ITPK1_ARATH
ID ITPK1_ARATH Reviewed; 319 AA.
AC Q9SBA5; O81633;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase 1;
DE EC=2.7.1.134 {ECO:0000305};
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 1;
DE Short=AtItpk-1;
DE Short=Inositol-triphosphate 5/6-kinase 1;
DE Short=Ins(1,3,4)P(3) 5/6-kinase 1;
DE EC=2.7.1.159 {ECO:0000269|PubMed:9126335};
GN Name=ITPK1; OrderedLocusNames=At5g16760; ORFNames=F5E19.100;
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], AND ENZYME ACTIVITY.
RX PubMed=9126335; DOI=10.1006/bbrc.1997.6355;
RA Wilson M.P., Majerus P.W.;
RT "Characterization of a cDNA encoding Arabidopsis thaliana inositol 1,3,4-
RT trisphosphate 5/6-kinase.";
RL Biochem. Biophys. Res. Commun. 232:678-681(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Xue H., Mueller-Roeber B.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=21698461; DOI=10.1007/s00438-011-0631-2;
RA Kim S.I., Tai T.H.;
RT "Identification of genes necessary for wild-type levels of seed phytic acid
RT in Arabidopsis thaliana using a reverse genetics approach.";
RL Mol. Genet. Genomics 286:119-133(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=23595027; DOI=10.1093/abbs/gmt039;
RA Tang Y., Tan S., Xue H.;
RT "Arabidopsis inositol 1,3,4-trisphosphate 5/6 kinase 2 is required for seed
RT coat development.";
RL Acta Biochim. Biophys. Sin. 45:549-560(2013).
CC -!- FUNCTION: Kinase that can phosphorylate various inositol polyphosphate
CC such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4
CC at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to
CC have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of
CC plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5
CC is not (By similarity). Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6
CC to form Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate
CC (InsP6) pathway (PubMed:9126335). {ECO:0000250|UniProtKB:Q13572,
CC ECO:0000269|PubMed:9126335}.
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:0000269|PubMed:9126335};
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 siliques.
CC {ECO:0000269|PubMed:23595027}.
CC -!- DISRUPTION PHENOTYPE: Low inositol hexakisphosphate (phytate) levels in
CC seed tissue. {ECO:0000269|PubMed:21698461}.
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; AF080173; AAC28859.1; -; mRNA.
DR EMBL; AJ001753; CAA04976.1; -; mRNA.
DR EMBL; AL391147; CAC01840.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92334.1; -; Genomic_DNA.
DR EMBL; AY072156; AAL59978.1; -; mRNA.
DR EMBL; AY096412; AAM20052.1; -; mRNA.
DR EMBL; AY087024; AAM64585.1; -; mRNA.
DR PIR; JC5401; JC5401.
DR RefSeq; NP_197178.1; NM_121682.3.
DR AlphaFoldDB; Q9SBA5; -.
DR SMR; Q9SBA5; -.
DR STRING; 3702.AT5G16760.1; -.
DR iPTMnet; Q9SBA5; -.
DR PaxDb; Q9SBA5; -.
DR PRIDE; Q9SBA5; -.
DR ProteomicsDB; 232282; -.
DR DNASU; 831539; -.
DR EnsemblPlants; AT5G16760.1; AT5G16760.1; AT5G16760.
DR GeneID; 831539; -.
DR Gramene; AT5G16760.1; AT5G16760.1; AT5G16760.
DR KEGG; ath:AT5G16760; -.
DR Araport; AT5G16760; -.
DR TAIR; locus:2148990; AT5G16760.
DR eggNOG; ENOG502QQS1; Eukaryota.
DR HOGENOM; CLU_041857_0_0_1; -.
DR InParanoid; Q9SBA5; -.
DR OMA; CKPLIAY; -.
DR OrthoDB; 1116241at2759; -.
DR PhylomeDB; Q9SBA5; -.
DR BioCyc; ARA:AT5G16760-MON; -.
DR BioCyc; MetaCyc:AT5G16760-MON; -.
DR BRENDA; 2.7.1.134; 399.
DR BRENDA; 2.7.1.159; 399.
DR PRO; PR:Q9SBA5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9SBA5; baseline and differential.
DR Genevisible; Q9SBA5; AT.
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; IDA:TAIR.
DR GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IDA:TAIR.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0052746; P:inositol phosphorylation; IDA:TAIR.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:TAIR.
DR InterPro; IPR011761; ATP-grasp.
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.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..319
FT /note="Inositol-tetrakisphosphate 1-kinase 1"
FT /id="PRO_0000220839"
FT DOMAIN 99..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 18
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 60
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 156
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 177..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 188
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 290
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 197
FT /note="K -> Q (in Ref. 1; AAC28859)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 36220 MW; C5EE6F3E55288D1B CRC64;
MSDSIQERYL VGYALAAKKQ HSFIQPSLIE HSRQRGIDLV KLDPTKSLLE QGKLDCIIHK
LYDVYWKENL HEFREKCPGV PVIDLPEAIE RLHNRVSMLE VITQLRFPVS DSERFGVPEQ
VVVMDSSVLS GGGALGELKF PVIAKPLDAD GSAKSHKMFL IYDQEGMKIL KAPIVLQEFV
NHGGVIFKVY VVGDHVKCVK RRSLPDISEE KIGTSKGSLP FSQISNLTAQ EDKNIEYGED
RSLEKVEMPP LSFLTDLAKA MRESMGLNLF NFDVIRDAKD ANRYLIIDIN YFPGYAKMPS
YEPVLTEFFW DMVTKKNHV
