ITPK4_ARATH
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 03-AUG-2022, entry version 128.
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; 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=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., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis 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 reference
RT 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., 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 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 acid
RT 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 of
CC Ins(1,4,6)P3 and Ins(3,4,6)P3 to form InsP4. Does not display inositol
CC 3,4,5,6-tetrakisphosphate 1-kinase activity, but possesses inositol
CC 1,4,5,6-tetrakisphosphate and inositol 1,3,4,5-tetrakisphosphate
CC isomerase activity (PubMed:17698066). Ins(1,3,4,6)P4 is an essential
CC molecule in the hexakisphosphate (InsP6) pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q13572, 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 -!- 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) levels in
CC 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};
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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 AlphaFoldDB; O80568; -.
DR SMR; O80568; -.
DR BioGRID; 4339; 1.
DR STRING; 3702.AT2G43980.1; -.
DR PaxDb; O80568; -.
DR PRIDE; O80568; -.
DR ProteomicsDB; 238960; -.
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; ENOG502QQ6B; Eukaryota.
DR HOGENOM; CLU_041857_2_0_1; -.
DR InParanoid; O80568; -.
DR OMA; KMAIVFR; -.
DR OrthoDB; 1116241at2759; -.
DR PhylomeDB; O80568; -.
DR BioCyc; ARA:AT2G43980-MON; -.
DR BRENDA; 2.7.1.159; 399.
DR PRO; PR:O80568; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80568; baseline and differential.
DR Genevisible; O80568; 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: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.
DR PIRSF; PIRSF038163; ITPK_uncN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..488
FT /note="Inositol 1,3,4-trisphosphate 5/6-kinase 4"
FT /id="PRO_0000220842"
FT DOMAIN 246..488
FT /note="ATP-grasp"
FT BINDING 208
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 224
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 315
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 326
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 349..360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 360
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 439
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 455
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 459
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="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
