Q9FWR4 (DHAR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	213 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytosol 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 process	Detoxification Ion transport Plant defense Stress response Transport
Cellular component	Cytoplasm Membrane Mitochondrion
Coding sequence diversity	Alternative splicing
Molecular function	Ion channel Transferase Voltage-gated channel
PTM	Glutathionylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	defense response Inferred from electronic annotation. Source: UniProtKB-KW 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 stimulus 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 toxin Inferred from electronic annotation. Source: UniProtKB-KW response to zinc ion Inferred from expression pattern PubMed 19880396. Source: TAIR
Cellular_component	apoplast Inferred from direct assay PubMed 18538804. 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_function	copper 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: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 213	213	Glutathione S-transferase DHAR1, mitochondrial		PRO_0000363142
Regions
	Domain	10 – 83	74	GST N-terminal
	Domain	84 – 213	130	GST C-terminal
	Region	20 – 21	2	Glutathione binding By similarity
	Region	46 – 47	2	Glutathione binding By similarity
	Region	59 – 60	2	Glutathione binding By similarity
	Region	72 – 73	2	Glutathione binding By similarity
	Motif	20 – 25	6	Glutathione-binding Potential
	Motif	133 – 137	5	Copper-binding Potential
Sites
	Active site	20	1
Amino acid modifications
	Modified residue	20	1	S-glutathionyl cysteine
Natural variations
	Alternative sequence	50	1	Missing in isoform 2.		VSP_036254
Experimental info
	Mutagenesis	6	1	C → S: Reduced activity by 50 percent. Ref.1
	Mutagenesis	20	1	C → S: No activity. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 7CB29B43A79C97D5	FASTA	213	23,641
	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
	Isoform 2 [UniParc]. Checksum: 0508DD9167467BBB	FASTA	212	23,455
	10 20 30 40 50 60 MALEICVKAA VGAPDHLGDC PFSQRALLTL EEKSLTYKIH LINLSDKPQF LDISPQGKVP 70 80 90 100 110 120 VLKIDDKWVT DSDVIVGILE EKYPDPPLKT PAEFASVGSN IFGTFGTFLK SKDSNDGSEH 130 140 150 160 170 180 ALLVELEALE NHLKSHDGPF IAGERVSAVD LSLAPKLYHL QVALGHFKSW SVPESFPHVH 190 200 210 NYMKTLFSLD SFEKTKTEEK YVISGWAPKV NP

References

	« Hide 'large scale' referencesShow '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, S-GLUTATHIONYLATION, 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. , 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. , 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, S-GLUTATHIONYLATION.
[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.
IPI	IPI00530621. IPI00846186.
PIR	D86328.
RefSeq	NP_001077564.1. NM_001084095.1. NP_173387.1. NM_101814.4.
UniGene	At.24135. At.46960.
3D structure databases
HSSP	HSSP built from PDB template 1E6B based on UniProtKB Q9ZVQ3.
ProteinModelPortal	Q9FWR4.
SMR	Q9FWR4. Positions 3-203.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9FWR4. 2 interactions.
STRING	3702.AT1G19570.1-P.
Protein family/group databases
TCDB	1.A.12.2.1. intracellular chloride channel (CLIC) family.
Proteomic databases
PaxDb	Q9FWR4.
PRIDE	Q9FWR4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G19570.1; AT1G19570.1; AT1G19570.
GeneID	838544.
KEGG	ath:AT1G19570.
Organism-specific databases
TAIR	At1g19570.
Phylogenomic databases
eggNOG	KOG1422.
HOGENOM	HOG000272670.
InParanoid	Q9FWR4.
OMA	YVISGWA.
PhylomeDB	Q9FWR4.
ProtClustDB	PLN02378.
Gene expression databases
Genevestigator	Q9FWR4.
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

DHAR1_ARATH

Accession

Primary (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:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program