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Protein

Inositol-3-phosphate synthase isozyme 1

Gene

IPS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the majority of myo-inositol synthesis required for plant growth and development. Acts as a repressor of programmed cell death and protects plant cells against cell death under high light intensity or long days. Controls its own transcription by inhibiting ATXR6 activity. Reduces the deposition of inhibitory histone marks on its own promoter.2 Publications

Catalytic activityi

D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate.1 Publication

Cofactori

Kineticsi

kcat is 6.4 min(-1) for D-glucose 6-phosphate. kcat is 5.0 min(-1) for NAD+.

  1. KM=0.68 mM for D-glucose 6-phosphate1 Publication
  2. KM=0.46 µM for NAD+1 Publication

    Pathwayi: myo-inositol biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Inositol-3-phosphate synthase isozyme 1 (IPS1), Probable inositol 3-phosphate synthase isozyme 3 (IPS3), Inositol-3-phosphate synthase isozyme 2 (IPS2)
    2. Bifunctional phosphatase IMPL2, chloroplastic (HISN7), Inositol-phosphate phosphatase (VTC4), Phosphatase IMPL1, chloroplastic (IMPL1)
    This subpathway is part of the pathway myo-inositol biosynthesis, which is itself part of Polyol metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate, the pathway myo-inositol biosynthesis and in Polyol metabolism.

    GO - Molecular functioni

    • inositol-3-phosphate synthase activity Source: TAIR

    GO - Biological processi

    • embryo development ending in seed dormancy Source: TAIR
    • inositol biosynthetic process Source: TAIR
    • myo-inositol hexakisphosphate biosynthetic process Source: TAIR
    • phosphatidylserine biosynthetic process Source: TAIR
    • post-embryonic development Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Inositol biosynthesis, Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciARA:AT4G39800-MONOMER.
    BRENDAi5.5.1.4. 399.
    ReactomeiR-ATH-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RKP42801.
    UniPathwayiUPA00823; UER00787.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol-3-phosphate synthase isozyme 1 (EC:5.5.1.4)
    Short name:
    AtIPS1
    Short name:
    MIP synthase 1
    Alternative name(s):
    Myo-inositol 1-phosphate synthase 1
    Short name:
    AtMIPS 1
    Short name:
    MI-1-P synthase 1
    Gene namesi
    Name:IPS1
    Synonyms:MIPS1
    Ordered Locus Names:At4g39800
    ORF Names:T19P19.190
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G39800.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: TAIR
    • nucleus Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Shorter seedlings with deformed cotyledons and altered root cap organization. Spontaneous lesion formation on mature leaves when plants are transferred under long days. Enhanced basal resistance to pathogens and increased sensitivity to abscisic acid during seed germination and root growth.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 511511Inositol-3-phosphate synthase isozyme 1PRO_0000195186Add
    BLAST

    Proteomic databases

    PaxDbiP42801.
    PRIDEiP42801.

    Expressioni

    Tissue specificityi

    Expressed in siliques, leaves, roots, seed endosperm, but not in embryos. Highest expression in leaves, but restricted to vascular tissue in older leaves.2 Publications

    Inductioni

    Up-regulated by the IPS1 protein itself. Down-regulate upon flagellin treatment.1 Publication

    Gene expression databases

    ExpressionAtlasiP42801. baseline and differential.
    GenevisibleiP42801. AT.

    Interactioni

    Subunit structurei

    Homotrimer or homotetramer. Interacts with ATXR5 and ATXR6.2 Publications

    Protein-protein interaction databases

    BioGridi15419. 4 interactions.
    IntActiP42801. 2 interactions.
    STRINGi3702.AT4G39800.1.

    Structurei

    3D structure databases

    ProteinModelPortaliP42801.
    SMRiP42801. Positions 8-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG0693. Eukaryota.
    COG1260. LUCA.
    HOGENOMiHOG000013469.
    InParanoidiP42801.
    KOiK01858.
    OMAiEAISPAM.
    PhylomeDBiP42801.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR002587. Myo-inos-1-P_Synthase.
    IPR013021. Myo-inos-1-P_Synthase_GAPDH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11510. PTHR11510. 1 hit.
    PfamiPF01658. Inos-1-P_synth. 1 hit.
    PF07994. NAD_binding_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015578. Myoinos-ppht_syn. 1 hit.
    SUPFAMiSSF51735. SSF51735. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P42801-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MFIESFKVES PNVKYTENEI HSVYDYETTE VVHEKTVNGT YQWIVKPKTV
    60 70 80 90 100
    KYDFKTDIRV PKLGVMLVGL GGNNGSTLTA GVIANKEGIS WATKDKVQQA
    110 120 130 140 150
    NYFGSLTQAS SIRVGSFNGE EIYAPFKSLL PMVNPDDVVF GGWDISDMNL
    160 170 180 190 200
    ADAMARARVL DIDLQKQLRP YMENIVPLPG IFDPDFIAAN QGSRANHVIK
    210 220 230 240 250
    GTKKEQVDHI IKDMREFKEK NKVDKVVVLW TANTERYSNV VVGMNDTMEN
    260 270 280 290 300
    LMESVDRDEA EISPSTLYAI ACVLEGIPFI NGSPQNTFVP GLIDMAIRNN
    310 320 330 340 350
    VLIGGDDFKS GQTKMKSVLV DFLVGAGIKP TSIVSYNHLG NNDGMNLSAP
    360 370 380 390 400
    QTFRSKEISK SNVVDDMVAS NGILFEPGEH PDHVVVIKYV PYVADSKRAM
    410 420 430 440 450
    DEYTSEIFMG GKNTIVMHNT CEDSLLAAPI ILDLVLLAEL STRIQFKSEG
    460 470 480 490 500
    EGKFHSFHPV ATILSYLTKA PLVPPGTPVI NALSKQRAML ENIMRACVGL
    510
    APENNMIMEF K
    Length:511
    Mass (Da):56,515
    Last modified:June 20, 2001 - v3
    Checksum:iA1BC7CB0474E9774
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti357 – 3582EI → GD in AAA85390 (PubMed:8058832).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U04876 mRNA. Translation: AAA85390.1.
    AL022605 Genomic DNA. Translation: CAA18766.1.
    AL161595 Genomic DNA. Translation: CAB80643.1.
    CP002687 Genomic DNA. Translation: AEE87121.1.
    AF372954 mRNA. Translation: AAK50093.1.
    BT001931 mRNA. Translation: AAN71930.1.
    AY085931 mRNA. Translation: AAM63143.1.
    PIRiT05017.
    RefSeqiNP_195690.1. NM_120143.3.
    UniGeneiAt.24599.

