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Q9FWR4 (DHAR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione S-transferase DHAR1, mitochondrial

EC=2.5.1.18
Alternative name(s):
Chloride intracellular channel homolog 1
Short name=CLIC homolog 1
Glutathione-dependent dehydroascorbate reductase 1
Short name=AtDHAR1
Short name=GSH-dependent dehydroascorbate reductase 1
Short name=mtDHAR
Gene names
Name:DHAR1
Synonyms:DHAR5
Ordered Locus Names:At1g19570
ORF Names:F14P1.9, F18O14.22
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

Displays a dual function. As a soluble protein, 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, subsequently to biotic or abiotic inducers. As a peripheral membrane protein, could also function as voltage-gated ion channel. Ref.1 Ref.9 Ref.13

Catalytic activity

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

Subunit structure

Monomer. Interacts with copper (Cu). Ref.1 Ref.12

Subcellular location

Mitochondrion. Cytoplasmcytosol Potential. Membrane; Peripheral membrane protein Potential. Note: Exists both as soluble protein and as membrane protein. Ref.7

Tissue specificity

Expressed at least in roots and leaves. Ref.7

Induction

Induced by jasmonic acid (JA), oxidative chemical stresses (e.g. norflurazon, menadione, paraquat, and antimycin A), and during photosynthetic operation in the light. Also up-regulated by insects such as Pieris rapae in a JA-dependent manner. Ref.7 Ref.8 Ref.9

Domain

May change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as ion channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion By similarity.

Post-translational modification

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

Disruption phenotype

Plants react normally to ozone. Ref.11

Sequence similarities

Belongs to the GST superfamily. DHAR family.

Contains 1 GST C-terminal domain.

Contains 1 GST N-terminal domain.

Biophysicochemical properties

Kinetic parameters:

KM=0.26 mM for DHA (at pH 6.5 and 30 degrees Celsius) Ref.1

KM=10 mM for GSH (at pH 6.5 and 30 degrees Celsius)

Mass spectrometry

Molecular mass is 24.561 Da from positions 1 - 213. Determined by ESI. Reduced form. Ref.10

Molecular mass is 25.319 Da from positions 1 - 213. Determined by ESI. S-glutathionylated form. Ref.10

Sequence caution

The sequence AAF79440.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene At1g19570 has been split into 2 genes: At1g19565 and At1g19570.

Ontologies

Keywords
   Biological processDetoxification
Ion transport
Plant defense
Stress response
Transport
   Cellular componentCytoplasm
Membrane
Mitochondrion
   Coding sequence diversityAlternative splicing
   Molecular functionIon channel
Transferase
Voltage-gated channel
   PTMGlutathionylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdefense response

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation-reduction process

Inferred from direct assay Ref.1. Source: GOC

protein glutathionylation

Inferred from direct assay Ref.1. Source: TAIR

regulation of symbiosis, encompassing mutualism through parasitism

Inferred from mutant phenotype PubMed 19386380. Source: TAIR

response to jasmonic acid

Inferred from expression pattern Ref.9. Source: TAIR

response to ozone

Inferred from expression pattern Ref.9. Source: TAIR

response to symbiotic fungus

Inferred from expression pattern PubMed 19386380. Source: TAIR

response to toxic substance

Inferred from electronic annotation. Source: UniProtKB-KW

response to zinc ion

Inferred from expression pattern PubMed 19880396. Source: TAIR

   Cellular_componentapoplast

Inferred from direct assay PubMed 18538804. Source: TAIR

chloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

chloroplast stroma

Inferred from direct assay PubMed 16207701. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

mitochondrion

Inferred from direct assay Ref.7. Source: TAIR

peroxisome

Inferred from direct assay PubMed 19329564. Source: TAIR

plasma membrane

Inferred from direct assay PubMed 17644812. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functioncopper ion binding

Inferred from direct assay Ref.12. Source: TAIR

glutathione dehydrogenase (ascorbate) activity

Inferred from direct assay Ref.1. Source: TAIR

glutathione transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

voltage-gated ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9FWR4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9FWR4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     50-50: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Glutathione S-transferase DHAR1, mitochondrial
PRO_0000363142

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
Motif133 – 1375Copper-binding Potential

Sites

Active site201

Amino acid modifications

Modified residue201S-glutathionyl cysteine

Natural variations

Alternative sequence501Missing in isoform 2.
VSP_036254

Experimental info

Mutagenesis61C → S: Reduced activity by 50 percent. Ref.1
Mutagenesis201C → S: No activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 7CB29B43A79C97D5

FASTA21323,641
        10         20         30         40         50         60 
MALEICVKAA VGAPDHLGDC PFSQRALLTL EEKSLTYKIH LINLSDKPQW FLDISPQGKV 

        70         80         90        100        110        120 
PVLKIDDKWV TDSDVIVGIL EEKYPDPPLK TPAEFASVGS NIFGTFGTFL KSKDSNDGSE 

       130        140        150        160        170        180 
HALLVELEAL ENHLKSHDGP FIAGERVSAV DLSLAPKLYH LQVALGHFKS WSVPESFPHV 

       190        200        210 
HNYMKTLFSL DSFEKTKTEE KYVISGWAPK VNP 

« Hide

Isoform 2 [UniParc].

