IPMKA_ARATH
ID IPMKA_ARATH Reviewed; 286 AA.
AC Q9LY23; Q8LBG7; Q9LF72;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Inositol polyphosphate multikinase alpha;
DE EC=2.7.1.140;
DE EC=2.7.1.151;
DE AltName: Full=Inositol polyphosphate 6-/3-/5-kinase alpha;
DE Short=AtIpk2-alpha;
DE Short=AtIpk2alpha;
GN Name=IPK2a; Synonyms=IP3K, IPMK; OrderedLocusNames=At5g07370;
GN ORFNames=T2I1.80;
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-98, FUNCTION, TISSUE
RP SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15618435; DOI=10.1104/pp.104.045427;
RA Xu J., Brearley C.A., Lin W.-H., Wang Y., Ye R., Mueller-Roeber B.,
RA Xu Z.-H., Xue H.-W.;
RT "A role of Arabidopsis inositol polyphosphate kinase, AtIPK2alpha, in
RT pollen germination and root growth.";
RL Plant Physiol. 137:94-103(2005).
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., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., 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., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis 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 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 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 16-286.
RX PubMed=22896696; DOI=10.1074/jbc.m112.365031;
RA Endo-Streeter S., Tsui M.K., Odom A.R., Block J., York J.D.;
RT "Structural studies and protein engineering of inositol phosphate
RT multikinase.";
RL J. Biol. Chem. 287:35360-35369(2012).
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). Regulates
CC pollen and root development probably through the regulation of InsP3-
CC mediated calcium accumulation. {ECO:0000269|PubMed:12226109,
CC ECO:0000269|PubMed:15618435}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14.6 uM for Ins(1,4,5)P3 {ECO:0000269|PubMed:12226109};
CC KM=15.5 uM for Ins(1,3,4,5)P4 {ECO:0000269|PubMed:12226109};
CC KM=31.7 uM for Ins(1,4,5,6)P4 {ECO:0000269|PubMed:12226109};
CC Vmax=0.052 umol/min/mg enzyme toward Ins(1,4,5)P3
CC {ECO:0000269|PubMed:12226109};
CC Vmax=0.096 umol/min/mg enzyme toward Ins(1,3,4,5)P4
CC {ECO:0000269|PubMed:12226109};
CC Vmax=0.116 umol/min/mg enzyme toward Ins(1,4,5,6)P4
CC {ECO:0000269|PubMed:12226109};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15618435}. Cell
CC membrane {ECO:0000269|PubMed:15618435}.
CC -!- TISSUE SPECIFICITY: Detected in leaves, stems, roots, siliques and
CC flowers. Highly expressed in root tissues, anthers, the stigma, pollen
CC grains and growing pollen tubes. {ECO:0000269|PubMed:12226109,
CC ECO:0000269|PubMed:15618435}.
CC -!- DEVELOPMENTAL STAGE: Expression persisted in the stigmatic tissue after
CC fertilization and in siliques during seed maturation.
CC {ECO:0000269|PubMed:15618435}.
CC -!- INDUCTION: Not induced by auxin. {ECO:0000269|PubMed:17434984}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Does not bind calmodulin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
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DR EMBL; AY147935; AAN63057.1; -; mRNA.
DR EMBL; AJ404678; CAB96043.1; -; mRNA.
DR EMBL; AL163912; CAB87926.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91144.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91145.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91146.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91147.1; -; Genomic_DNA.
DR EMBL; AY136378; AAM97044.1; -; mRNA.
DR EMBL; BT000196; AAN15515.1; -; mRNA.
DR EMBL; AY087217; AAM64773.1; -; mRNA.
DR PIR; T49876; T49876.
DR RefSeq; NP_196354.1; NM_120819.2.
DR RefSeq; NP_850786.1; NM_180455.3.
DR RefSeq; NP_850787.1; NM_180456.2.
DR RefSeq; NP_974748.1; NM_203019.2.
DR PDB; 4FRF; X-ray; 2.90 A; A/B=16-286.
DR PDBsum; 4FRF; -.
DR AlphaFoldDB; Q9LY23; -.
DR SMR; Q9LY23; -.
DR STRING; 3702.AT5G07370.4; -.
DR PaxDb; Q9LY23; -.
DR PRIDE; Q9LY23; -.
DR ProteomicsDB; 247182; -.
DR DNASU; 830628; -.
DR EnsemblPlants; AT5G07370.1; AT5G07370.1; AT5G07370.
DR EnsemblPlants; AT5G07370.2; AT5G07370.2; AT5G07370.
DR EnsemblPlants; AT5G07370.3; AT5G07370.3; AT5G07370.
DR EnsemblPlants; AT5G07370.4; AT5G07370.4; AT5G07370.
DR GeneID; 830628; -.
DR Gramene; AT5G07370.1; AT5G07370.1; AT5G07370.
DR Gramene; AT5G07370.2; AT5G07370.2; AT5G07370.
DR Gramene; AT5G07370.3; AT5G07370.3; AT5G07370.
DR Gramene; AT5G07370.4; AT5G07370.4; AT5G07370.
DR KEGG; ath:AT5G07370; -.
DR Araport; AT5G07370; -.
DR TAIR; locus:2183389; AT5G07370.
DR eggNOG; KOG1620; Eukaryota.
DR HOGENOM; CLU_042569_1_0_1; -.
DR InParanoid; Q9LY23; -.
DR OMA; AHVYEGR; -.
DR OrthoDB; 902814at2759; -.
DR PhylomeDB; Q9LY23; -.
DR BioCyc; ARA:AT5G07370-MON; -.
DR BioCyc; MetaCyc:AT5G07370-MON; -.
DR BRENDA; 2.7.1.151; 399.
DR BRENDA; 2.7.4.21; 399.
DR SABIO-RK; Q9LY23; -.
DR PRO; PR:Q9LY23; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LY23; baseline and differential.
DR Genevisible; Q9LY23; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; 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; IBA:GO_Central.
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: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0010183; P:pollen tube guidance; IGI:TAIR.
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 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..286
FT /note="Inositol polyphosphate multikinase alpha"
FT /id="PRO_0000341576"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 98
FT /note="D->A: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12226109"
FT CONFLICT 92
FT /note="T -> S (in Ref. 6; AAM64773)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="D -> Y (in Ref. 1; AAN63057 and 2; CAB96043)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="F -> L (in Ref. 1; AAN63057 and 2; CAB96043)"
FT /evidence="ECO:0000305"
FT HELIX 43..52
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:4FRF"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:4FRF"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4FRF"
FT STRAND 130..141
FT /evidence="ECO:0007829|PDB:4FRF"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:4FRF"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:4FRF"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:4FRF"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:4FRF"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4FRF"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:4FRF"
SQ SEQUENCE 286 AA; 31946 MW; 98578D433C157EFC CRC64;
MQLKVPEHQV AGHIAKDGKP GPLVDDKGRF FKPLQGDSRG EIEVKFYESF SSNTEVPEHI
HRYFPVYHGT QAVEGSDGAA MMVLENLLAE YTKPSVMDVK MGSRTWYPDA SEEYIQKCLK
KDTGTTTVSS GFRISGFEVY DHKESSFWKP ERKLLRGLDV DGARLTLRKF VSSNSLSDTG
SKPDSAFASS VYGGSHGILT QLLELKTWFE NQTLYHFNSC SILMVYENES ILKGNDDDAR
PQVKLVDFAH VLDGNGVIDH NFLGGLCSFI NFIREILQSP DESADS
