MIK_ORYSJ
ID MIK_ORYSJ Reviewed; 397 AA.
AC Q84R36; A0A0P0W3B4; Q7Y1F1;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Inositol 3-kinase {ECO:0000305};
DE EC=2.7.1.64 {ECO:0000250|UniProtKB:Q5GA22};
DE AltName: Full=Myo-inositol kinase {ECO:0000303|PubMed:18726583};
DE Short=OsMIK {ECO:0000303|PubMed:18726583};
DE AltName: Full=Protein LOW PHYTIC ACID {ECO:0000303|PubMed:18726583};
GN Name=MIK {ECO:0000305}; Synonyms=LPA {ECO:0000303|PubMed:18726583};
GN OrderedLocusNames=Os03g0737701 {ECO:0000312|EMBL:BAH92363.1},
GN LOC_Os03g52760 {ECO:0000312|EMBL:ABF98765.1};
GN ORFNames=OSJNBa0057G07.25 {ECO:0000312|EMBL:AAP44711.1},
GN OSJNBb0016H12.26 {ECO:0000312|EMBL:AAP03418.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14530400; DOI=10.1073/pnas.1434476100;
RA Ilic K., SanMiguel P.J., Bennetzen J.L.;
RT "A complex history of rearrangement in an orthologous region of the maize,
RT sorghum, and rice genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12265-12270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Nipponbare;
RX PubMed=18726583; DOI=10.1007/s00122-008-0863-7;
RA Kim S.I., Andaya C.B., Newman J.W., Goyal S.S., Tai T.H.;
RT "Isolation and characterization of a low phytic acid rice mutant reveals a
RT mutation in the rice orthologue of maize MIK.";
RL Theor. Appl. Genet. 117:1291-1301(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17219209; DOI=10.1007/s00122-006-0478-9;
RA Liu Q.L., Xu X.H., Ren X.L., Fu H.W., Wu D.X., Shu Q.Y.;
RT "Generation and characterization of low phytic acid germplasm in rice
RT (Oryza sativa L.).";
RL Theor. Appl. Genet. 114:803-814(2007).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=24042572; DOI=10.1007/s00122-013-2189-3;
RA Zhao H.J., Cui H.R., Xu X.H., Tan Y.Y., Fu J.J., Liu G.Z., Poirier Y.,
RA Shu Q.Y.;
RT "Characterization of OsMIK in a rice mutant with reduced phytate content
RT reveals an insertion of a rearranged retrotransposon.";
RL Theor. Appl. Genet. 126:3009-3020(2013).
CC -!- FUNCTION: Kinase that phosphorylates myo-inositol to produce multiple
CC myo-inositol monophosphates. Participates in phytic acid biosynthesis
CC in developing seeds. Phytic acid is the primary storage form of
CC phosphorus in cereal grains and other plant seeds.
CC {ECO:0000269|PubMed:17219209, ECO:0000269|PubMed:18726583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + myo-inositol = 1D-myo-inositol 3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:21804, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58401, ChEBI:CHEBI:456216;
CC EC=2.7.1.64; Evidence={ECO:0000250|UniProtKB:Q5GA22};
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaf blade shoots, leaf sheath
CC shoots and panicles. {ECO:0000269|PubMed:18726583}.
CC -!- DISRUPTION PHENOTYPE: Strong reduction in seed phytic acid with a molar
CC equivalent increase in inorganic phosphate. Strong increase in myo-
CC inositol levels in seeds. {ECO:0000269|PubMed:17219209,
CC ECO:0000269|PubMed:18726583, ECO:0000269|PubMed:24042572}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP44711.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY387483; AAR07075.1; -; Genomic_DNA.
DR EMBL; EU366952; ACB38658.1; -; mRNA.
DR EMBL; AC117988; AAP44711.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC118133; AAP03418.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98765.1; -; Genomic_DNA.
DR EMBL; AP008209; BAH92363.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86280.1; -; Genomic_DNA.
DR RefSeq; XP_015627815.1; XM_015772329.1.
DR AlphaFoldDB; Q84R36; -.
DR SMR; Q84R36; -.
DR STRING; 4530.OS03T0737701-00; -.
DR PaxDb; Q84R36; -.
DR PRIDE; Q84R36; -.
DR EnsemblPlants; Os03t0737701-01; Os03t0737701-01; Os03g0737701.
DR GeneID; 9272095; -.
DR Gramene; Os03t0737701-01; Os03t0737701-01; Os03g0737701.
DR KEGG; osa:9272095; -.
DR eggNOG; KOG2855; Eukaryota.
DR HOGENOM; CLU_061466_0_0_1; -.
DR InParanoid; Q84R36; -.
DR OMA; ESGFFHL; -.
DR OrthoDB; 1230087at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q84R36; OS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019140; F:inositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR031094; MIK.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR43085:SF13; PTHR43085:SF13; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..397
FT /note="Inositol 3-kinase"
FT /id="PRO_0000431867"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 278..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
SQ SEQUENCE 397 AA; 41540 MW; AF2F37C674A12F36 CRC64;
MAPSPAAAMP LAAEPDEVVV EVEEEEERGV KGGGGVAGLD EVEGLVVGSY CHDVLLRGGR
VVGETLGGAA AFVSNVLDAA SPAGASLAVV SKVGHDFAYA TAAAPARHPP VLCASPTTSF
HARFSDDAAS AHAPDRQLRR VHACDPIYPA DLPDRRFAYG LAVGVAGEVL PETLERMIRL
CRAVLVDAQA LIRAFDGEAK GGGAVRHVAL EATPYARLLP RVAFLKASSE EAPYVGVETA
RRRCCVIVTE GRDGCRLYWD GGEARVAPFP AVQVDPTGAG DSFLAGFASG LLWGLSATDA
ALLGNFFGAA AVSQVGVPTF DPKMLQAVKQ ILEKAVKRPC THINGNTFTF QRSSMHDELH
KSLQEAAMLV CEQKQANSPA TDNGDVCSIN ELTSLPS
