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P42760 (GSTF6_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 F6

Short name=AtGSTF6
EC=2.5.1.18
Alternative name(s):
AtGSTF3
GST class-phi member 6
Glutathione S-transferase 1
Short name=AtGST1
Protein EARLY RESPONSE TO DEHYDRATION 11
Gene names
Name:GSTF6
Synonyms:ERD11, GST1, GSTF3
Ordered Locus Names:At1g02930
ORF Names:F22D16.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in camalexin biosynthesis by probably catalyzing the conjugation of GSH with indole-3-acetonitrile (IAN). 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. Ref.10

Catalytic activity

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

Subcellular location

Cytoplasmcytosol Probable.

Induction

By dehydration stress, salicylic acid, ethylene, methyl jasmonate, auxin, H2O2, copper, metolachlor, and the pathogens P.syringae and Hyaloperonospora parasitica. Ref.7 Ref.8 Ref.9

Disruption phenotype

No visible phenotype under normal growth conditions, but reduced levels of camalexin production during infection by B.cinerea. 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 processDetoxification
Plant defense
Stress response
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response to bacterium

Inferred from expression pattern PubMed 17028151. Source: TAIR

response to cadmium ion

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

response to oxidative stress

Inferred from direct assay PubMed 12492832. 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 water deprivation

Inferred from expression pattern Ref.1. Source: TAIR

toxin catabolic process

Traceable author statement Ref.7. Source: TAIR

   Cellular_componentcell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

cytoplasm

Non-traceable author statement Ref.7. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

mitochondrion

Inferred from direct assay PubMed 12492832PubMed 14671022. 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 PubMed 21631432. Source: TAIR

cobalt ion binding

Inferred from direct assay PubMed 20018591. Source: TAIR

copper ion binding

Inferred from direct assay PubMed 16526091. Source: TAIR

glutathione binding

Inferred from direct assay PubMed 15159623. Source: TAIR

glutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

quercitrin binding

Inferred from direct assay PubMed 21631432. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 208207Glutathione S-transferase F6
PRO_0000185846

Regions

Domain2 – 8382GST N-terminal
Domain89 – 208120GST C-terminal
Region12 – 132Glutathione binding By similarity
Region41 – 422Glutathione binding By similarity
Region54 – 552Glutathione binding By similarity
Region67 – 682Glutathione binding By similarity

Experimental info

Sequence conflict121S → F in BAA04553. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42760 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 113CED008A11902F

FASTA20823,486
        10         20         30         40         50         60 
MAGIKVFGHP ASTATRRVLI ALHEKNVDFE FVHVELKDGE HKKEPFILRN PFGKVPAFED 

        70         80         90        100        110        120 
GDFKIFESRA ITQYIAHEFS DKGNNLLSTG KDMAIIAMGI EIESHEFDPV GSKLVWEQVL 

       130        140        150        160        170        180 
KPLYGMTTDK TVVEEEEAKL AKVLDVYEHR LGESKYLASD HFTLVDLHTI PVIQYLLGTP 

       190        200 
TKKLFDERPH VSAWVADITS RPSAQKVL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of two cDNAs (ERD11 and ERD13) for dehydration-inducible genes that encode putative glutathione S-transferases in Arabidopsis thaliana L."
Kiyosue T., Yamaguchi-Shinozaki K., Shinozaki K.
FEBS Lett. 335:189-192(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Characterization of a glutathione S-transferase gene ATGST1 in Arabidopsis thaliana."
Yang K.Y., Kim E.Y., Kim K.S., Choi S.N., Guh J.O., Kim K.C., Cho B.-H.
Plant Cell Rep. 17:700-704(1999)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Landsberg erecta.
[3]Yu G.-L., Ausubel F.M.
Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"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.
[7]"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: INDUCTION, GENE FAMILY, NOMENCLATURE.
[8]"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.
[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]"Glutathione-indole-3-acetonitrile is required for camalexin biosynthesis in Arabidopsis thaliana."
Su T., Xu J., Li Y., Lei L., Zhao L., Yang H., Feng J., Liu G., Ren D.
Plant Cell 23:364-380(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D17672 mRNA. Translation: BAA04553.1.
Y11727 Genomic DNA. Translation: CAA72413.1.
L12057 Genomic RNA. No translation available.
AC009525 Genomic DNA. Translation: AAF02873.1.
CP002684 Genomic DNA. Translation: AEE27497.1.
CP002684 Genomic DNA. Translation: AEE27498.1.
AY050332 mRNA. Translation: AAK91349.1.
AY097392 mRNA. Translation: AAM19908.1.
PIRG86159.
S39541.
RefSeqNP_001184893.1. NM_001197964.1.
NP_171792.1. NM_100174.2.
UniGeneAt.20350.
At.23846.

3D structure databases

ProteinModelPortalP42760.
SMRP42760. Positions 3-207.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid24750. 2 interactions.
IntActP42760. 3 interactions.
STRING3702.AT1G02930.1-P.

2D gel databases

SWISS-2DPAGEP42760.

Proteomic databases

PaxDbP42760.
PRIDEP42760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G02930.1; AT1G02930.1; AT1G02930.
AT1G02930.2; AT1G02930.2; AT1G02930.
GeneID839515.
KEGGath:AT1G02930.

Organism-specific databases

TAIRAT1G02930.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125746.
InParanoidP42760.
KOK00799.
OMALWLEVES.
PhylomeDBP42760.

Enzyme and pathway databases

BioCycARA:AT1G02930-MONOMER.
ARA:GQT-844-MONOMER.

Gene expression databases

GenevestigatorP42760.

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...

Entry information

Entry nameGSTF6_ARATH
AccessionPrimary (citable) accession number: P42760
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 116 of the entry and version 2 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names