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Database: UniProt
Entry: O80568
LinkDB: O80568
Original site: O80568 
ID   ITPK4_ARATH             Reviewed;         488 AA.
AC   O80568; Q8VYL6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   13-FEB-2019, entry version 115.
DE   RecName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 4;
DE            Short=AtItpk-4;
DE            Short=Inositol-triphosphate 5/6-kinase 4;
DE            Short=Ins(1,3,4)P(3) 5/6-kinase 4;
DE            EC=2.7.1.159 {ECO:0000269|PubMed:17698066};
DE   AltName: Full=Inositol-tetrakisphosphate 1-kinase 4;
GN   Name=ITPK4; OrderedLocusNames=At2g43980; ORFNames=F6E13.11;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(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;
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   [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   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).
CC   -!- FUNCTION: Kinase that can phosphorylate the inositol polyphosphate
CC       Ins(1,3,4)P3 to form InsP4. Also phosphorylates a racemic mixture
CC       of Ins(1,4,6)P3 and Ins(3,4,6)P3 to form InsP4. Does not display
CC       inositol 3,4,5,6-tetrakisphosphate 1-kinase activity, but
CC       possesses inositol 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-
CC       tetrakisphosphate isomerase activity (PubMed:17698066).
CC       Ins(1,3,4,6)P4 is an essential molecule in the hexakisphosphate
CC       (InsP6) pathway (By similarity). {ECO:0000250|UniProtKB:Q13572,
CC       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   -!- TISSUE SPECIFICITY: Expressed in roots, leaf vasculature, cauline
CC       leaves, flower buds and siliques. {ECO:0000269|PubMed:17698066}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC23406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AC004005; AAC23406.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC10358.1; -; Genomic_DNA.
DR   EMBL; AY070449; AAL49852.1; -; mRNA.
DR   EMBL; AY096566; AAM20216.1; -; mRNA.
DR   PIR; T00678; T00678.
DR   RefSeq; NP_850407.1; NM_180076.2.
DR   UniGene; At.28352; -.
DR   ProteinModelPortal; O80568; -.
DR   SMR; O80568; -.
DR   BioGrid; 4339; 1.
DR   STRING; 3702.AT2G43980.1; -.
DR   PaxDb; O80568; -.
DR   PRIDE; O80568; -.
DR   EnsemblPlants; AT2G43980.1; AT2G43980.1; AT2G43980.
DR   GeneID; 819003; -.
DR   Gramene; AT2G43980.1; AT2G43980.1; AT2G43980.
DR   KEGG; ath:AT2G43980; -.
DR   Araport; AT2G43980; -.
DR   TAIR; locus:2051744; AT2G43980.
DR   eggNOG; ENOG410II4S; Eukaryota.
DR   eggNOG; ENOG4110UUV; LUCA.
DR   HOGENOM; HOG000070545; -.
DR   InParanoid; O80568; -.
DR   KO; K01765; -.
DR   OMA; CFLKIDS; -.
DR   OrthoDB; 1116241at2759; -.
DR   PhylomeDB; O80568; -.
DR   BioCyc; ARA:AT2G43980-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:O80568; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80568; baseline and differential.
DR   Genevisible; O80568; 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; 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:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:TAIR.
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.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN         1    488       Inositol 1,3,4-trisphosphate 5/6-kinase
FT                                4.
FT                                /FTId=PRO_0000220842.
FT   DOMAIN      246    488       ATP-grasp.
FT   NP_BIND     349    360       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       439    439       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       453    453       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       453    453       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   METAL       455    455       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     208    208       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     224    224       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     263    263       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     315    315       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     326    326       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     360    360       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     375    375       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     398    398       ATP. {ECO:0000250|UniProtKB:Q13572}.
FT   BINDING     455    455       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
FT   BINDING     459    459       1D-myo-inositol 1,3,4-trisphosphate.
FT                                {ECO:0000250|UniProtKB:Q9XYQ1}.
SQ   SEQUENCE   488 AA;  54180 MW;  CB540875BD23C911 CRC64;
     MKGVLLDESV LFSPESEDSS PSLRESVPSL LRLLRYSMIR TGISYGLDLP ENKVDLLRKT
     AAEYSINCLP LETSLTSVTF GDTLKAWYSD GSILYVASSR KEEILRELSP SQLVVLLDVE
     GDSLEDPNII HIHSLEELPM TICCINKKAM GDGAAIVAYI MKPSRVEDFA KRGALPMYPT
     SCGLIFLPLM FEFPLASQLK HADIIFHKAT DEILSIELNC SDSKSSVAVT FSTGMEKLKK
     YMEDQNACAI VDPIRNIYPV VDRLKMQHIL LGLEGLGAAG RKIRGACFLK IDSYDEPDLA
     QNLSRAGLSL PCIVKPQVAC GVADAHSMAI VFRVEDFKNL NTPVPAIIQE YVDHSSRIFK
     FYVLGETIFH AVKKSIPSSS SLRKSAEENG LKPILFDSLK SLPVDSANQN PVSEIDLELV
     TEAATWLRKK LDLTIFGFDV VIQEGTGDHV IVDLNYLPSF KEVPDNIAVP AFWEAIRNRF
     DQHVQEKH
//
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