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Database: UniProt
Entry: O81893
LinkDB: O81893
Original site: O81893 
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   16-JAN-2019, entry version 119.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   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
RT   reference 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
RT   (AtITPK4) is an outlier to a family of ATP-grasp fold proteins from
RT   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
RT   seed coat development.";
RL   Acta Biochim. Biophys. Sin. 45:549-560(2013).
CC   -!- FUNCTION: Kinase that can phosphorylate various inositol
CC       polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3.
CC       Phosphorylates Ins(3,4,5,6)P4 to form InsP5 (PubMed:17698066).
CC       This reaction is thought to have regulatory importance, since
CC       Ins(3,4,5,6)P4 is an inhibitor of plasma membrane Ca(2+)-activated
CC       Cl(-) channels, while Ins(1,3,4,5,6)P5 is not (By similarity).
CC       Also phosphorylates Ins(1,3,4)P3 or a racemic mixture of
CC       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
CC       (InsP6) pathway (By similarity). Plays a role in seed coat
CC       development and lipid polyester barrier formation
CC       (PubMed:23595027). {ECO:0000250|UniProtKB:Q13572,
CC       ECO:0000269|PubMed:17698066, 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-
CC         inositol 1,3,4,5-tetrakisphosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:13253, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57895, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216;
CC         EC=2.7.1.159; Evidence={ECO:0000269|PubMed:17698066};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-
CC         inositol 1,3,4,6-tetrakisphosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:20940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57660, ChEBI:CHEBI:58414, ChEBI:CHEBI:456216;
CC         EC=2.7.1.159; 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,
CC       rosette leaves, cauline leaves, stems, flowers, siliques and
CC       seeds. {ECO:0000269|PubMed:17698066, ECO:0000269|PubMed:23595027}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the seed coat of developing
CC       seeds from 2 to 6 days after fertilization.
CC       {ECO:0000269|PubMed:23595027}.
CC   -!- DISRUPTION PHENOTYPE: Distorted seed coat with reduced mucilage
CC       content and decreased suberin and cutin composition. Crumpled
CC       columellas. {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};
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   UniGene; At.31554; -.
DR   ProteinModelPortal; O81893; -.
DR   SMR; O81893; -.
DR   BioGrid; 14801; 1.
DR   IntAct; O81893; 1.
DR   STRING; 3702.AT4G33770.1; -.
DR   PaxDb; O81893; -.
DR   PRIDE; O81893; -.
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; ENOG410IHA6; Eukaryota.
DR   eggNOG; ENOG4110KIK; LUCA.
DR   HOGENOM; HOG000220790; -.
DR   InParanoid; O81893; -.
DR   KO; K00913; -.
DR   OrthoDB; 1116241at2759; -.
DR   PhylomeDB; O81893; -.
DR   BioCyc; ARA:AT4G33770-MONOMER; -.
DR   BRENDA; 2.7.1.159; 399.
DR   Reactome; R-ATH-1855167; Synthesis of pyrophosphates in the cytosol.
DR   Reactome; R-ATH-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR   Reactome; R-ATH-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:O81893; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O81893; baseline and differential.
DR   Genevisible; O81893; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   PANTHER; PTHR14217; PTHR14217; 1.
DR   Pfam; PF05770; Ins134_P3_kin; 1.
DR   PIRSF; PIRSF038186; ITPK; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Complete proteome; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN         1    391       Inositol-tetrakisphosphate 1-kinase 2.
FT                                /FTId=PRO_0000220841.
FT   DOMAIN      178    384       ATP-grasp.
FT   NP_BIND     249    260       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   COMPBIAS     50     56       Poly-Glu.
FT   METAL       340    340       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       355    355       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       355    355       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       357    357       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING      90     90       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     132    132       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     167    167       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     217    217       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     228    228       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     260    260       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     275    275       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     357    357       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
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
//
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