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P46422

- GSTF2_ARATH

UniProt

P46422 - GSTF2_ARATH

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Protein
Glutathione S-transferase F2
Gene
GSTF2, PM24.1, At4g02520, T10P11.18
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 212212Glutathione S-transferase F2
PRO_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.

Protein-protein interaction databases

BioGridi13222. 6 interactions.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP46422.

Family & Domainsi

Domains and Repeats

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

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...

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 127 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

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