INO1_ARATH
ID INO1_ARATH Reviewed; 511 AA.
AC P42801; O65667;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Inositol-3-phosphate synthase isozyme 1;
DE Short=AtIPS1;
DE Short=MIP synthase 1;
DE EC=5.5.1.4;
DE AltName: Full=Myo-inositol 1-phosphate synthase 1;
DE Short=AtMIPS 1;
DE Short=MI-1-P synthase 1;
GN Name=IPS1; Synonyms=MIPS1; OrderedLocusNames=At4g39800;
GN ORFNames=T19P19.190;
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].
RC STRAIN=cv. Columbia;
RX PubMed=8058832; DOI=10.1104/pp.105.3.1023;
RA Johnson M.A.;
RT "The Arabidopsis thaliana myo-inositol 1-phosphate synthase (EC 5.5.1.4).";
RL Plant Physiol. 105:1023-1024(1994).
RN [2]
RP SEQUENCE REVISION.
RA Johnson M.A.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=18603618; DOI=10.1093/jxb/ern161;
RA Mitsuhashi N., Kondo M., Nakaune S., Ohnishi M., Hayashi M.,
RA Hara-Nishimura I., Richardson A., Fukaki H., Nishimura M., Mimura T.;
RT "Localization of myo-inositol-1-phosphate synthase to the endosperm in
RT developing seeds of Arabidopsis.";
RL J. Exp. Bot. 59:3069-3076(2008).
RN [8]
RP INTERACTION WITH ATXR5 AND ATXR6, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19812700; DOI=10.1371/journal.pone.0007364;
RA Meng P.H., Raynaud C., Tcherkez G., Blanchet S., Massoud K.,
RA Domenichini S., Henry Y., Soubigou-Taconnat L., Lelarge-Trouverie C.,
RA Saindrenan P., Renou J.P., Bergounioux C.;
RT "Crosstalks between myo-inositol metabolism, programmed cell death and
RT basal immunity in Arabidopsis.";
RL PLoS ONE 4:E7364-E7364(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=20215587; DOI=10.1105/tpc.109.071779;
RA Donahue J.L., Alford S.R., Torabinejad J., Kerwin R.E., Nourbakhsh A.,
RA Ray W.K., Hernick M., Huang X., Lyons B.M., Hein P.P., Gillaspy G.E.;
RT "The Arabidopsis thaliana Myo-inositol 1-phosphate synthase1 gene is
RT required for Myo-inositol synthesis and suppression of cell death.";
RL Plant Cell 22:888-903(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATXR6, AND INDUCTION BY
RP FLAGELLIN AND IPS1.
RX PubMed=23341037; DOI=10.1093/nar/gks1458;
RA Latrasse D., Jegu T., Meng P.H., Mazubert C., Hudik E., Delarue M.,
RA Charon C., Crespi M., Hirt H., Raynaud C., Bergounioux C., Benhamed M.;
RT "Dual function of MIPS1 as a metabolic enzyme and transcriptional
RT regulator.";
RL Nucleic Acids Res. 41:2907-2917(2013).
CC -!- FUNCTION: Catalyzes the majority of myo-inositol synthesis required for
CC plant growth and development. Acts as a repressor of programmed cell
CC death and protects plant cells against cell death under high light
CC intensity or long days. Controls its own transcription by inhibiting
CC ATXR6 activity. Reduces the deposition of inhibitory histone marks on
CC its own promoter. {ECO:0000269|PubMed:20215587,
CC ECO:0000269|PubMed:23341037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate;
CC Xref=Rhea:RHEA:10716, ChEBI:CHEBI:58401, ChEBI:CHEBI:61548;
CC EC=5.5.1.4; Evidence={ECO:0000269|PubMed:20215587};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.68 mM for D-glucose 6-phosphate {ECO:0000269|PubMed:20215587};
CC KM=0.46 uM for NAD(+) {ECO:0000269|PubMed:20215587};
CC Note=kcat is 6.4 min(-1) for D-glucose 6-phosphate. kcat is 5.0 min(-
CC 1) for NAD(+).;
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 1/2.
CC -!- SUBUNIT: Homotrimer or homotetramer. Interacts with ATXR5 and ATXR6.
CC {ECO:0000269|PubMed:19812700, ECO:0000269|PubMed:23341037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in siliques, leaves, roots, seed
CC endosperm, but not in embryos. Highest expression in leaves, but
CC restricted to vascular tissue in older leaves.
CC {ECO:0000269|PubMed:18603618, ECO:0000269|PubMed:20215587}.
