ID ITPK6_ORYSJ Reviewed; 547 AA.
AC Q0J0B2; A0A0P0XQ65; Q69IU4;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase 6 {ECO:0000305};
DE EC=2.7.1.134 {ECO:0000305};
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 6 {ECO:0000305};
DE Short=Inositol-triphosphate 5/6-kinase 6 {ECO:0000305};
DE Short=Ins(1,3,4)P(3) 5/6-kinase 6 {ECO:0000305};
DE Short=OsITP5/6K-6 {ECO:0000303|PubMed:17961936};
DE Short=OsITPK6 {ECO:0000303|PubMed:22038091};
DE EC=2.7.1.159 {ECO:0000305};
GN Name=ITPK6;
GN OrderedLocusNames=Os09g0518700 {ECO:0000312|EMBL:BAF25603.1},
GN LOC_Os09g34300 {ECO:0000305};
GN ORFNames=OSJNOa211K08.2 {ECO:0000312|EMBL:BAD54694.1},
GN P0498F03.7 {ECO:0000312|EMBL:BAD34407.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=17961936; DOI=10.1016/j.gene.2007.09.006;
RA Suzuki M., Tanaka K., Kuwano M., Yoshida K.T.;
RT "Expression pattern of inositol phosphate-related enzymes in rice (Oryza
RT sativa L.): implications for the phytic acid biosynthetic pathway.";
RL Gene 405:55-64(2007).
RN [6]
RP INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22038091; DOI=10.1007/s11103-011-9830-9;
RA Du H., Liu L., You L., Yang M., He Y., Li X., Xiong L.;
RT "Characterization of an inositol 1,3,4-trisphosphate 5/6-kinase gene that
RT is essential for drought and salt stress responses in rice.";
RL Plant Mol. Biol. 77:547-563(2011).
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. Phytic acid is the primary storage
CC form of phosphorus in cereal grains and other plant seeds.
CC {ECO:0000250|UniProtKB:Q84Y01}.
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:0000305};
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:0000305};
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:0000305};
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: Highly expressed in embryos and at lower levels in
CC roots, leaves, flowers and anthers. {ECO:0000269|PubMed:17961936}.
CC -!- INDUCTION: By drought stress. {ECO:0000269|PubMed:22038091}.
CC -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD34407.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD54694.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP006525; BAD34407.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP007254; BAD54694.1; ALT_INIT; Genomic_DNA.
DR EMBL; AP008215; BAF25603.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT08993.1; -; Genomic_DNA.
DR EMBL; AK102571; BAG95621.1; -; mRNA.
DR AlphaFoldDB; Q0J0B2; -.
DR SMR; Q0J0B2; -.
DR STRING; 39947.Q0J0B2; -.
DR PaxDb; 39947-Q0J0B2; -.
DR EnsemblPlants; Os09t0518700-01; Os09t0518700-01; Os09g0518700.
DR Gramene; Os09t0518700-01; Os09t0518700-01; Os09g0518700.
DR eggNOG; ENOG502QQ6B; Eukaryota.
DR InParanoid; Q0J0B2; -.
DR OMA; KMAIVFR; -.
DR BRENDA; 2.7.1.134; 8948.
DR BRENDA; 2.7.1.159; 8948.
DR PlantReactome; R-OSA-1119434; Phytic acid biosynthesis (lipid-independent).
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR ExpressionAtlas; Q0J0B2; baseline and differential.
DR Genevisible; Q0J0B2; OS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IBA:GO_Central.
DR GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IEA:EnsemblPlants.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
DR InterPro; IPR040464; InsP(3)kin_ATP-grasp.
DR PANTHER; PTHR14217; INOSITOL-TETRAKISPHOSPHATE 1-KINASE; 1.
DR PANTHER; PTHR14217:SF1; INOSITOL-TETRAKISPHOSPHATE 1-KINASE; 1.
DR Pfam; PF05770; Ins134_P3_kin; 1.
DR PIRSF; PIRSF038163; ITPK_uncN; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..547
FT /note="Inositol-tetrakisphosphate 1-kinase 6"
FT /id="PRO_0000431879"
FT DOMAIN 327..539
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 263
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 317
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 381
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 404..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 415
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 513
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 513
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 517
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
SQ SEQUENCE 547 AA; 60800 MW; 4A40E1D4E0847C94 CRC64;
MPSMRVTTDT WPRRAAQEPL LLLLLRSSLM KSASLQALNP NRAMAAMGRS VRVVLDSSVL
LDPSGVTAEE EEVVVALRPG AEALLRRLRY SNLRVAICHP EGLPTNESGF LEKTAKLYSF
GYMPLTSPSG SNLLNELMLE WSGTNFCFYV TSGVHEGLLS ELQNHNWEVI AMGNEDVIKN
SGVIHISMLQ ELLITLATSI KKEIGNSSAF VVGYVMKQSR EEDFAKRGAF PIYPSKNDLI
FVPLSFELPL ASQLQEVDLV LHKITDEIIN IDPNSSISFP KGISFSPGMS EIIRFVEEHC
DFCVIDPFKN IYPLLDRIQI QEILIRLEGL SAEGRPKLRA PCFLKIESFC GSELQKQLAE
AKLSFPLIVK PQVACGVADA HNMALIFKIE EFSNLSVPLP AILQEYIDHG SKIFKFYAIG
DKIFHAIKNS MPNASHLKSS SGGKPLTFNS LKTLPVATKE QLLQNEVQDS KLLDINLVEE
AAKLLKELLG LTIFGFDVVV QESSGDHVIV DLNYLPSFKE VPDNVAMPAF WDAIKQSYES
RKQMTQT
//
