GenomeNet

Database: UniProt
Entry: Q9SBA5
LinkDB: Q9SBA5
Original site: Q9SBA5 
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   16-JAN-2019, entry version 115.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   1,3,4-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.,
RA   Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
RA   Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
RA   Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
RA   Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
RA   Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
RA   Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
RA   Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
RA   Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
RA   Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
RA   Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
RA   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.,
RA   Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
RA   Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
RA   van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
RA   Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
RA   Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
RA   Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   acid 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
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., 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
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 at position 1 to form
CC       Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory
CC       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
CC       is not (By similarity). Also phosphorylates Ins(1,3,4)P3 on O-5
CC       and O-6 to form Ins(1,3,4,6)P4, an essential molecule in the
CC       hexakisphosphate (InsP6) pathway (PubMed:9126335).
CC       {ECO:0000250|UniProtKB:Q13572, 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-
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:0000305};
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: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)
CC       levels in seed tissue. {ECO:0000269|PubMed:21698461}.
CC   -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
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   UniGene; At.5370; -.
DR   ProteinModelPortal; Q9SBA5; -.
DR   STRING; 3702.AT5G16760.1; -.
DR   iPTMnet; Q9SBA5; -.
DR   PaxDb; Q9SBA5; -.
DR   PRIDE; Q9SBA5; -.
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; ENOG410IHA6; Eukaryota.
DR   eggNOG; ENOG4110KIK; LUCA.
DR   HOGENOM; HOG000220790; -.
DR   InParanoid; Q9SBA5; -.
DR   KO; K00913; -.
DR   OMA; MQDERIC; -.
DR   OrthoDB; 1116241at2759; -.
DR   PhylomeDB; Q9SBA5; -.
DR   BioCyc; ARA:AT5G16760-MONOMER; -.
DR   BioCyc; MetaCyc:AT5G16760-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:Q9SBA5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9SBA5; baseline and differential.
DR   Genevisible; Q9SBA5; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
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   PANTHER; PTHR14217; PTHR14217; 1.
DR   Pfam; PF05770; Ins134_P3_kin; 1.
DR   PIRSF; PIRSF038186; ITPK; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Complete proteome; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895}.
FT   CHAIN         2    319       Inositol-tetrakisphosphate 1-kinase 1.
FT                                /FTId=PRO_0000220839.
FT   DOMAIN       99    318       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     177    188       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       273    273       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       288    288       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       288    288       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       290    290       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING      18     18       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING      60     60       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING      95     95       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     145    145       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     156    156       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     188    188       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     203    203       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     290    290       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:22223895}.
FT   CONFLICT    197    197       K -> Q (in Ref. 1; AAC28859).
FT                                {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
//
DBGET integrated database retrieval system