Glutathione S-transferase DHAR2 - Arabidopsis thaliana (Mouse-ear cress)

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Q9FRL8 (DHAR2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glutathione S-transferase DHAR2
EC=2.5.1.18

Alternative name(s):
Chloride intracellular channel homolog 2
Short name=CLIC homolog 2
Glutathione-dependent dehydroascorbate reductase 2
Short name=AtDHAR2
Short name=CytDHAR
Short name=GSH-dependent dehydroascorbate reductase 2

Gene names

Name:	DHAR2
Synonyms:	DHAR
Ordered Locus Names:	At1g75270
ORF Names:	F22H5.1

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exhibits glutathione-dependent thiol transferase and dehydroascorbate (DHA) reductase activities. Key component of the ascorbate recycling system. Involved in the redox homeostasis, especially in scavenging of ROS under oxidative stresses. Plays a role in ozone tolerance. Ref.8
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm › cytosol Potential.
Induction	By ozone. By salicylic acid (SA) (at protein level). Ref.7 Ref.8
Post-translational modification	Spontaneous S-glutathionylation in the presence of oxidized glutathione (GSSG).
Disruption phenotype	Mutant develops distinct foliar lesions under ozone exposure. Ref.8
Sequence similarities	Belongs to the GST superfamily. DHAR 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	Transferase
PTM	Glutathionylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glutathionylation Inferred from direct assay Ref.6. Source: TAIR response to stress Inferred from electronic annotation. Source: UniProtKB-KW response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR plasma membrane Inferred from direct assay PubMed 17644812. Source: TAIR
Molecular_function	glutathione binding Inferred from direct assay Ref.7. Source: TAIR glutathione dehydrogenase (ascorbate) activity Inferred from direct assay Ref.6. Source: TAIR glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

Glutathione S-transferase DHAR2

PRO_0000395482

Regions

Domain

10 – 83

GST N-terminal

Domain

84 – 213

130

GST C-terminal

Region

20 – 21

Glutathione binding By similarity

Region

46 – 47

Glutathione binding By similarity

Region

59 – 60

Glutathione binding By similarity

Region

72 – 73

Glutathione binding By similarity

Motif

20 – 25

Glutathione-binding Potential

Sites

Active site

By similarity

Amino acid modifications

Modified residue

S-glutathionyl cysteine

Modified residue

S-glutathionyl cysteine

Experimental info

Sequence conflict

195

N → K in AAM65005. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

Q9FRL8 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 23543B0F81F96041
Show »

FASTA

213

23,407

        10         20         30         40         50         60 
MALDICVKVA VGAPDVLGDC PFSQRVLLTL EEKKLPYKTH LINVSDKPQW FLDISPEGKV 

        70         80         90        100        110        120 
PVVKLDGKWV ADSDVIVGLL EEKYPEPSLK TPPEFASVGS KIFGAFVTFL KSKDANDGSE 

       130        140        150        160        170        180 
KALVDELEAL ENHLKTHSGP FVAGEKITAV DLSLAPKLYH LEVALGHYKN WSVPESLTSV 

       190        200        210 
RNYAKALFSR ESFENTKAKK EIVVAGWESK VNA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Increasing vitamin C content of plants through enhanced ascorbate recycling." Chen Z., Young T.E., Ling J., Chang S.C., Gallie D.R. Proc. Natl. Acad. Sci. U.S.A. 100:3525-3530(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. 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. 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]	"Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana." Dixon D.P., Davis B.G., Edwards R. J. Biol. Chem. 277:30859-30869(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENE FAMILY, IDENTIFICATION BY MASS SPECTROMETRY, S-GLUTATHIONYLATION.
[7]	"Proteomic analysis of glutathione S -transferases of Arabidopsis thaliana reveals differential salicylic acid-induced expression of the plant-specific phi and tau classes." Sappl P.G., Onate-Sanchez L., Singh K.B., Millar A.H. Plant Mol. Biol. 54:205-219(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION BY SA.
[8]	"Cytosolic dehydroascorbate reductase is important for ozone tolerance in Arabidopsis thaliana." Yoshida S., Tamaoki M., Shikano T., Nakajima N., Ogawa D., Ioki M., Aono M., Kubo A., Kamada H., Inoue Y., Saji H. Plant Cell Physiol. 47:304-308(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY OZONE, FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY074785 mRNA. Translation: AAL71855.1. AC025814 Genomic DNA. Translation: AAG12679.1. CP002684 Genomic DNA. Translation: AEE35696.1. AY140019 mRNA. Translation: AAM98161.1. BT006257 mRNA. Translation: AAP13365.1. AY087460 mRNA. Translation: AAM65005.1.
IPI	IPI00542474.
PIR	B96783.
RefSeq	NP_177662.1. NM_106182.3.
UniGene	At.27979.
3D structure databases
HSSP	HSSP built from PDB template 1E6B based on UniProtKB Q9ZVQ3.
ProteinModelPortal	Q9FRL8.
SMR	Q9FRL8. Positions 17-205.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9FRL8. 1 interaction.
STRING	3702.AT1G75270.1-P.
Proteomic databases
PaxDb	Q9FRL8.
PRIDE	Q9FRL8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G75270.1; AT1G75270.1; AT1G75270.
GeneID	843864.
KEGG	ath:AT1G75270.
Organism-specific databases
TAIR	At1g75270.
Phylogenomic databases
eggNOG	COG0625.
HOGENOM	HOG000272670.
InParanoid	Q9FRL8.
OMA	LVTPPEY.
PhylomeDB	Q9FRL8.
ProtClustDB	CLSN2914231.
Gene expression databases
Genevestigator	Q9FRL8.
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. IPR012336. Thioredoxin-like_fold. [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

DHAR2_ARATH

Accession

Primary (citable) accession number: Q9FRL8
Secondary accession number(s): Q8LB28

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents