IPMKB_ARATH
ID IPMKB_ARATH Reviewed; 300 AA.
AC Q9FLT2; Q8LDQ5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Inositol polyphosphate multikinase beta;
DE EC=2.7.1.140;
DE EC=2.7.1.151;
DE AltName: Full=Inositol polyphosphate 6-/3-/5-kinase beta;
DE Short=AtIpk2-beta;
DE Short=AtIpk2beta;
GN Name=IPK2b; Synonyms=IP3K, IPMK; OrderedLocusNames=At5g61760;
GN ORFNames=MAC9.7, MAC9_60;
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 [MRNA], MUTAGENESIS OF ASP-100, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=12226109; DOI=10.1074/jbc.m209112200;
RA Stevenson-Paulik J., Odom A.R., York J.D.;
RT "Molecular and biochemical characterization of two plant inositol
RT polyphosphate 6-/3-/5-kinases.";
RL J. Biol. Chem. 277:42711-42718(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=12566584; DOI=10.1105/tpc.006676;
RA Xia H.-J., Brearley C., Elge S., Kaplan B., Fromm H., Mueller-Roeber B.;
RT "Arabidopsis inositol polyphosphate 6-/3-kinase is a nuclear protein that
RT complements a yeast mutant lacking a functional ArgR-Mcm1 transcription
RT complex.";
RL Plant Cell 15:449-463(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 reference
RT 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., 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 [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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16107538; DOI=10.1073/pnas.0504172102;
RA Stevenson-Paulik J., Bastidas R.J., Chiou S.-T., Frye R.A., York J.D.;
RT "Generation of phytate-free seeds in Arabidopsis through disruption of
RT inositol polyphosphate kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12612-12617(2005).
RN [8]
RP FUNCTION, AND INDUCTION BY AUXIN.
RX PubMed=17434984; DOI=10.1104/pp.106.092163;
RA Zhang Z.-B., Yang G., Arana F., Chen Z., Li Y., Xia H.-J.;
RT "Arabidopsis inositol polyphosphate 6-/3-kinase (AtIpk2beta) is involved in
RT axillary shoot branching via auxin signaling.";
RL Plant Physiol. 144:942-951(2007).
RN [9]
RP DISRUPTION PHENOTYPE, INTERACTION WITH KIN10 AND KIN11, PHOSPHORYLATION,
RP AND ACTIVITY REGULATION.
RX PubMed=29216370; DOI=10.1093/pcp/pcx186;
RA Yang Q., Sang S., Chen Y., Wei Z., Wang P.;
RT "The role of Arabidopsis inositol polyphosphate kinase AtIPK2beta in
RT glucose suppression of seed germination and seedling development.";
RL Plant Cell Physiol. 59:343-354(2018).
CC -!- FUNCTION: Inositol phosphate kinase with a broad substrate specificity.
CC Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), inositol
CC 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), inositol 1,3,4,5-
CC tetrakisphosphate (Ins(1,3,4,5)P4), inositol 1,3,4,6-tetrakisphosphate
CC (Ins(1,3,4,6)P4) and inositol 1,2,3,4,6-pentakisphosphate
CC (Ins(1,2,3,4,6)P5) but not inositol 1,4-bisphosphate (Ins(1,4)P2),
CC inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), inositol 1,2,6-
CC trisphosphate (Ins(1,2,6)P3), inositol 3,4,5,6-tetrakisphosphate
CC (Ins(3,4,5,6)P4), inositol 1,3,4,5,6-pentakisphosphate
CC (Ins(1,3,4,5,6)P5), inositol 1,2,4,5,6-pentakisphosphate
CC (Ins(1,2,4,5,6)P5) or inositol hexakisphosphate (InsP6). Involved in
CC the auxin signaling pathway. Regulates axillary shoot branching and is
CC required for phytate synthesis in seeds. {ECO:0000269|PubMed:12226109,
CC ECO:0000269|PubMed:16107538, ECO:0000269|PubMed:17434984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol
CC 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+); Xref=Rhea:RHEA:32359,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.151;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,6-tetrakisphosphate + ATP = 1D-myo-
CC inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:12717, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57660, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216;
CC EC=2.7.1.140;
CC -!- ACTIVITY REGULATION: Down-regulated by KIN10 through its protein
CC phosphorylation. {ECO:0000269|PubMed:29216370}.
CC -!- SUBUNIT: Interacts with KIN10 and KIN11. {ECO:0000269|PubMed:29216370}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12566584}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, siliques and
CC flowers. Detected in vascular strands, stigma cells, the abscission
CC zones of fully elongated siliques, the root central cylinder and the
CC root tip. {ECO:0000269|PubMed:12226109, ECO:0000269|PubMed:12566584}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mature pollen, but not in immature
CC pollen grains. {ECO:0000269|PubMed:12566584}.
CC -!- INDUCTION: Induced by auxin, but not by salt, abscisic acid, mannitol,
CC water or drought. {ECO:0000269|PubMed:12566584,
CC ECO:0000269|PubMed:17434984}.
