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Q9ZRW8 (GSTUJ_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. 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 U19

Short name=AtGSTU19
EC=2.5.1.18
Alternative name(s):
GST class-tau member 19
Glutathione S-transferase 8
Gene names
Name:GSTU19
Synonyms:GST8
Ordered Locus Names:At1g78380
ORF Names:F3F9.11
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length219 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the glutathionylation of 12-oxophytodienoate (OPDA). 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. Ref.6 Ref.9 Ref.10

Catalytic activity

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

Subcellular location

Cytoplasmcytosol Ref.11.

Induction

By dehydration stress, salicylic acid, ethylene, methyl jasmonate, auxin, H2O2, copper, benoxacor, isothiocyanates and the pathogen Hyaloperonospora parasitica. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12

Sequence similarities

Belongs to the GST superfamily. Tau 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 – 219218Glutathione S-transferase U19
PRO_0000413565

Regions

Domain3 – 8280GST N-terminal
Domain88 – 208121GST C-terminal
Region13 – 142Glutathione binding By similarity
Region39 – 402Glutathione binding By similarity
Region53 – 542Glutathione binding By similarity
Region66 – 672Glutathione binding By similarity

Experimental info

Sequence conflict161G → R in AAM64593. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9ZRW8 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E79AABD8C14C6F15

FASTA21925,651
        10         20         30         40         50         60 
MANEVILLDF WPSMFGMRTR IALREKGVEF EYREEDLRNK SPLLLQMNPI HKKIPVLIHN 

        70         80         90        100        110        120 
GKPVNESIIQ VQYIDEVWSH KNPILPSDPY LRAQARFWAD FIDKKLYDAQ RKVWATKGEE 

       130        140        150        160        170        180 
QEAGKKDFIE ILKTLESELG DKPYFSGDDF GYVDIALIGF YTWFPAYEKF ANFSIESEVP 

       190        200        210 
KLIAWVKKCL QRESVAKSLP DPEKVTEFVS ELRKKFVPE 

« Hide

References

« Hide 'large scale' references
[1]"Drought regulation of GST8, encoding the Arabidopsis homologue of ParC/Nt107 glutathione transferase/peroxidase."
Bianchi M.W., Roux C., Vartanian N.
Physiol. Plantarum 116:96-105(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[2]"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.
[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].
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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, INDUCTION, GENE FAMILY, NOMENCLATURE.
Strain: cv. Columbia.
[7]"Induction of glutathione S-transferases in Arabidopsis by herbicide safeners."
DeRidder B.P., Dixon D.P., Beussman D.J., Edwards R., Goldsbrough P.B.
Plant Physiol. 130:1497-1505(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[8]"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.
[9]"Organ-specific expression of glutathione S-transferases and the efficacy of herbicide safeners in Arabidopsis."
DeRidder B.P., Goldsbrough P.B.
Plant Physiol. 140:167-175(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[10]"Selective binding of glutathione conjugates of fatty acid derivatives by plant glutathione transferases."
Dixon D.P., Edwards R.
J. Biol. Chem. 284:21249-21256(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily."
Dixon D.P., Hawkins T., Hussey P.J., Edwards R.
J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[12]"Exogenously applied isothiocyanates enhance glutathione S-transferase expression in Arabidopsis but act as herbicides at higher concentrations."
Hara M., Yatsuzuka Y., Tabata K., Kuboi T.
J. Plant Physiol. 167:643-649(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ012571 mRNA. Translation: CAA10060.1.
AC013430 Genomic DNA. No translation available.
CP002684 Genomic DNA. Translation: AEE36099.1.
AF385691 mRNA. Translation: AAK60284.1.
AY078012 mRNA. Translation: AAL77713.1.
AY087032 mRNA. Translation: AAM64593.1.
PIRT51607.
RefSeqNP_565178.1. NM_106485.3.
UniGeneAt.25493.
At.67704.

3D structure databases

ProteinModelPortalQ9ZRW8.
SMRQ9ZRW8. Positions 4-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid29393. 6 interactions.
IntActQ9ZRW8. 5 interactions.
STRING3702.AT1G78380.1-P.

Proteomic databases

PRIDEQ9ZRW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G78380.1; AT1G78380.1; AT1G78380.
GeneID844174.
KEGGath:AT1G78380.

Organism-specific databases

TAIRAT1G78380.

Phylogenomic databases

HOGENOMHOG000125749.
InParanoidQ9ZRW8.
KOK00799.
OMASERAMKT.
PhylomeDBQ9ZRW8.

Enzyme and pathway databases

BioCycARA:AT1G78380-MONOMER.
MetaCyc:AT1G78380-MONOMER.

Gene expression databases

ArrayExpressQ9ZRW8.
GenevestigatorQ9ZRW8.

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.
PF13417. GST_N_3. 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 nameGSTUJ_ARATH
AccessionPrimary (citable) accession number: Q9ZRW8
Secondary accession number(s): Q8LBS1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 101 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