    Genome annotation databases

    EnsemblPlantsiAT4G39800.1; AT4G39800.1; AT4G39800.
    GeneIDi830139.
    GrameneiAT4G39800.1; AT4G39800.1; AT4G39800.
    KEGGiath:AT4G39800.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U04876 mRNA. Translation: AAA85390.1.
    AL022605 Genomic DNA. Translation: CAA18766.1.
    AL161595 Genomic DNA. Translation: CAB80643.1.
    CP002687 Genomic DNA. Translation: AEE87121.1.
    AF372954 mRNA. Translation: AAK50093.1.
    BT001931 mRNA. Translation: AAN71930.1.
    AY085931 mRNA. Translation: AAM63143.1.
    PIRiT05017.
    RefSeqiNP_195690.1. NM_120143.3.
    UniGeneiAt.24599.

    3D structure databases

    ProteinModelPortaliP42801.
    SMRiP42801. Positions 8-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi15419. 4 interactions.
    IntActiP42801. 2 interactions.
    STRINGi3702.AT4G39800.1.

    Proteomic databases

    PaxDbiP42801.
    PRIDEiP42801.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G39800.1; AT4G39800.1; AT4G39800.
    GeneIDi830139.
    GrameneiAT4G39800.1; AT4G39800.1; AT4G39800.
    KEGGiath:AT4G39800.

    Organism-specific databases

    TAIRiAT4G39800.

    Phylogenomic databases

    eggNOGiKOG0693. Eukaryota.
    COG1260. LUCA.
    HOGENOMiHOG000013469.
    InParanoidiP42801.
    KOiK01858.
    OMAiEAISPAM.
    PhylomeDBiP42801.

    Enzyme and pathway databases

    UniPathwayiUPA00823; UER00787.
    BioCyciARA:AT4G39800-MONOMER.
    BRENDAi5.5.1.4. 399.
    ReactomeiR-ATH-1855183. Synthesis of IP2, IP, and Ins in the cytosol.
    SABIO-RKP42801.

    Miscellaneous databases

    PROiP42801.

    Gene expression databases

    ExpressionAtlasiP42801. baseline and differential.
    GenevisibleiP42801. AT.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR002587. Myo-inos-1-P_Synthase.
    IPR013021. Myo-inos-1-P_Synthase_GAPDH.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR11510. PTHR11510. 1 hit.
    PfamiPF01658. Inos-1-P_synth. 1 hit.
    PF07994. NAD_binding_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015578. Myoinos-ppht_syn. 1 hit.
    SUPFAMiSSF51735. SSF51735. 2 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The Arabidopsis thaliana myo-inositol 1-phosphate synthase (EC 5.5.1.4)."
      Johnson M.A.
      Plant Physiol. 105:1023-1024(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
    2. Johnson M.A.
      Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "Localization of myo-inositol-1-phosphate synthase to the endosperm in developing seeds of Arabidopsis."
      Mitsuhashi N., Kondo M., Nakaune S., Ohnishi M., Hayashi M., Hara-Nishimura I., Richardson A., Fukaki H., Nishimura M., Mimura T.
      J. Exp. Bot. 59:3069-3076(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Strain: cv. Columbia.
    8. Cited for: INTERACTION WITH ATXR5 AND ATXR6, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    9. "The Arabidopsis thaliana Myo-inositol 1-phosphate synthase1 gene is required for Myo-inositol synthesis and suppression of cell death."
      Donahue J.L., Alford S.R., Torabinejad J., Kerwin R.E., Nourbakhsh A., Ray W.K., Hernick M., Huang X., Lyons B.M., Hein P.P., Gillaspy G.E.
      Plant Cell 22:888-903(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
    10. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATXR6, INDUCTION BY FLAGELLIN AND IPS1.

    Entry informationi

    Entry nameiINO1_ARATH
    AccessioniPrimary (citable) accession number: P42801
    Secondary accession number(s): O65667
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: June 20, 2001
    Last modified: February 17, 2016
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Caution

    Was called MIPS2.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.