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P46422 (GSTF2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase F2

Short name=AtGSTF2
EC=2.5.1.18
Alternative name(s):
24 kDa auxin-binding protein
Short name=AtPM24
GST class-phi member 2
Gene names
Name:GSTF2
Synonyms:PM24.1
Ordered Locus Names:At4g02520
ORF Names:T10P11.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.12

Catalytic activity

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

Subunit structure

Homodimer.

Subcellular location

Cytoplasmcytosol. Microsome. Endoplasmic reticulum. Note: Plasma membrane vesicles. Ref.11

Tissue specificity

Expressed in the root-shoot transition zone and root tips. Ref.8

Induction

By ethylene, auxin, glutathione, salicylic acid, copper, paraquat, acetochlor, metolachlor and the pathogens P.syringae and Hyaloperonospora parasitica. Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Sequence similarities

Belongs to the GST superfamily. Phi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Ontologies

Keywords
   Biological processAuxin signaling pathway
Detoxification
Plant defense
Stress response
   Cellular componentCytoplasm
Endoplasmic reticulum
Microsome
   Molecular functionOxidoreductase
Peroxidase
Transferase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processauxin-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from expression pattern PubMed 17028151. Source: TAIR

defense response to fungus

Inferred from expression pattern PubMed 21711359. Source: TAIR

response to cadmium ion

Inferred from expression pattern PubMed 16502469PubMed 17075075. Source: TAIR

response to cold

Inferred from expression pattern PubMed 14535880. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 17916636. Source: TAIR

response to toxic substance

Inferred from electronic annotation. Source: UniProtKB-KW

response to zinc ion

Inferred from expression pattern PubMed 19880396. Source: TAIR

toxin catabolic process

Traceable author statement Ref.6. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 16207701PubMed 18633119PubMed 20061580. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Inferred from direct assay Ref.1. Source: TAIR

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17317660Ref.1. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functioncamalexin binding

Inferred from direct assay Ref.12. Source: TAIR

glutathione binding

Inferred from direct assay PubMed 15159623. Source: TAIR

glutathione transferase activity

Inferred from direct assay Ref.1. Source: TAIR

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

quercitrin binding

Inferred from direct assay Ref.12. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Glutathione S-transferase F2
PRO_0000185848

Regions

Domain2 – 8382GST N-terminal
Domain93 – 212120GST C-terminal
Region12 – 132Glutathione binding
Region41 – 422Glutathione binding
Region54 – 552Glutathione binding
Region67 – 682Glutathione binding

Secondary structure

.......................................... 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46422 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 90A1CBEEEBAC815B

FASTA21224,129
        10         20         30         40         50         60 
MAGIKVFGHP ASIATRRVLI ALHEKNLDFE LVHVELKDGE HKKEPFLSRN PFGQVPAFED 

        70         80         90        100        110        120 
GDLKLFESRA ITQYIAHRYE NQGTNLLQTD SKNISQYAIM AIGMQVEDHQ FDPVASKLAF 

       130        140        150        160        170        180 
EQIFKSIYGL TTDEAVVAEE EAKLAKVLDV YEARLKEFKY LAGETFTLTD LHHIPAIQYL 

       190        200        210 
LGTPTKKLFT ERPRVNEWVA EITKRPASEK VQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS35268.
RefSeqNP_192161.1. NM_116486.2.
UniGeneAt.22195.
At.24972.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BX9X-ray2.60A2-212[»]
1GNWX-ray2.20A/B2-212[»]
ProteinModelPortalP46422.
SMRP46422. Positions 3-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13222. 6 interactions.

2D gel databases

SWISS-2DPAGEP46422.

Proteomic databases

PRIDEP46422.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G02520.1; AT4G02520.1; AT4G02520.
GeneID827931.
KEGGath:AT4G02520.

Organism-specific databases

TAIRAT4G02520.

Phylogenomic databases

HOGENOMHOG000125746.
InParanoidP46422.
KOK00799.
OMAQYAIMAI.
PhylomeDBP46422.

Enzyme and pathway databases

BioCycARA:AT4G02520-MONOMER.

Gene expression databases

GenevestigatorP46422.

Family and domain databases

Gene3D1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46422.

Entry information

Entry nameGSTF2_ARATH
AccessionPrimary (citable) accession number: P46422
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names