Reviewed, UniProtKB/Swiss-Prot Q9FWR4 (DHAR1_ARATH)

Names and origin

Protein names

Recommended name:
    Glutathione S-transferase DHAR1, mitochondrial
    EC=2.5.1.18
Alternative name(s):
    Glutathione-dependent dehydroascorbate reductase 1
      Short name=GSH-dependent dehydroascorbate reductase 1
      Short name=mtDHAR
      Short name=AtDHAR1

Gene names

Name:	DHAR1
Ordered Locus Names:	At1g19570
ORF Names:	F14P1.9, F18O14.22

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	213 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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, subsequently to biotic or abiotic inducers. Ref.1 Ref.10
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Monomer. Interacts with copper (Cu). Ref.1 Ref.11
Subcellular location	Mitochondrion. Ref.6
Tissue specificity	Expressed at least in roots and leaves. Ref.6
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.10 Ref.6 Ref.7
Post-translational modification	Spontaneous S-glutathionylation in the presence of oxidized glutathione (GSSG).
Disruption phenotype	Plants react normaly to ozone. Ref.9
Sequence similarities	Belongs to the GST superfamily. Omega 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) 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.8 Molecular mass is 25.319 Da from positions 1 - 213. Determined by ESI. S-glutathionylated form. Ref.8
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	Plant defense
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Molecular function	Transferase
PTM	Glutathionylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	defense response Inferred from electronic annotation. Source: UniProtKB-KW regulation of symbiosis, encompassing mutualism through parasitism Inferred from mutant phenotype. Source: TAIR response to jasmonic acid stimulus Ref.10 Inferred from expression pattern. Source: TAIR response to ozone Ref.10 Inferred from expression pattern. Source: TAIR response to symbiotic fungus Inferred from expression pattern. Source: TAIR
Cellular component	apoplast Inferred from direct assay. Source: TAIR chloroplast stroma Inferred from direct assay. Source: TAIR mitochondrion Ref.6 Inferred from direct assay. Source: TAIR peroxisome Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	copper ion binding Ref.11 Inferred from direct assay. Source: TAIR glutathione dehydrogenase (ascorbate) activity Ref.1 Inferred from direct assay. Source: TAIR glutathione transferase activity Inferred from electronic annotation. Source: EC
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 – 65	56	GST N-terminal
	Domain	66 – 213	148	GST C-terminal
	Motif	133 – 137	5	Cu binding Potential
Sites
	Active site	20	1
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. 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: 12077129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF CYS-6 AND CYS-20, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, S-GLUTATHIONYLATION.
[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: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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] (ISOFORM 1).
[6]	"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: 12954611] [Abstract] Cited for: PROTEIN SEQUENCE OF 9-25, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
[7]	"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: 15494554] [Abstract] Cited for: INDUCTION BY INSECTS.
[8]	"Stress-induced protein S-glutathionylation in Arabidopsis." Dixon D.P., Skipsey M., Grundy N.M., Edwards R. Plant Physiol. 138:2233-2244(2005) [PubMed: 16055689] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, S-GLUTATHIONYLATION.
[9]	"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: 16361320] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[10]	"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: 16262714] [Abstract] Cited for: FUNCTION, INDUCTION BY JA.
[11]	"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: 16526091] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH COPPER.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC024609 Genomic DNA. Translation: AAF98403.1. AC025808 Genomic DNA. Translation: AAF79440.1. Sequence problems. 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. NP_173387.1.
UniGene	At.24135 At.24444 At.46960
3D structure databases
HSSP	HSSP built from PDB template 1E6B based on UniProtKB Q9ZVQ3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9FWR4.
Protein family/group databases
TCDB	1.A.12.2.1. intracellular chloride channel (CLIC) family.
Proteomic databases
PRIDE	Q9FWR4.
ProMEX	Q9FWR4.
Genome annotation databases
GeneID	838544.
GenomeReviews	Gene locus AT1G19570 in contig CT485782_GR.
KEGG	ath:AT1G19570.
NMPDR	fig|3702.1.peg.2305.
Organism-specific databases
TAIR	At1g19570.
Phylogenomic databases
OMA	TSAENEG.
Gene expression databases
Genevestigator	Q9FWR4.
Family and domain databases
InterPro	IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:1.20.1050.10. GST_C_like. 1 hit. G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view]
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:	November 3, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)