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Q9ZRW8

- GSTUJ_ARATH

UniProt

Q9ZRW8 - GSTUJ_ARATH

Protein

Glutathione S-transferase U19

Gene

GSTU19

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Catalyzes the glutathionylation of 12-oxophytodienoate (OPDA). In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC), and glutathione peroxidase activity toward cumene hydroperoxide.3 Publications

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.

    GO - Molecular functioni

    1. glutathione binding Source: TAIR
    2. glutathione transferase activity Source: TAIR
    3. peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular response to water deprivation Source: TAIR
    2. response to cadmium ion Source: TAIR
    3. response to oxidative stress Source: TAIR
    4. response to toxic substance Source: UniProtKB-KW
    5. toxin catabolic process Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase, Transferase

    Keywords - Biological processi

    Detoxification, Stress response

    Enzyme and pathway databases

    BioCyciARA:AT1G78380-MONOMER.
    MetaCyc:AT1G78380-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase U19 (EC:2.5.1.18)
    Short name:
    AtGSTU19
    Alternative name(s):
    GST class-tau member 19
    Glutathione S-transferase 8
    Gene namesi
    Name:GSTU19
    Synonyms:GST8
    Ordered Locus Names:At1g78380
    ORF Names:F3F9.11
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G78380.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. chloroplast Source: TAIR
    2. chloroplast stroma Source: TAIR
    3. cytoplasm Source: TAIR
    4. cytosol Source: TAIR
    5. plasma membrane Source: TAIR
    6. vacuolar membrane Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 219218Glutathione S-transferase U19PRO_0000413565Add
    BLAST

    Proteomic databases

    PRIDEiQ9ZRW8.

    Expressioni

    Inductioni

    By dehydration stress, salicylic acid, ethylene, methyl jasmonate, auxin, H2O2, copper, benoxacor, isothiocyanates and the pathogen Hyaloperonospora parasitica.6 Publications

    Gene expression databases

    ArrayExpressiQ9ZRW8.
    GenevestigatoriQ9ZRW8.

    Interactioni

    Protein-protein interaction databases

    BioGridi29393. 6 interactions.
    IntActiQ9ZRW8. 5 interactions.
    STRINGi3702.AT1G78380.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZRW8.
    SMRiQ9ZRW8. Positions 4-216.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8280GST N-terminalAdd
    BLAST
    Domaini88 – 208121GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni13 – 142Glutathione bindingBy similarity
    Regioni39 – 402Glutathione bindingBy similarity
    Regioni53 – 542Glutathione bindingBy similarity
    Regioni66 – 672Glutathione bindingBy similarity

    Sequence similaritiesi

    Belongs to the GST superfamily. Tau family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    HOGENOMiHOG000125749.
    InParanoidiQ9ZRW8.
    KOiK00799.
    OMAiDFWANGF.
    PhylomeDBiQ9ZRW8.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9ZRW8-1 [UniParc]FASTAAdd to Basket

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    MANEVILLDF WPSMFGMRTR IALREKGVEF EYREEDLRNK SPLLLQMNPI    50
    HKKIPVLIHN GKPVNESIIQ VQYIDEVWSH KNPILPSDPY LRAQARFWAD 100
    FIDKKLYDAQ RKVWATKGEE QEAGKKDFIE ILKTLESELG DKPYFSGDDF 150
    GYVDIALIGF YTWFPAYEKF ANFSIESEVP KLIAWVKKCL QRESVAKSLP 200
    DPEKVTEFVS ELRKKFVPE 219
    Length:219
    Mass (Da):25,651
    Last modified:May 1, 1999 - v1
    Checksum:iE79AABD8C14C6F15
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161G → R in AAM64593. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012571 mRNA. Translation: CAA10060.1.
    AC013430 Genomic DNA. No translation available.
    CP002684 Genomic DNA. Translation: AEE36099.1.
    AF385691 mRNA. Translation: AAK60284.1.
    AY078012 mRNA. Translation: AAL77713.1.
    AY087032 mRNA. Translation: AAM64593.1.
    PIRiT51607.
    RefSeqiNP_565178.1. NM_106485.3.
    UniGeneiAt.25493.
    At.67704.

