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P46422

- GSTF2_ARATH

UniProt

P46422 - GSTF2_ARATH

Protein

Glutathione S-transferase F2

Gene

GSTF2

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 128 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Binds auxin, endogenous flavonoids and the phytoalexin camalexin and may be involved in regulating the binding and transport of small bioactive natural products and defense-related compounds during plant stress. Binds a series of heterocyclic compounds, including lumichrome, harmane, norharmane and indole-3-aldehyde. In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). Acts as glutathione peroxidase on cumene hydroperoxide, linoleic acid-13-hydroperoxide and trans-stilbene oxide, but not trans-cinnamic acid or IAA-CoA.2 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. camalexin binding Source: TAIR
    2. glutathione binding Source: TAIR
    3. glutathione transferase activity Source: TAIR
    4. peroxidase activity Source: UniProtKB-KW
    5. quercitrin binding Source: TAIR

    GO - Biological processi

    1. auxin-activated signaling pathway Source: UniProtKB-KW
    2. defense response to bacterium Source: TAIR
    3. defense response to fungus Source: TAIR
    4. response to cadmium ion Source: TAIR
    5. response to cold Source: TAIR
    6. response to salt stress Source: TAIR
    7. response to toxic substance Source: UniProtKB-KW
    8. response to zinc ion Source: TAIR
    9. toxin catabolic process Source: TAIR

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase, Transferase

    Keywords - Biological processi

    Auxin signaling pathway, Detoxification, Plant defense, Stress response

    Enzyme and pathway databases

    BioCyciARA:AT4G02520-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase F2 (EC:2.5.1.18)
    Short name:
    AtGSTF2
    Alternative name(s):
    24 kDa auxin-binding protein
    Short name:
    AtPM24
    GST class-phi member 2
    Gene namesi
    Name:GSTF2
    Synonyms:PM24.1
    Ordered Locus Names:At4g02520
    ORF Names:T10P11.18
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G02520.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Microsome 1 Publication. Endoplasmic reticulum 1 Publication
    Note: Plasma membrane vesicles.

    GO - Cellular componenti

    1. apoplast Source: TAIR
    2. chloroplast Source: TAIR
    3. chloroplast stroma Source: TAIR
    4. cytosol Source: TAIR
    5. endoplasmic reticulum Source: UniProtKB-SubCell
    6. intracellular membrane-bounded organelle Source: TAIR
    7. membrane Source: TAIR
    8. plasma membrane Source: TAIR
    9. plasmodesma Source: TAIR
    10. vacuole Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 212212Glutathione S-transferase F2PRO_0000185848Add
    BLAST

    Proteomic databases

    PRIDEiP46422.

    2D gel databases

    SWISS-2DPAGEP46422.

    Expressioni

    Tissue specificityi

    Expressed in the root-shoot transition zone and root tips.1 Publication

    Inductioni

    By ethylene, auxin, glutathione, salicylic acid, copper, paraquat, acetochlor, metolachlor and the pathogens P.syringae and Hyaloperonospora parasitica.6 Publications

    Gene expression databases

    GenevestigatoriP46422.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi13222. 6 interactions.

    Structurei

    Secondary structure

    1
    212
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi13 – 2412
    Beta strandi30 – 334
    Helixi36 – 383
    Helixi40 – 423
    Helixi46 – 483
    Beta strandi57 – 604
    Beta strandi63 – 664
    Helixi68 – 7811
    Turni79 – 813
    Beta strandi82 – 843
    Helixi94 – 10916
    Helixi112 – 12211
    Helixi124 – 1274
    Helixi134 – 15522
    Beta strandi159 – 1657
    Helixi168 – 1714
    Helixi174 – 1807
    Helixi184 – 1863
    Helixi187 – 1904
    Helixi193 – 20311
    Helixi206 – 2094

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BX9X-ray2.60A2-212[»]
    1GNWX-ray2.20A/B2-212[»]
    ProteinModelPortaliP46422.
    SMRiP46422. Positions 3-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46422.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8382GST N-terminalAdd
    BLAST
    Domaini93 – 212120GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni12 – 132Glutathione binding
    Regioni41 – 422Glutathione binding
    Regioni54 – 552Glutathione binding
    Regioni67 – 682Glutathione binding

    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

    HOGENOMiHOG000125746.
    InParanoidiP46422.
    KOiK00799.
    OMAiQYAIMAI.
    PhylomeDBiP46422.

    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]

    Sequencei

    Sequence statusi: Complete.

