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Protein

Glutathione S-transferase F7

Gene

GSTF7

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

Functioni

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.By similarity

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  1. defense response to bacterium Source: TAIR
  2. defense response to fungus, incompatible interaction Source: TAIR
  3. response to cadmium ion Source: TAIR
  4. response to salt stress Source: TAIR
  5. response to toxic substance Source: UniProtKB-KW
  6. toxin catabolic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Detoxification, Stress response

Enzyme and pathway databases

BioCyciARA:AT1G02920-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase F7 (EC:2.5.1.18)
Alternative name(s):
AtGSTF8
GST class-phi member 7
Glutathione S-transferase 11
Gene namesi
Name:GSTF7
Synonyms:GST11, GSTF8
Ordered Locus Names:At1g02920
ORF Names:F22D16.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G02920.

Subcellular locationi

Cytoplasmcytosol Curated

GO - Cellular componenti

  1. cytoplasm Source: TAIR
  2. cytosol Source: UniProtKB-SubCell
  3. nucleus Source: TAIR
  4. vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 209208Glutathione S-transferase F7PRO_0000185852Add
BLAST

Proteomic databases

PaxDbiQ9SRY5.
PRIDEiQ9SRY5.

2D gel databases

SWISS-2DPAGEQ9SRY5.

Expressioni

Inductioni

By ethylene, salicylic acid, copper and the bacterial pathogen P.syringae.3 Publications

Gene expression databases

GenevestigatoriQ9SRY5.

Interactioni

Protein-protein interaction databases

BioGridi24530. 1 interaction.
IntActiQ9SRY5. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9SRY5.
SMRiQ9SRY5. Positions 3-208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8382GST N-terminalAdd
BLAST
Domaini90 – 209120GST 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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi135 – 1384Poly-Glu

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.
InParanoidiQ9SRY5.
KOiK00799.
OMAiKEPFIFR.
PhylomeDBiQ9SRY5.

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.

Q9SRY5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGIKVFGHP ASTATRRVLI ALHEKNLDFE FVHIELKDGE HKKEPFIFRN
60 70 80 90 100
PFGKVPAFED GDFKLFESRA ITQYIAHFYS DKGNQLVSLG SKDIAGIAMG
110 120 130 140 150
IEIESHEFDP VGSKLVWEQV LKPLYGMTTD KTVVEEEEAK LAKVLDVYEH
160 170 180 190 200
RLGESKYLAS DKFTLVDLHT IPVIQYLLGT PTKKLFDERP HVSAWVADIT

SRPSAKKVL
Length:209
Mass (Da):23,598
Last modified:February 5, 2008 - v3
Checksum:iFD2CC0FD28A31ACC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871D → A in CAA74639 (Ref. 1) Curated
Sequence conflicti187 – 1871D → A in AAG30126 (PubMed:12090627).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14251 Genomic DNA. Translation: CAA74639.1.
AF288177 mRNA. Translation: AAG30126.1.
AC009525 Genomic DNA. Translation: AAF02874.1.
CP002684 Genomic DNA. Translation: AEE27496.1.
AY062642 mRNA. Translation: AAL32720.1.
AY093281 mRNA. Translation: AAM13280.1.
PIRiF86159.
RefSeqiNP_171791.1. NM_100173.3.
UniGeneiAt.20350.
At.23846.
At.71571.

Genome annotation databases

EnsemblPlantsiAT1G02920.1; AT1G02920.1; AT1G02920.
GeneIDi839295.
KEGGiath:AT1G02920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14251 Genomic DNA. Translation: CAA74639.1.
AF288177 mRNA. Translation: AAG30126.1.
AC009525 Genomic DNA. Translation: AAF02874.1.
CP002684 Genomic DNA. Translation: AEE27496.1.
AY062642 mRNA. Translation: AAL32720.1.
AY093281 mRNA. Translation: AAM13280.1.
PIRiF86159.
RefSeqiNP_171791.1. NM_100173.3.
UniGeneiAt.20350.
At.23846.
At.71571.

3D structure databases

ProteinModelPortaliQ9SRY5.
SMRiQ9SRY5. Positions 3-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi24530. 1 interaction.
IntActiQ9SRY5. 2 interactions.

2D gel databases

SWISS-2DPAGEQ9SRY5.

Proteomic databases

PaxDbiQ9SRY5.
PRIDEiQ9SRY5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G02920.1; AT1G02920.1; AT1G02920.
GeneIDi839295.
KEGGiath:AT1G02920.

Organism-specific databases

TAIRiAT1G02920.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000125746.
InParanoidiQ9SRY5.
KOiK00799.
OMAiKEPFIFR.
PhylomeDBiQ9SRY5.

Enzyme and pathway databases

BioCyciARA:AT1G02920-MONOMER.

Gene expression databases

GenevestigatoriQ9SRY5.

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 a novel glutathione S-transferase gene in Arabidopsis thaliana."
    Yang K.Y., Kim C.S., Kim K.C., Cho B.-H.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: cv. Landsberg erecta.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: cv. Columbia.
  3. "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.
  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. "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.
  7. "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.

Entry informationi

Entry nameiGSTF7_ARATH
AccessioniPrimary (citable) accession number: Q9SRY5
Secondary accession number(s): O23720, Q541C6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: February 5, 2008
Last modified: March 4, 2015
This is version 111 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

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.