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Protein

Glutathione S-transferase F6

Gene

GSTF6

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. camalexin binding Source: TAIR
  2. cobalt ion binding Source: TAIR
  3. copper ion binding Source: TAIR
  4. glutathione binding Source: TAIR
  5. glutathione transferase activity Source: UniProtKB-EC
  6. quercitrin binding Source: TAIR

GO - Biological processi

  1. defense response to bacterium Source: TAIR
  2. response to cadmium ion Source: TAIR
  3. response to oxidative stress Source: TAIR
  4. response to salt stress Source: TAIR
  5. response to toxic substance Source: UniProtKB-KW
  6. response to water deprivation Source: TAIR
  7. toxin catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Detoxification, Plant defense, Stress response

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase F6 (EC:2.5.1.18)
Short name:
AtGSTF6
Alternative name(s):
AtGSTF3
GST class-phi member 6
Glutathione S-transferase 1
Short name:
AtGST1
Protein EARLY RESPONSE TO DEHYDRATION 11
Gene namesi
Name:GSTF6
Synonyms:ERD11, GST1, GSTF3
Ordered Locus Names:At1g02930
ORF Names:F22D16.7
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G02930.

Subcellular locationi

Cytoplasmcytosol Curated

GO - Cellular componenti

  1. cell wall Source: TAIR
  2. cytoplasm Source: TAIR
  3. cytosol Source: TAIR
  4. mitochondrion Source: TAIR
  5. plasmodesma Source: TAIR
  6. vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but reduced levels of camalexin production during infection by B.cinerea.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 208207Glutathione S-transferase F6PRO_0000185846Add
BLAST

Proteomic databases

PaxDbiP42760.
PRIDEiP42760.

2D gel databases

SWISS-2DPAGEP42760.

Expressioni

Inductioni

By dehydration stress, salicylic acid, ethylene, methyl jasmonate, auxin, H2O2, copper, metolachlor, and the pathogens P.syringae and Hyaloperonospora parasitica.3 Publications

Gene expression databases

GenevestigatoriP42760.

Interactioni

Protein-protein interaction databases

BioGridi24750. 2 interactions.
IntActiP42760. 3 interactions.
STRINGi3702.AT1G02930.1-P.

Structurei

3D structure databases

ProteinModelPortaliP42760.
SMRiP42760. Positions 3-207.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GST N-terminalAdd
BLAST
Domaini89 – 208120GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 132Glutathione bindingBy similarity
Regioni41 – 422Glutathione bindingBy similarity
Regioni54 – 552Glutathione bindingBy similarity
Regioni67 – 682Glutathione 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.
InParanoidiP42760.
KOiK00799.
OMAiYIAHEFS.
PhylomeDBiP42760.

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.

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

P42760-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGIKVFGHP ASTATRRVLI ALHEKNVDFE FVHVELKDGE HKKEPFILRN
60 70 80 90 100
PFGKVPAFED GDFKIFESRA ITQYIAHEFS DKGNNLLSTG KDMAIIAMGI
110 120 130 140 150
EIESHEFDPV GSKLVWEQVL KPLYGMTTDK TVVEEEEAKL AKVLDVYEHR
160 170 180 190 200
LGESKYLASD HFTLVDLHTI PVIQYLLGTP TKKLFDERPH VSAWVADITS

RPSAQKVL
Length:208
Mass (Da):23,486
Last modified:November 1, 1997 - v2
Checksum:i113CED008A11902F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121S → F in BAA04553. (PubMed:8253194)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG86159.
S39541.
RefSeqiNP_001184893.1. NM_001197964.1.
NP_171792.1. NM_100174.2.
UniGeneiAt.20350.
At.23846.

Genome annotation databases

EnsemblPlantsiAT1G02930.1; AT1G02930.1; AT1G02930.
AT1G02930.2; AT1G02930.2; AT1G02930.
GeneIDi839515.
KEGGiath:AT1G02930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG86159.
S39541.
RefSeqiNP_001184893.1. NM_001197964.1.
NP_171792.1. NM_100174.2.
UniGeneiAt.20350.
At.23846.

3D structure databases

ProteinModelPortaliP42760.
SMRiP42760. Positions 3-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi24750. 2 interactions.
IntActiP42760. 3 interactions.
STRINGi3702.AT1G02930.1-P.

2D gel databases

SWISS-2DPAGEP42760.

Proteomic databases

PaxDbiP42760.
PRIDEiP42760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G02930.1; AT1G02930.1; AT1G02930.
AT1G02930.2; AT1G02930.2; AT1G02930.
GeneIDi839515.
KEGGiath:AT1G02930.

Organism-specific databases

TAIRiAT1G02930.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125746.
InParanoidiP42760.
KOiK00799.
OMAiYIAHEFS.
PhylomeDBiP42760.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatoriP42760.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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.

Entry informationi

Entry nameiGSTF6_ARATH
AccessioniPrimary (citable) accession number: P42760
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: January 7, 2015
This is version 118 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.