CC -!- INDUCTION: Up-regulated by the IPS1 protein itself. Down-regulate upon
CC flagellin treatment. {ECO:0000269|PubMed:23341037}.
CC -!- DISRUPTION PHENOTYPE: Shorter seedlings with deformed cotyledons and
CC altered root cap organization. Spontaneous lesion formation on mature
CC leaves when plants are transferred under long days. Enhanced basal
CC resistance to pathogens and increased sensitivity to abscisic acid
CC during seed germination and root growth. {ECO:0000269|PubMed:19812700,
CC ECO:0000269|PubMed:20215587}.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was called MIPS2. {ECO:0000305|PubMed:18603618}.
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DR EMBL; U04876; AAA85390.1; -; mRNA.
DR EMBL; AL022605; CAA18766.1; -; Genomic_DNA.
DR EMBL; AL161595; CAB80643.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE87121.1; -; Genomic_DNA.
DR EMBL; AF372954; AAK50093.1; -; mRNA.
DR EMBL; BT001931; AAN71930.1; -; mRNA.
DR EMBL; AY085931; AAM63143.1; -; mRNA.
DR PIR; T05017; T05017.
DR RefSeq; NP_195690.1; NM_120143.4.
DR AlphaFoldDB; P42801; -.
DR SMR; P42801; -.
DR BioGRID; 15419; 4.
DR IntAct; P42801; 2.
DR STRING; 3702.AT4G39800.1; -.
DR PaxDb; P42801; -.
DR PRIDE; P42801; -.
DR ProteomicsDB; 248458; -.
DR EnsemblPlants; AT4G39800.1; AT4G39800.1; AT4G39800.
DR GeneID; 830139; -.
DR Gramene; AT4G39800.1; AT4G39800.1; AT4G39800.
DR KEGG; ath:AT4G39800; -.
DR Araport; AT4G39800; -.
DR TAIR; locus:2135297; AT4G39800.
DR eggNOG; KOG0693; Eukaryota.
DR HOGENOM; CLU_021486_2_0_1; -.
DR InParanoid; P42801; -.
DR OMA; MNDTMEN; -.
DR OrthoDB; 451916at2759; -.
DR PhylomeDB; P42801; -.
DR BioCyc; ARA:AT4G39800-MON; -.
DR BRENDA; 5.5.1.4; 399.
DR SABIO-RK; P42801; -.
DR UniPathway; UPA00823; UER00787.
DR PRO; PR:P42801; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P42801; baseline and differential.
DR Genevisible; P42801; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IGI:TAIR.
DR GO; GO:0006021; P:inositol biosynthetic process; IDA:TAIR.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:TAIR.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:TAIR.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11510; PTHR11510; 1.
DR Pfam; PF01658; Inos-1-P_synth; 1.
DR Pfam; PF07994; NAD_binding_5; 1.
DR PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Inositol biosynthesis; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; NAD; Nucleus; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome.
FT CHAIN 1..511
FT /note="Inositol-3-phosphate synthase isozyme 1"
FT /id="PRO_0000195186"
FT CONFLICT 357..358
FT /note="EI -> GD (in Ref. 1; AAA85390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 56515 MW; A1BC7CB0474E9774 CRC64;
MFIESFKVES PNVKYTENEI HSVYDYETTE VVHEKTVNGT YQWIVKPKTV KYDFKTDIRV
PKLGVMLVGL GGNNGSTLTA GVIANKEGIS WATKDKVQQA NYFGSLTQAS SIRVGSFNGE
EIYAPFKSLL PMVNPDDVVF GGWDISDMNL ADAMARARVL DIDLQKQLRP YMENIVPLPG
IFDPDFIAAN QGSRANHVIK GTKKEQVDHI IKDMREFKEK NKVDKVVVLW TANTERYSNV
VVGMNDTMEN LMESVDRDEA EISPSTLYAI ACVLEGIPFI NGSPQNTFVP GLIDMAIRNN
VLIGGDDFKS GQTKMKSVLV DFLVGAGIKP TSIVSYNHLG NNDGMNLSAP QTFRSKEISK
SNVVDDMVAS NGILFEPGEH PDHVVVIKYV PYVADSKRAM DEYTSEIFMG GKNTIVMHNT
CEDSLLAAPI ILDLVLLAEL STRIQFKSEG EGKFHSFHPV ATILSYLTKA PLVPPGTPVI
NALSKQRAML ENIMRACVGL APENNMIMEF K
