ITPK3_ARATH
ID ITPK3_ARATH Reviewed; 353 AA.
AC Q9SUG3; Q3EA71; Q93VQ8;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase 3;
DE EC=2.7.1.134 {ECO:0000269|PubMed:17698066};
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 3;
DE Short=AtItpk-3;
DE Short=Inositol-triphosphate 5/6-kinase 3;
DE Short=Ins(1,3,4)P(3) 5/6-kinase 3;
DE EC=2.7.1.159 {ECO:0000269|PubMed:17698066};
GN Name=ITPK3; OrderedLocusNames=At4g08170; ORFNames=T12G13.10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=17698066; DOI=10.1016/j.febslet.2007.07.046;
RA Sweetman D., Stavridou I., Johnson S., Green P., Caddick S.E.,
RA Brearley C.A.;
RT "Arabidopsis thaliana inositol 1,3,4-trisphosphate 5/6-kinase 4 (AtITPK4)
RT is an outlier to a family of ATP-grasp fold proteins from Arabidopsis.";
RL FEBS Lett. 581:4165-4171(2007).
RN [5]
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 to form InsP5 (PubMed:17698066). 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 not
CC (By similarity). Also phosphorylates Ins(1,3,4)P3 or a racemic mixture
CC of Ins(1,4,6)P3 and Ins(3,4,6)P3 to form InsP4 (PubMed:17698066).
CC Ins(1,3,4,6)P4 is an essential molecule in the hexakisphosphate (InsP6)
CC pathway (By similarity). {ECO:0000250|UniProtKB:Q13572,
CC ECO:0000269|PubMed:17698066}.
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:17698066};
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:17698066};
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:17698066};
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SUG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SUG3-2; Sequence=VSP_018095, VSP_018096;
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves and flowers, and at
CC lower levels in roots, stems, cauline leaves and siliques.
CC {ECO:0000269|PubMed:17698066, ECO:0000269|PubMed:23595027}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45787.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81153.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL080252; CAB45787.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161510; CAB81153.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82601.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82602.1; -; Genomic_DNA.
DR EMBL; AY050408; AAK91424.1; -; mRNA.
DR EMBL; AY058241; AAL15415.1; -; mRNA.
DR PIR; T10544; T10544.
DR RefSeq; NP_001319879.1; NM_001340572.1. [Q9SUG3-2]
DR RefSeq; NP_567334.1; NM_116886.3. [Q9SUG3-1]
DR AlphaFoldDB; Q9SUG3; -.
DR SMR; Q9SUG3; -.
DR BioGRID; 11667; 4.
DR STRING; 3702.AT4G08170.2; -.
DR PaxDb; Q9SUG3; -.
DR PRIDE; Q9SUG3; -.
DR ProteomicsDB; 238959; -. [Q9SUG3-1]
DR EnsemblPlants; AT4G08170.1; AT4G08170.1; AT4G08170. [Q9SUG3-2]
DR EnsemblPlants; AT4G08170.2; AT4G08170.2; AT4G08170. [Q9SUG3-1]
DR GeneID; 826367; -.
DR Gramene; AT4G08170.1; AT4G08170.1; AT4G08170. [Q9SUG3-2]
DR Gramene; AT4G08170.2; AT4G08170.2; AT4G08170. [Q9SUG3-1]
DR KEGG; ath:AT4G08170; -.
DR Araport; AT4G08170; -.
DR TAIR; locus:2132487; AT4G08170.
DR eggNOG; ENOG502QQS1; Eukaryota.
DR HOGENOM; CLU_041857_0_0_1; -.
DR InParanoid; Q9SUG3; -.
DR OMA; QHLYNRQ; -.
DR OrthoDB; 1116241at2759; -.
DR PhylomeDB; Q9SUG3; -.
DR BioCyc; ARA:AT4G08170-MON; -.
DR BRENDA; 2.7.1.134; 399.
DR BRENDA; 2.7.1.159; 399.
DR PRO; PR:Q9SUG3; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUG3; baseline and differential.
DR Genevisible; Q9SUG3; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IDA:UniProtKB.
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:0009611; P:response to wounding; IEP: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 Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..353
FT /note="Inositol-tetrakisphosphate 1-kinase 3"
FT /id="PRO_0000220840"
FT DOMAIN 138..350
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 92
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 177
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 209..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 220
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 317
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018095"
FT VAR_SEQ 89..92
FT /note="VLHK -> MYWQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018096"
SQ SEQUENCE 353 AA; 39631 MW; 92C707E500D6EF90 CRC64;
MKLTDNEEIT MNGTREMETT EQETSSPCSL VIEAFPVKKS IIVGYALTSK KIKSFLQPKL
EGLARNKGIL FVAIDQNKPL SEQGPFDIVL HKQIGKEWRR ILEEFRLAHP DVTVLDPPDA
ILHLRNRQSM LQCVADMNLS DSNGRVGVPK QLVIKKDASS IPEAVNNAGL RLPLVAKPLV
ADGSAKSHEL SLAYDQHSLL KLEPPLVLQE FVNHGGVLFK VYIVGEAIRV VRRFSLPDVS
RRELPKSAGV FRFPRVSCAA ASADDADLDP SIAELPPRPL LERLAKELRR GLGLRLFNLD
IIREHGTRDR FYVIDINYFP GYGKMPEYEH VFTDFLLSVV QSQCKKRALA DQY
