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Q9FRL8 (DHAR2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. 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 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Cytoplasmcytosol 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Glutathione S-transferase DHAR2
PRO_0000395482

Regions

Domain10 – 8374GST N-terminal
Domain84 – 213130GST C-terminal
Region20 – 212Glutathione binding By similarity
Region46 – 472Glutathione binding By similarity
Region59 – 602Glutathione binding By similarity
Region72 – 732Glutathione binding By similarity
Motif20 – 256Glutathione-binding Potential

Sites

Active site201 By similarity

Amino acid modifications

Modified residue61S-glutathionyl cysteine
Modified residue201S-glutathionyl cysteine

Experimental info

Sequence conflict1951N → K in AAM65005. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9FRL8 [UniParc].

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

FASTA21323,407
        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' 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. 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]"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.

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.
PIRB96783.
RefSeqNP_177662.1. NM_106182.3.
UniGeneAt.27979.

3D structure databases

ProteinModelPortalQ9FRL8.
SMRQ9FRL8. Positions 17-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9FRL8. 1 interaction.
STRING3702.AT1G75270.1-P.

Proteomic databases

PaxDbQ9FRL8.
PRIDEQ9FRL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G75270.1; AT1G75270.1; AT1G75270.
GeneID843864.
KEGGath:AT1G75270.

Organism-specific databases

TAIRAT1G75270.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000272670.
InParanoidQ9FRL8.
OMASKDANDG.
PhylomeDBQ9FRL8.
ProtClustDBCLSN2914231.

Enzyme and pathway databases

BioCycARA:AT1G75270-MONOMER.

Gene expression databases

GenevestigatorQ9FRL8.

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.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF13417. 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 nameDHAR2_ARATH
AccessionPrimary (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: February 19, 2014
This is version 99 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