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O80852

- GSTF9_ARATH

UniProt

O80852 - GSTF9_ARATH

Protein

Glutathione S-transferase F9

Gene

GSTF9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    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 and linoleic acid-13-hydroperoxide. May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.2 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. copper ion binding Source: TAIR
    2. glutathione binding Source: TAIR
    3. glutathione peroxidase activity Source: TAIR
    4. glutathione transferase activity Source: TAIR

    GO - Biological processi

    1. defense response Source: TAIR
    2. defense response to bacterium Source: TAIR
    3. response to cadmium ion Source: TAIR
    4. response to toxic substance Source: UniProtKB-KW
    5. response to zinc ion Source: TAIR
    6. toxin catabolic process Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase, Transferase

    Keywords - Biological processi

    Detoxification, Stress response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase F9 (EC:2.5.1.18)
    Short name:
    AtGSTF9
    Alternative name(s):
    AtGSTF7
    GST class-phi member 9
    Gene namesi
    Name:GSTF9
    Synonyms:GLUTTR, GSTF7
    Ordered Locus Names:At2g30860
    ORF Names:F7F1.7
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 2

    Organism-specific databases

    TAIRiAT2G30860.

    Subcellular locationi

    Cytoplasmcytosol Curated

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. chloroplast Source: TAIR
    3. chloroplast stroma Source: TAIR
    4. cytoplasm Source: TAIR
    5. cytosol Source: TAIR
    6. plasma membrane Source: TAIR
    7. plasmodesma Source: TAIR
    8. thylakoid Source: TAIR
    9. vacuole Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 215214Glutathione S-transferase F9PRO_0000413544Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiO80852.

    Expressioni

    Inductioni

    By zinc in roots and benoxacor.2 Publications

    Gene expression databases

    GenevestigatoriO80852.

    Interactioni

    Protein-protein interaction databases

    BioGridi2985. 1 interaction.
    IntActiO80852. 1 interaction.
    STRINGi3702.AT2G30860.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliO80852.
    SMRiO80852. Positions 3-214.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8180GST N-terminalAdd
    BLAST
    Domaini88 – 215128GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 402Glutathione bindingBy similarity
    Regioni52 – 532Glutathione bindingBy similarity
    Regioni65 – 662Glutathione bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000125746.
    InParanoidiO80852.
    KOiK00799.
    OMAiVWIISAK.
    PhylomeDBiO80852.

    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.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O80852-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MVLKVYGPHF ASPKRALVTL IEKGVAFETI PVDLMKGEHK QPAYLALQPF    50
    GTVPAVVDGD YKIFESRAVM RYVAEKYRSQ GPDLLGKTVE DRGQVEQWLD 100
    VEATTYHPPL LNLTLHIMFA SVMGFPSDEK LIKESEEKLA GVLDVYEAHL 150
    SKSKYLAGDF VSLADLAHLP FTDYLVGPIG KAYMIKDRKH VSAWWDDISS 200
    RPAWKETVAK YSFPA 215
    Length:215
    Mass (Da):24,146
    Last modified:November 1, 1998 - v1
    Checksum:i961996318A186F9C
    GO
    Isoform 2 (identifier: O80852-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         154-166: KYLAGDFVSLADL → NIHSQLKMCSSSW
         167-215: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:166
    Mass (Da):18,622
    Checksum:i4B1DB5773B081D65
    GO

    Sequence cautioni

    The sequence BAH56998.1 differs from that shown. Reason: Frameshift at position 154.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871K → E in BAH56998. (PubMed:19423640)Curated
    Sequence conflicti147 – 1515EAHLS → KAQRA in CAA72973. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei154 – 16613KYLAG…SLADL → NIHSQLKMCSSSW in isoform 2. 1 PublicationVSP_041938Add
    BLAST
    Alternative sequencei167 – 21549Missing in isoform 2. 1 PublicationVSP_041939Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12295 mRNA. Translation: CAA72973.1.
    AC004669 Genomic DNA. Translation: AAC20720.1.
    CP002685 Genomic DNA. Translation: AEC08448.1.
    CP002685 Genomic DNA. Translation: AEC08449.1.
    AF372905 mRNA. Translation: AAK49621.1.
    BT002679 mRNA. Translation: AAO11595.1.
    AK318883 mRNA. Translation: BAH56998.1. Frameshift.
    PIRiE84713.
    RefSeqiNP_001077983.1. NM_001084514.1. [O80852-2]
    NP_180643.1. NM_128638.2. [O80852-1]
    UniGeneiAt.22585.
    At.74970.
    At.74982.

    Genome annotation databases

    EnsemblPlantsiAT2G30860.1; AT2G30860.1; AT2G30860. [O80852-1]
    GeneIDi817636.
    KEGGiath:AT2G30860.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y12295 mRNA. Translation: CAA72973.1 .
    AC004669 Genomic DNA. Translation: AAC20720.1 .
    CP002685 Genomic DNA. Translation: AEC08448.1 .
    CP002685 Genomic DNA. Translation: AEC08449.1 .
    AF372905 mRNA. Translation: AAK49621.1 .
    BT002679 mRNA. Translation: AAO11595.1 .
    AK318883 mRNA. Translation: BAH56998.1 . Frameshift.
    PIRi E84713.
    RefSeqi NP_001077983.1. NM_001084514.1. [O80852-2 ]
    NP_180643.1. NM_128638.2. [O80852-1 ]
    UniGenei At.22585.
    At.74970.
    At.74982.

    3D structure databases

    ProteinModelPortali O80852.
    SMRi O80852. Positions 3-214.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 2985. 1 interaction.
    IntActi O80852. 1 interaction.
    STRINGi 3702.AT2G30860.1-P.

    Proteomic databases

    PRIDEi O80852.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT2G30860.1 ; AT2G30860.1 ; AT2G30860 . [O80852-1 ]
    GeneIDi 817636.
    KEGGi ath:AT2G30860.

    Organism-specific databases

    TAIRi AT2G30860.

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000125746.
    InParanoidi O80852.
    KOi K00799.
    OMAi VWIISAK.
    PhylomeDBi O80852.

    Gene expression databases

    Genevestigatori O80852.

    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.
    PF02798. GST_N. 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. "Cloning, expression and characterisation of an Arabidopsis glutathione transferase gene."
      Jemth P., Jiang F., Mannervik B.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    2. 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] (ISOFORM 1).
      Strain: cv. Columbia.
    5. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: cv. Columbia.
      Tissue: Rosette leaf.
    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, GENE FAMILY, NOMENCLATURE.
      Strain: cv. Columbia.
    7. "Characterization of two Arabidopsis thaliana glutathione S-transferases."
      Nutricati E., Miceli A., Blando F., De Bellis L.
      Plant Cell Rep. 25:997-1005(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    8. "Identification of zinc-responsive proteins in the roots of Arabidopsis thaliana using a highly improved method of two-dimensional electrophoresis."
      Fukao Y., Ferjani A., Fujiwara M., Nishimori Y., Ohtsu I.
      Plant Cell Physiol. 50:2234-2239(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ZINC.
    9. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGSTF9_ARATH
    AccessioniPrimary (citable) accession number: O80852
    Secondary accession number(s): A8MR26, C0Z2R9, O23626
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2011
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 105 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