Checksum: 0508DD9167467BBB
Show »

FASTA21223,455

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, MUTAGENESIS OF CYS-6 AND CYS-20, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLUTATHIONYLATION AT CYS-20, GENE FAMILY.
[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]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[5]"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] (ISOFORM 1).
Strain: cv. Columbia.
[6]"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] (ISOFORM 1).
[7]"Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants."
Chew O., Whelan J., Millar A.H.
J. Biol. Chem. 278:46869-46877(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 9-25, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
[8]"A conserved transcript pattern in response to a specialist and a generalist herbivore."
Reymond P., Bodenhausen N., Van Poecke R.M.P., Krishnamurthy V., Dicke M., Farmer E.E.
Plant Cell 16:3132-3147(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY INSECTS.
[9]"Coordinated activation of metabolic pathways for antioxidants and defence compounds by jasmonates and their roles in stress tolerance in Arabidopsis."
Sasaki-Sekimoto Y., Taki N., Obayashi T., Aono M., Matsumoto F., Sakurai N., Suzuki H., Hirai M.Y., Noji M., Saito K., Masuda T., Takamiya K., Shibata D., Ohta H.
Plant J. 44:653-668(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY JA.
[10]"Stress-induced protein S-glutathionylation in Arabidopsis."
Dixon D.P., Skipsey M., Grundy N.M., Edwards R.
Plant Physiol. 138:2233-2244(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, GLUTATHIONYLATION AT CYS-20.
[11]"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: DISRUPTION PHENOTYPE.
[12]"Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry."
Kung C.-C.S., Huang W.-N., Huang Y.-C., Yeh K.-C.
Proteomics 6:2746-2758(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH COPPER.
[13]"A plant homolog of animal chloride intracellular channels (CLICs) generates an ion conductance in heterologous systems."
Elter A., Hartel A., Sieben C., Hertel B., Fischer-Schliebs E., Luttge U., Moroni A., Thiel G.
J. Biol. Chem. 282:8786-8792(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC024609 Genomic DNA. Translation: AAF98403.1.
AC025808 Genomic DNA. Translation: AAF79440.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29868.1.
CP002684 Genomic DNA. Translation: AEE29869.1.
AY039590 mRNA. Translation: AAK62645.1.
AY052211 mRNA. Translation: AAK97681.1.
AY055790 mRNA. Translation: AAL06957.1.
AY085426 mRNA. Translation: AAM62653.1.
AK117865 mRNA. Translation: BAC42506.1.
PIRD86328.
RefSeqNP_001077564.1. NM_001084095.1.
NP_173387.1. NM_101814.4.
UniGeneAt.24135.
At.46960.

3D structure databases

ProteinModelPortalQ9FWR4.
SMRQ9FWR4. Positions 3-203.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid23783. 3 interactions.
IntActQ9FWR4. 2 interactions.
STRING3702.AT1G19570.1-P.

Protein family/group databases

TCDB1.A.12.2.1. the intracellular chloride channel (clic) family.

Proteomic databases

PaxDbQ9FWR4.
PRIDEQ9FWR4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G19570.1; AT1G19570.1; AT1G19570. [Q9FWR4-1]
GeneID838544.
KEGGath:AT1G19570.

Organism-specific databases

TAIRAT1G19570.

Phylogenomic databases

eggNOGKOG1422.
HOGENOMHOG000272670.
InParanoidQ9FWR4.
OMAYVISGWA.
PhylomeDBQ9FWR4.
ProtClustDBPLN02378.

Enzyme and pathway databases

BioCycARA:AT1G19570-MONOMER.
ARA:GQT-400-MONOMER.
SABIO-RKQ9FWR4.

Gene expression databases

GenevestigatorQ9FWR4.

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 nameDHAR1_ARATH
AccessionPrimary (citable) accession number: Q9FWR4
Secondary accession number(s): A8MRM5, Q9LN37
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: March 1, 2001
Last modified: April 16, 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