CC -!- PTM: Phosphorylated by KIN10. {ECO:0000269|PubMed:29216370}.
CC -!- DISRUPTION PHENOTYPE: Loss-of-function mutant atIpk2beta-1 (T-DNA
CC insertion) is fully complemented by AtIPK2alpha in tissue but not in
CC seeds, leading to the generation of phytate-free seeds. Increased
CC sensitivity to 6% glucose during seedling development and decreased
CC germination in response to the gibberellin biosynthesis inhibitor
CC paclobutrazol (PAC) (PubMed:29216370). {ECO:0000269|PubMed:16107538,
CC ECO:0000269|PubMed:29216370}.
CC -!- MISCELLANEOUS: Does not bind calmodulin.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
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DR EMBL; AY147936; AAN63058.1; -; mRNA.
DR EMBL; AJ245521; CAC43071.1; -; mRNA.
DR EMBL; AB010069; BAB10076.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97513.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70375.1; -; Genomic_DNA.
DR EMBL; AJ243592; CAC43070.1; -; Genomic_DNA.
DR EMBL; AF412073; AAL06526.1; -; mRNA.
DR EMBL; AY072621; AAL62012.1; -; mRNA.
DR EMBL; AY085862; AAM63075.1; -; mRNA.
DR RefSeq; NP_001331991.1; NM_001345497.1.
DR RefSeq; NP_200984.1; NM_125570.4.
DR AlphaFoldDB; Q9FLT2; -.
DR SMR; Q9FLT2; -.
DR STRING; 3702.AT5G61760.1; -.
DR iPTMnet; Q9FLT2; -.
DR PaxDb; Q9FLT2; -.
DR PRIDE; Q9FLT2; -.
DR ProteomicsDB; 248514; -.
DR DNASU; 836298; -.
DR EnsemblPlants; AT5G61760.1; AT5G61760.1; AT5G61760.
DR EnsemblPlants; AT5G61760.2; AT5G61760.2; AT5G61760.
DR GeneID; 836298; -.
DR Gramene; AT5G61760.1; AT5G61760.1; AT5G61760.
DR Gramene; AT5G61760.2; AT5G61760.2; AT5G61760.
DR KEGG; ath:AT5G61760; -.
DR Araport; AT5G61760; -.
DR TAIR; locus:2159203; AT5G61760.
DR eggNOG; KOG1620; Eukaryota.
DR HOGENOM; CLU_042569_1_0_1; -.
DR InParanoid; Q9FLT2; -.
DR OMA; KPECGER; -.
DR OrthoDB; 902814at2759; -.
DR PhylomeDB; Q9FLT2; -.
DR BioCyc; ARA:AT5G61760-MON; -.
DR BioCyc; MetaCyc:AT5G61760-MON; -.
DR BRENDA; 2.7.1.151; 399.
DR BRENDA; 2.7.4.21; 399.
DR PRO; PR:Q9FLT2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLT2; baseline and differential.
DR Genevisible; Q9FLT2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000824; F:inositol tetrakisphosphate 3-kinase activity; IDA:TAIR.
DR GO; GO:0047326; F:inositol tetrakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0051765; F:inositol tetrakisphosphate kinase activity; IDA:TAIR.
DR GO; GO:0051766; F:inositol trisphosphate kinase activity; IDA:TAIR.
DR GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IDA:TAIR.
DR GO; GO:0008440; F:inositol-1,4,5-trisphosphate 3-kinase activity; IBA:GO_Central.
DR GO; GO:0000823; F:inositol-1,4,5-trisphosphate 6-kinase activity; IDA:TAIR.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0102732; F:myo-inositol-1,2,3,4,6-heptakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR Gene3D; 3.30.470.160; -; 1.
DR InterPro; IPR005522; IPK.
DR InterPro; IPR038286; IPK_sf.
DR PANTHER; PTHR12400; PTHR12400; 1.
DR Pfam; PF03770; IPK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..300
FT /note="Inositol polyphosphate multikinase beta"
FT /id="PRO_0000341577"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MUTAGEN 100
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12226109"
FT CONFLICT 53
FT /note="M -> K (in Ref. 6; AAM63075)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="Q -> K (in Ref. 6; AAM63075)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="D -> N (in Ref. 6; AAM63075)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33487 MW; 6903A3818CBF27D7 CRC64;
MLKVPEHQVA GHIASDGKLG PLVDDQGRFF KPLQGDSRGE HEAKFYESFT SNMKVPDHIH
RYFPVYHGTQ LVEASDGSGK LPHLVLDDVV SGYANPSVMD VKIGSRTWYP DVSEEYFKKC
IKKDRQTTTV SLGFRVSGFK IFDHQESSFW RAEKKLVLGY NADGARLALR KFVSSNSPAD
SNLTPNCAFA SEVYGGCNGI LAQLLELKDW FETQTLYHFN SCSILMIYEN ESILMQGGDD
APAPRAQVKL VDFAHVLDGN GVIDHNFLGG LCSFIKFIKD ILQSVEKHDE TDTSLLENGR
