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Protein

Glutathione S-transferase DHAR2

Gene

DHAR2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei20 – 201By similarity

GO - Molecular functioni

  • glutathione binding Source: TAIR
  • glutathione dehydrogenase (ascorbate) activity Source: TAIR
  • glutathione transferase activity Source: UniProtKB-EC

GO - Biological processi

  • oxidation-reduction process Source: GOC
  • protein glutathionylation Source: TAIR
  • response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Detoxification, Stress response

Enzyme and pathway databases

BioCyciARA:AT1G75270-MONOMER.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DHAR2
Synonyms:DHAR
Ordered Locus Names:At1g75270
ORF Names:F22H5.1
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G75270.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mutant develops distinct foliar lesions under ozone exposure.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Glutathione S-transferase DHAR2PRO_0000395482Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61S-glutathionyl cysteine1 Publication
Modified residuei20 – 201S-glutathionyl cysteine1 Publication

Post-translational modificationi

Spontaneous S-glutathionylation in the presence of oxidized glutathione (GSSG).1 Publication

Keywords - PTMi

Glutathionylation

Proteomic databases

PaxDbiQ9FRL8.
PRIDEiQ9FRL8.

Expressioni

Inductioni

By ozone. By salicylic acid (SA) (at protein level).2 Publications

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ9FRL8. 1 interaction.
STRINGi3702.AT1G75270.1.

Structurei

3D structure databases

ProteinModelPortaliQ9FRL8.
SMRiQ9FRL8. Positions 17-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 8374GST N-terminalAdd
BLAST
Domaini84 – 213130GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 212Glutathione bindingBy similarity
Regioni46 – 472Glutathione bindingBy similarity
Regioni59 – 602Glutathione bindingBy similarity
Regioni72 – 732Glutathione bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 256Glutathione-bindingSequence Analysis

Sequence similaritiesi

Belongs to the GST superfamily. DHAR family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000272670.
InParanoidiQ9FRL8.
OMAiVCLKYRS.
PhylomeDBiQ9FRL8.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FRL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALDICVKVA VGAPDVLGDC PFSQRVLLTL EEKKLPYKTH LINVSDKPQW
60 70 80 90 100
FLDISPEGKV PVVKLDGKWV ADSDVIVGLL EEKYPEPSLK TPPEFASVGS
110 120 130 140 150
KIFGAFVTFL KSKDANDGSE KALVDELEAL ENHLKTHSGP FVAGEKITAV
160 170 180 190 200
DLSLAPKLYH LEVALGHYKN WSVPESLTSV RNYAKALFSR ESFENTKAKK
210
EIVVAGWESK VNA
Length:213
Mass (Da):23,407
Last modified:March 1, 2001 - v1
Checksum:i23543B0F81F96041
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951N → K in AAM65005 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB96783.
RefSeqiNP_177662.1. NM_106182.3.
UniGeneiAt.27979.

Genome annotation databases

EnsemblPlantsiAT1G75270.1; AT1G75270.1; AT1G75270.
GeneIDi843864.
KEGGiath:AT1G75270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiB96783.
RefSeqiNP_177662.1. NM_106182.3.
UniGeneiAt.27979.

3D structure databases

ProteinModelPortaliQ9FRL8.
SMRiQ9FRL8. Positions 17-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9FRL8. 1 interaction.
STRINGi3702.AT1G75270.1.

Proteomic databases

PaxDbiQ9FRL8.
PRIDEiQ9FRL8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G75270.1; AT1G75270.1; AT1G75270.
GeneIDi843864.
KEGGiath:AT1G75270.

Organism-specific databases

TAIRiAT1G75270.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000272670.
InParanoidiQ9FRL8.
OMAiVCLKYRS.
PhylomeDBiQ9FRL8.

Enzyme and pathway databases

BioCyciARA:AT1G75270-MONOMER.

Miscellaneous databases

PROiQ9FRL8.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "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, GLUTATHIONYLATION AT CYS-6 AND CYS-20.
  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.

Entry informationi

Entry nameiDHAR2_ARATH
AccessioniPrimary (citable) accession number: Q9FRL8
Secondary accession number(s): Q8LB28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: March 1, 2001
Last modified: July 22, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.