Q9ZRW8 (GSTUJ_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytosol 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.

Ontologies

Keywords
Biological process	Detoxification Stress response
Cellular component	Cytoplasm
Molecular function	Oxidoreductase Peroxidase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to water deprivation Inferred from expression pattern Ref.1. Source: TAIR response to cadmium ion Inferred from expression pattern PubMed 16502469. Source: TAIR response to oxidative stress Inferred from expression pattern Ref.1. Source: TAIR response to toxic substance Inferred from electronic annotation. Source: UniProtKB-KW toxin catabolic process Traceable author statement Ref.6. Source: TAIR
Cellular_component	chloroplast stroma Inferred from direct assay PubMed 16207701. Source: TAIR cytosol Inferred from direct assay PubMed 21166475. Source: TAIR plasma membrane Inferred from direct assay PubMed 17644812. Source: TAIR vacuolar membrane Inferred from direct assay PubMed 17151019. Source: TAIR
Molecular_function	glutathione binding Inferred from direct assay PubMed 15159623. Source: TAIR glutathione transferase activity Inferred from sequence or structural similarity Ref.1. Source: TAIR peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 219	219	Glutathione S-transferase U19		PRO_0000413565
Regions
	Domain	3 – 82	80	GST N-terminal
	Domain	88 – 208	121	GST C-terminal
	Region	13 – 14	2	Glutathione binding By similarity
	Region	39 – 40	2	Glutathione binding By similarity
	Region	53 – 54	2	Glutathione binding By similarity
	Region	66 – 67	2	Glutathione binding By similarity
Experimental info
	Sequence conflict	16	1	G → R in AAM64593. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9ZRW8 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: E79AABD8C14C6F15	FASTA	219	25,651
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
+	Additional computationally mapped references.

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.
IPI	IPI00655471.
PIR	T51607.
RefSeq	NP_565178.1. NM_106485.3.
UniGene	At.25493. At.67704.
3D structure databases
ProteinModelPortal	Q9ZRW8.
SMR	Q9ZRW8. Positions 4-216.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ZRW8. 5 interactions.
STRING	3702.AT1G78380.1-P.
Proteomic databases
PRIDE	Q9ZRW8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G78380.1; AT1G78380.1; AT1G78380.
GeneID	844174.
KEGG	ath:AT1G78380.
Organism-specific databases
TAIR	At1g78380.
Phylogenomic databases
HOGENOM	HOG000125749.
InParanoid	Q9ZRW8.
KO	K00799.
OMA	PSYERYG.
PhylomeDB	Q9ZRW8.
Enzyme and pathway databases
BioCyc	ARA:AT1G78380-MONOMER. MetaCyc:AT1G78380-MONOMER.
Gene expression databases
ArrayExpress	Q9ZRW8.
Genevestigator	Q9ZRW8.
Family and domain databases
Gene3D	1.20.1050.10. 1 hit. 3.40.30.10. 1 hit.
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF00043. GST_C. 1 hit. [Graphical view]
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GSTUJ_ARATH

Accession

Primary (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:	May 29, 2013
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program