDING 70 70 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250|UniProtKB:Q9XYQ1}.
BINDING 105 105 ATP. {ECO:0000250|UniProtKB:Q13572}.
BINDING 155 155 ATP. {ECO:0000250|UniProtKB:Q13572}.
BINDING 166 166 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250|UniProtKB:Q9XYQ1}.
BINDING 198 198 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250|UniProtKB:Q9XYQ1}.
BINDING 213 213 ATP. {ECO:0000250|UniProtKB:Q13572}.
BINDING 299 299 1D-myo-inositol 1,3,4-trisphosphate.
{ECO:0000250|UniProtKB:Q9XYQ1}.
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


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