    P46422-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGIKVFGHP ASIATRRVLI ALHEKNLDFE LVHVELKDGE HKKEPFLSRN    50
    PFGQVPAFED GDLKLFESRA ITQYIAHRYE NQGTNLLQTD SKNISQYAIM 100
    AIGMQVEDHQ FDPVASKLAF EQIFKSIYGL TTDEAVVAEE EAKLAKVLDV 150
    YEARLKEFKY LAGETFTLTD LHHIPAIQYL LGTPTKKLFT ERPRVNEWVA 200
    EITKRPASEK VQ 212
    Length:212
    Mass (Da):24,129
    Last modified:January 23, 2007 - v3
    Checksum:i90A1CBEEEBAC815B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75303 mRNA. Translation: CAA53051.1.
    L07589 mRNA. Translation: AAA32800.1.
    L11601 mRNA. Translation: AAA32801.1.
    AC002330 Genomic DNA. Translation: AAC78264.1.
    AL161494 Genomic DNA. Translation: CAB80745.1.
    CP002687 Genomic DNA. Translation: AEE82183.1.
    AF324681 mRNA. Translation: AAG40032.1.
    AF326903 mRNA. Translation: AAG41485.1.
    AF349527 mRNA. Translation: AAK15574.1.
    AY039580 mRNA. Translation: AAK62635.1.
    AY056082 mRNA. Translation: AAL06970.1.
    PIRiS35268.
    RefSeqiNP_192161.1. NM_116486.2.
    UniGeneiAt.22195.
    At.24972.

    Genome annotation databases

    EnsemblPlantsiAT4G02520.1; AT4G02520.1; AT4G02520.
    GeneIDi827931.
    KEGGiath:AT4G02520.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75303 mRNA. Translation: CAA53051.1 .
    L07589 mRNA. Translation: AAA32800.1 .
    L11601 mRNA. Translation: AAA32801.1 .
    AC002330 Genomic DNA. Translation: AAC78264.1 .
    AL161494 Genomic DNA. Translation: CAB80745.1 .
    CP002687 Genomic DNA. Translation: AEE82183.1 .
    AF324681 mRNA. Translation: AAG40032.1 .
    AF326903 mRNA. Translation: AAG41485.1 .
    AF349527 mRNA. Translation: AAK15574.1 .
    AY039580 mRNA. Translation: AAK62635.1 .
    AY056082 mRNA. Translation: AAL06970.1 .
    PIRi S35268.
    RefSeqi NP_192161.1. NM_116486.2.
    UniGenei At.22195.
    At.24972.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BX9 X-ray 2.60 A 2-212 [» ]
    1GNW X-ray 2.20 A/B 2-212 [» ]
    ProteinModelPortali P46422.
    SMRi P46422. Positions 3-212.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 13222. 6 interactions.

    2D gel databases

    SWISS-2DPAGE P46422.

    Proteomic databases

    PRIDEi P46422.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G02520.1 ; AT4G02520.1 ; AT4G02520 .
    GeneIDi 827931.
    KEGGi ath:AT4G02520.

    Organism-specific databases

    TAIRi AT4G02520.

    Phylogenomic databases

    HOGENOMi HOG000125746.
    InParanoidi P46422.
    KOi K00799.
    OMAi QYAIMAI.
    PhylomeDBi P46422.

    Enzyme and pathway databases

    BioCyci ARA:AT4G02520-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P46422.

    Gene expression databases

    Genevestigatori P46422.

    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. "Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: identification of a glutathione S-transferase."
      Zettl R., Schell J., Palme K.
      Proc. Natl. Acad. Sci. U.S.A. 91:689-693(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "An Arabidopsis gene with homology to glutathione S-transferases is regulated by ethylene."
      Zhou J., Goldsbrough P.B.
      Plant Mol. Biol. 22:517-523(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY ETHYLENE.
      Tissue: Leaf.
    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. "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.
    7. "The rapid induction of glutathione S-transferases AtGSTF2 and AtGSTF6 by avirulent Pseudomonas syringae is the result of combined salicylic acid and ethylene signaling."
      Lieberherr D., Wagner U., Dubuis P.H., Metraux J.P., Mauch F.
      Plant Cell Physiol. 44:750-757(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Arabidopsis AtGSTF2 is regulated by ethylene and auxin, and encodes a glutathione S-transferase that interacts with flavonoids."
      Smith A.P., Nourizadeh S.D., Peer W.A., Xu J., Bandyopadhyay A., Murphy A.S., Goldsbrough P.B.
      Plant J. 36:433-442(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    9. "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 BY COPPER.
    10. "Gene expression and microscopic analysis of Arabidopsis exposed to chloroacetanilide herbicides and explosive compounds. A phytoremediation approach."
      Mezzari M.P., Walters K., Jelinkova M., Shih M.C., Just C.L., Schnoor J.L.
      Plant Physiol. 138:858-869(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    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. "The Arabidopsis phi class glutathione transferase AtGSTF2: binding and regulation by biologically active heterocyclic ligands."
      Dixon D.P., Sellars J.D., Edwards R.
      Biochem. J. 438:63-70(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Three-dimensional structure of glutathione S-transferase from Arabidopsis thaliana at 2.2-A resolution: structural characterization of herbicide-conjugating plant glutathione S-transferases and a novel active site architecture."
      Reinemer P., Prade L., Hof P., Neuefeind T., Huber R., Zettl R., Palme K., Schell J., Koelln I., Bartunik H.D., Bieseler B.
      J. Mol. Biol. 255:289-309(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH HEXYLGLUTATHIONE.
    14. "Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase -- explanations for the selectivity of the enzyme in plants."
      Prade L., Huber R., Bieseler B.
      Structure 6:1445-1452(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.

    Entry informationi

    Entry nameiGSTF2_ARATH
    AccessioniPrimary (citable) accession number: P46422
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3