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O80852 (GSTF9_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 104. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase F9

Short name=AtGSTF9
EC=2.5.1.18
Alternative name(s):
AtGSTF7
GST class-phi member 9
Gene names
Name:GSTF9
Synonyms:GLUTTR, GSTF7
Ordered Locus Names:At2g30860
ORF Names:F7F1.7
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC), and glutathione peroxidase activity toward cumene hydroperoxide and linoleic acid-13-hydroperoxide. 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.6 Ref.7

Catalytic activity

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

Subcellular location

Cytoplasmcytosol Probable.

Induction

By zinc in roots and benoxacor. Ref.7 Ref.8

Sequence similarities

Belongs to the GST superfamily. Phi family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Sequence caution

The sequence BAH56998.1 differs from that shown. Reason: Frameshift at position 154.

Ontologies

Keywords
   Biological processDetoxification
Stress response
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionOxidoreductase
Peroxidase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response

Inferred from expression pattern Ref.7. Source: TAIR

defense response to bacterium

Inferred from expression pattern PubMed 17028151. Source: TAIR

response to cadmium ion

Inferred from expression pattern PubMed 20005002. Source: TAIR

response to toxic substance

Inferred from electronic annotation. Source: UniProtKB-KW

response to zinc ion

Inferred from expression pattern Ref.8. 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 18431481. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 18633119. Source: TAIR

cytoplasm

Non-traceable author statement Ref.6. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17644812. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

thylakoid

Inferred from direct assay PubMed 11826309PubMed 16648217. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functioncopper ion binding

Inferred from direct assay PubMed 16526091PubMed 20018591. Source: TAIR

glutathione binding

Inferred from direct assay PubMed 15159623. Source: TAIR

glutathione peroxidase activity

Inferred from direct assay Ref.7. Source: TAIR

glutathione transferase activity

Inferred from direct assay Ref.7. Source: TAIR

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O80852-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O80852-2)

The sequence of this isoform differs from the canonical sequence as follows:
     154-166: KYLAGDFVSLADL → NIHSQLKMCSSSW
     167-215: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 215214Glutathione S-transferase F9
PRO_0000413544

Regions

Domain2 – 8180GST N-terminal
Domain88 – 215128GST C-terminal
Region39 – 402Glutathione binding By similarity
Region52 – 532Glutathione binding By similarity
Region65 – 662Glutathione binding By similarity

Amino acid modifications

Modified residue121Phosphoserine Ref.9

Natural variations

Alternative sequence154 – 16613KYLAG…SLADL → NIHSQLKMCSSSW in isoform 2.
VSP_041938
Alternative sequence167 – 21549Missing in isoform 2.
VSP_041939

Experimental info

Sequence conflict871K → E in BAH56998. Ref.5
Sequence conflict147 – 1515EAHLS → KAQRA in CAA72973. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 961996318A186F9C

FASTA21524,146
        10         20         30         40         50         60 
MVLKVYGPHF ASPKRALVTL IEKGVAFETI PVDLMKGEHK QPAYLALQPF GTVPAVVDGD 

        70         80         90        100        110        120 
YKIFESRAVM RYVAEKYRSQ GPDLLGKTVE DRGQVEQWLD VEATTYHPPL LNLTLHIMFA 

       130        140        150        160        170        180 
SVMGFPSDEK LIKESEEKLA GVLDVYEAHL SKSKYLAGDF VSLADLAHLP FTDYLVGPIG 

       190        200        210 
KAYMIKDRKH VSAWWDDISS RPAWKETVAK YSFPA 

« Hide

Isoform 2 [UniParc].

Checksum: 4B1DB5773B081D65
Show »

FASTA16618,622

References

« Hide 'large scale' references
[1]"Cloning, expression and characterisation of an Arabidopsis glutathione transferase gene."
Jemth P., Jiang F., Mannervik B.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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] (ISOFORM 1).
Strain: cv. Columbia.
[5]"Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
Tissue: Rosette leaf.
[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, GENE FAMILY, NOMENCLATURE.
Strain: cv. Columbia.
[7]"Characterization of two Arabidopsis thaliana glutathione S-transferases."
Nutricati E., Miceli A., Blando F., De Bellis L.
Plant Cell Rep. 25:997-1005(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[8]"Identification of zinc-responsive proteins in the roots of Arabidopsis thaliana using a highly improved method of two-dimensional electrophoresis."
Fukao Y., Ferjani A., Fujiwara M., Nishimori Y., Ohtsu I.
Plant Cell Physiol. 50:2234-2239(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY ZINC.
[9]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y12295 mRNA. Translation: CAA72973.1.
AC004669 Genomic DNA. Translation: AAC20720.1.
CP002685 Genomic DNA. Translation: AEC08448.1.
CP002685 Genomic DNA. Translation: AEC08449.1.
AF372905 mRNA. Translation: AAK49621.1.
BT002679 mRNA. Translation: AAO11595.1.
AK318883 mRNA. Translation: BAH56998.1. Frameshift.
PIRE84713.
RefSeqNP_001077983.1. NM_001084514.1. [O80852-2]
NP_180643.1. NM_128638.2. [O80852-1]
UniGeneAt.22585.
At.74970.
At.74982.

3D structure databases

ProteinModelPortalO80852.
SMRO80852. Positions 3-214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid2985. 1 interaction.
IntActO80852. 1 interaction.
STRING3702.AT2G30860.1-P.

Proteomic databases

PRIDEO80852.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G30860.1; AT2G30860.1; AT2G30860. [O80852-1]
GeneID817636.
KEGGath:AT2G30860.

Organism-specific databases

TAIRAT2G30860.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000125746.
InParanoidO80852.
KOK00799.
OMAVWIISAK.
PhylomeDBO80852.

Gene expression databases

GenevestigatorO80852.

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 nameGSTF9_ARATH
AccessionPrimary (citable) accession number: O80852
Secondary accession number(s): A8MR26, C0Z2R9, O23626
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: November 1, 1998
Last modified: May 14, 2014
This is version 104 of the entry and version 1 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