ITPK2_ARATH
ID ITPK2_ARATH Reviewed; 391 AA.
AC O81893; Q058I3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase 2;
DE EC=2.7.1.134 {ECO:0000269|PubMed:17698066};
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 2;
DE Short=AtItpk-2;
DE Short=Inositol-triphosphate 5/6-kinase 2;
DE Short=Ins(1,3,4)P(3) 5/6-kinase 2;
DE EC=2.7.1.159 {ECO:0000269|PubMed:17698066};
GN Name=ITPK2; OrderedLocusNames=At4g33770; ORFNames=T16L1.260;
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].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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). Plays a role in seed coat development and
CC lipid polyester barrier formation (PubMed:23595027).
CC {ECO:0000250|UniProtKB:Q13572, ECO:0000269|PubMed:17698066,
CC ECO:0000269|PubMed:23595027}.
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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O81893-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in seedling roots, cotyledons, rosette
CC leaves, cauline leaves, stems, flowers, siliques and seeds.
CC {ECO:0000269|PubMed:17698066, ECO:0000269|PubMed:23595027}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the seed coat of developing seeds
CC from 2 to 6 days after fertilization. {ECO:0000269|PubMed:23595027}.
CC -!- DISRUPTION PHENOTYPE: Distorted seed coat with reduced mucilage content
CC and decreased suberin and cutin composition. Crumpled columellas.
CC {ECO:0000269|PubMed:23595027}.
CC -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20590.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL031394; CAA20590.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80094.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86275.1; -; Genomic_DNA.
DR EMBL; BT029235; ABJ98567.1; -; mRNA.
DR PIR; T04994; T04994.
DR RefSeq; NP_195103.3; NM_119535.5. [O81893-1]
DR AlphaFoldDB; O81893; -.
DR SMR; O81893; -.
DR BioGRID; 14801; 1.
DR IntAct; O81893; 1.
DR STRING; 3702.AT4G33770.1; -.
DR PaxDb; O81893; -.
DR PRIDE; O81893; -.
DR ProteomicsDB; 238958; -. [O81893-1]
DR EnsemblPlants; AT4G33770.1; AT4G33770.1; AT4G33770. [O81893-1]
DR GeneID; 829519; -.
DR Gramene; AT4G33770.1; AT4G33770.1; AT4G33770. [O81893-1]
DR KEGG; ath:AT4G33770; -.
DR Araport; AT4G33770; -.
DR TAIR; locus:2134253; AT4G33770.
DR eggNOG; ENOG502QQS1; Eukaryota.
DR HOGENOM; CLU_041857_0_0_1; -.
DR InParanoid; O81893; -.
DR OrthoDB; 1116241at2759; -.
DR PhylomeDB; O81893; -.
DR BioCyc; ARA:AT4G33770-MON; -.
DR BRENDA; 2.7.1.134; 399.
DR BRENDA; 2.7.1.159; 399.
DR PRO; PR:O81893; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O81893; baseline and differential.
DR Genevisible; O81893; AT.
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:0010214; P:seed coat development; 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.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..391
FT /note="Inositol-tetrakisphosphate 1-kinase 2"
FT /id="PRO_0000220841"
FT DOMAIN 178..384
FT /note="ATP-grasp"
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 132
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 228
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 249..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 260
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 357
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
SQ SEQUENCE 391 AA; 44172 MW; 56BFA59FCCF0FC1A CRC64;
MFGTLASGEI ETARLNRNLG ITSNLGVSCG GFEDFAMRFE GENMVPYKGE EQEEEEDQVV
VNETTPFQFQ QPLFLQQQQK LVVGYALTSK KKKSFLQPKL ELLARRKGIF FVAIDLNRPL
SEQGPFDVVL HKLLGKEWEE VIEDYQQKHP EVTVLDPPGS IQRIYNRQSM LQGMADLKLS
DCSGSLFVPK QMVVLKDSAA SADAVVEAGL KFPLVAKPLW IDGTAKSHQL YLAYDRRSLA
ELDPPLVLQE FVNHGGVMFK VFVVGDVIKV MRRFSLPNVS NCEKAKVDGV FQFPRVSSAA
ASADNADLDP RVAELPPKPF LEALVKELRS LLGLRLFNID MIREHGSKNV FYVIDINYFP
GYGKLPDYEQ VFVDFFQNLA QVKYKKRQHC K