    Genome annotation databases

    EnsemblPlantsiAT1G78380.1; AT1G78380.1; AT1G78380.
    GeneIDi844174.
    KEGGiath:AT1G78380.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012571 mRNA. Translation: CAA10060.1 .
    AC013430 Genomic DNA. No translation available.
    CP002684 Genomic DNA. Translation: AEE36099.1 .
    AF385691 mRNA. Translation: AAK60284.1 .
    AY078012 mRNA. Translation: AAL77713.1 .
    AY087032 mRNA. Translation: AAM64593.1 .
    PIRi T51607.
    RefSeqi NP_565178.1. NM_106485.3.
    UniGenei At.25493.
    At.67704.

    3D structure databases

    ProteinModelPortali Q9ZRW8.
    SMRi Q9ZRW8. Positions 4-216.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 29393. 6 interactions.
    IntActi Q9ZRW8. 5 interactions.
    STRINGi 3702.AT1G78380.1-P.

    Proteomic databases

    PRIDEi Q9ZRW8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G78380.1 ; AT1G78380.1 ; AT1G78380 .
    GeneIDi 844174.
    KEGGi ath:AT1G78380.

    Organism-specific databases

    TAIRi AT1G78380.

    Phylogenomic databases

    HOGENOMi HOG000125749.
    InParanoidi Q9ZRW8.
    KOi K00799.
    OMAi DFWANGF.
    PhylomeDBi Q9ZRW8.

    Enzyme and pathway databases

    BioCyci ARA:AT1G78380-MONOMER.
    MetaCyc:AT1G78380-MONOMER.

    Gene expression databases

    ArrayExpressi Q9ZRW8.
    Genevestigatori Q9ZRW8.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Drought regulation of GST8, encoding the Arabidopsis homologue of ParC/Nt107 glutathione transferase/peroxidase."
      Bianchi M.W., Roux C., Vartanian N.
      Physiol. Plantarum 116:96-105(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "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.
    5. "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].
    6. "Probing the diversity of the Arabidopsis glutathione S-transferase gene family."
      Wagner U., Edwards R., Dixon D.P., Mauch F.
      Plant Mol. Biol. 49:515-532(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, GENE FAMILY, NOMENCLATURE.
      Strain: cv. Columbia.
    7. "Induction of glutathione S-transferases in Arabidopsis by herbicide safeners."
      DeRidder B.P., Dixon D.P., Beussman D.J., Edwards R., Goldsbrough P.B.
      Plant Physiol. 130:1497-1505(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Proteomic analysis of Arabidopsis glutathione S-transferases from benoxacor- and copper-treated seedlings."
      Smith A.P., DeRidder B.P., Guo W.J., Seeley E.H., Regnier F.E., Goldsbrough P.B.
      J. Biol. Chem. 279:26098-26104(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    9. "Organ-specific expression of glutathione S-transferases and the efficacy of herbicide safeners in Arabidopsis."
      DeRidder B.P., Goldsbrough P.B.
      Plant Physiol. 140:167-175(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    10. "Selective binding of glutathione conjugates of fatty acid derivatives by plant glutathione transferases."
      Dixon D.P., Edwards R.
      J. Biol. Chem. 284:21249-21256(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily."
      Dixon D.P., Hawkins T., Hussey P.J., Edwards R.
      J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    12. "Exogenously applied isothiocyanates enhance glutathione S-transferase expression in Arabidopsis but act as herbicides at higher concentrations."
      Hara M., Yatsuzuka Y., Tabata K., Kuboi T.
      J. Plant Physiol. 167:643-649(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiGSTUJ_ARATH
    AccessioniPrimary (citable) accession number: Q9ZRW8
    Secondary accession number(s): Q8LBS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 103 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3