ITPK2_ORYSJ
ID ITPK2_ORYSJ Reviewed; 349 AA.
AC Q10PL5; A0A0P0VUY1; A1KXK8; B9F6M0; Q8GSI5;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase 2 {ECO:0000305};
DE EC=2.7.1.134 {ECO:0000305};
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 2 {ECO:0000305};
DE Short=Inositol-triphosphate 5/6-kinase 2 {ECO:0000305};
DE Short=Ins(1,3,4)P(3) 5/6-kinase 2 {ECO:0000305};
DE Short=OsITP5/6K-2 {ECO:0000303|PubMed:17961936};
DE Short=OsITPK2 {ECO:0000303|PubMed:22038091};
DE EC=2.7.1.159 {ECO:0000305};
DE AltName: Full=OsITL1 {ECO:0000303|PubMed:18421420};
DE AltName: Full=Protein DROUGHT- AND SALT-SENSITIVE MUTANT 3 {ECO:0000303|PubMed:22038091};
DE Short=OsDSM3 {ECO:0000303|PubMed:22038091};
GN Name=ITPK2;
GN Synonyms=DSM3 {ECO:0000303|PubMed:22038091},
GN ITL1 {ECO:0000303|PubMed:18421420};
GN OrderedLocusNames=Os03g0230500 {ECO:0000312|EMBL:BAF11371.1},
GN LOC_Os03g12840 {ECO:0000312|EMBL:ABF94780.1};
GN ORFNames=OJ1017C11.3 {ECO:0000312|EMBL:AAO00682.1},
GN OJ1781E12.6 {ECO:0000312|EMBL:AAO06958.1},
GN OsJ_10020 {ECO:0000312|EMBL:EEE58643.1};
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 [MRNA], FUNCTION, AND INDUCTION.
RC STRAIN=cv. Zhongzuo-93;
RX PubMed=18421420; DOI=10.1007/s10529-008-9730-5;
RA Niu X., Chen Q., Wang X.;
RT "OsITL1 gene encoding an inositol 1,3,4-trisphosphate 5/6-kinase is a
RT negative regulator of osmotic stress signaling.";
RL Biotechnol. Lett. 30:1687-1692(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, GENE FAMILY, AND
RP 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 (By
CC similarity). May be involved in the negative regulation of osmotic
CC stress signaling (PubMed:18421420, PubMed:22038091).
CC {ECO:0000250|UniProtKB:Q84Y01, ECO:0000269|PubMed:18421420,
CC ECO:0000269|PubMed:22038091}.
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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:22038091}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, flowers, anthers and
CC embryos. {ECO:0000269|PubMed:17961936}.
CC -!- INDUCTION: By drought and salt stresses. {ECO:0000269|PubMed:18421420}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show increased sensitivity to salt and
CC drought stresses. {ECO:0000269|PubMed:22038091}.
CC -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO00682.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAO06958.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY323825; AAQ02374.1; -; mRNA.
DR EMBL; AC105927; AAO06958.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC135157; AAO00682.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF94780.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11371.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83098.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE58643.1; -; Genomic_DNA.
DR EMBL; AK100971; BAG94858.1; -; mRNA.
DR RefSeq; XP_015632763.1; XM_015777277.1.
DR AlphaFoldDB; Q10PL5; -.
DR SMR; Q10PL5; -.
DR STRING; 4530.OS03T0230500-01; -.
DR PaxDb; Q10PL5; -.
DR PRIDE; Q10PL5; -.
DR EnsemblPlants; Os03t0230500-01; Os03t0230500-01; Os03g0230500.
DR GeneID; 4332146; -.
DR Gramene; Os03t0230500-01; Os03t0230500-01; Os03g0230500.
DR KEGG; osa:4332146; -.
DR eggNOG; ENOG502QQS1; Eukaryota.
DR HOGENOM; CLU_041857_0_0_1; -.
DR InParanoid; Q10PL5; -.
DR OMA; FLAYDQC; -.
DR OrthoDB; 1116241at2759; -.
DR BRENDA; 2.7.1.159; 4460.
DR PlantReactome; R-OSA-1119434; Phytic acid biosynthesis (lipid-independent).
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q10PL5; OS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0047484; P:regulation of response to osmotic stress; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Endoplasmic reticulum; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..349
FT /note="Inositol-tetrakisphosphate 1-kinase 2"
FT /id="PRO_0000431871"
FT BINDING 48
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 90
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 186
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 207..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 218
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 315
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT CONFLICT 20
FT /note="P -> Q (in Ref. 6; EEE58643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38800 MW; 6759CDB676A83E67 CRC64;
MRLHGEVSFD EDEEEVVMVP AAALSSSPLN GGAVPVTRLV VGYALTKKKV KSFLQPNLLL
LARKKGINLV AIDDTRPLAE QGPFDVILHK ITSKEWQQVL EDYHEEHPEV TVLDPPNAIN
HLNNRQSMLA EVSDLNLSSF YGEVCTPRQL VIMRDPSSIP TAVAMAGLTL PLVAKPLVVD
GTSKSHELSL AYDEASLSML DPPLVLQEFV NHGGILFKVY IIGETIQVVR RFSLPDVNTY
DLLNNVGVYR FPRVSCAAAS ADHADLDPHI SELPPRPLLE KLGKELRGRL GLRLFNIDMI
RELGTKDRYY IIDINYFPGF GKMPGYEHIF TDFLLNLAQS KYKKCLSGG
