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Q9SRY5 (GSTF7_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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 F7

EC=2.5.1.18
Alternative name(s):
AtGSTF8
GST class-phi member 7
Glutathione S-transferase 11
Gene names
Name:GSTF7
Synonyms:GST11, GSTF8
Ordered Locus Names:At1g02920
ORF Names:F22D16.8
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subcellular location

Cytoplasmcytosol Probable.

Induction

By ethylene, salicylic acid, copper and the bacterial pathogen P.syringae. Ref.2 Ref.6 Ref.7

Sequence similarities

Belongs to the GST superfamily. Phi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 209208Glutathione S-transferase F7
PRO_0000185852

Regions

Domain2 – 8382GST N-terminal
Domain90 – 209120GST C-terminal
Region12 – 132Glutathione binding By similarity
Region41 – 422Glutathione binding By similarity
Region54 – 552Glutathione binding By similarity
Region67 – 682Glutathione binding By similarity
Compositional bias135 – 1384Poly-Glu

Experimental info

Sequence conflict1871D → A in CAA74639. Ref.1
Sequence conflict1871D → A in AAG30126. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9SRY5 [UniParc].

Last modified February 5, 2008. Version 3.
Checksum: FD2CC0FD28A31ACC

FASTA20923,598
        10         20         30         40         50         60 
MAGIKVFGHP ASTATRRVLI ALHEKNLDFE FVHIELKDGE HKKEPFIFRN PFGKVPAFED 

        70         80         90        100        110        120 
GDFKLFESRA ITQYIAHFYS DKGNQLVSLG SKDIAGIAMG IEIESHEFDP VGSKLVWEQV 

       130        140        150        160        170        180 
LKPLYGMTTD KTVVEEEEAK LAKVLDVYEH RLGESKYLAS DKFTLVDLHT IPVIQYLLGT 

       190        200 
PTKKLFDERP HVSAWVADIT SRPSAKKVL 

« Hide

References

« Hide 'large scale' references
[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. 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.
[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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRF86159.
RefSeqNP_171791.1. NM_100173.3.
UniGeneAt.20350.
At.23846.
At.71571.

3D structure databases

ProteinModelPortalQ9SRY5.
SMRQ9SRY5. Positions 3-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid24530. 1 interaction.
IntActQ9SRY5. 2 interactions.

2D gel databases

SWISS-2DPAGEQ9SRY5.

Proteomic databases

PaxDbQ9SRY5.
PRIDEQ9SRY5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G02920.1; AT1G02920.1; AT1G02920.
GeneID839295.
KEGGath:AT1G02920.

Organism-specific databases

TAIRAT1G02920.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125746.
InParanoidQ9SRY5.
KOK00799.
OMAKEPFIFR.
PhylomeDBQ9SRY5.
ProtClustDBCLSN2679613.

Enzyme and pathway databases

BioCycARA:AT1G02920-MONOMER.

Gene expression databases

GenevestigatorQ9SRY5.

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 nameGSTF7_ARATH
AccessionPrimary (citable) accession number: Q9SRY5
Secondary accession number(s): O23720, Q541C6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 106 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names