Q8LE52 (DHAR3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase DHAR3, chloroplastic
EC=2.5.1.18

Alternative name(s):
Chloride intracellular channel homolog 3
Short name=CLIC homolog 3
Glutathione-dependent dehydroascorbate reductase 3
Short name=AtDHAR3
Short name=ChlDHAR
Short name=GSH-dependent dehydroascorbate reductase 3

Gene names

Name:	DHAR3
Ordered Locus Names:	At5g16710
ORF Names:	F5E19.50

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	258 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Catalytic activity	RX + glutathione = HX + R-S-glutathione.
Subunit structure	Monomer By similarity. Interacts with TRX3. Ref.12
Subcellular location	Plastid › chloroplast stroma Ref.10 Ref.11 Ref.13 Ref.14 Ref.15.
Post-translational modification	Partial S-glutathionylation and intramolecular disulfid bond formation between Cys-66 and Cys-69 in the presence of oxidized glutathione (GSSG). Could be reduced by TRX-dependent process.
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=0.50 mM for DHA (at pH 6.5 and 30 degrees Celsius) Ref.9 KM=10 mM for GSH (at pH 6.5 and 30 degrees Celsius)
Sequence caution	The sequence CAC01835.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 2 genes: At5g16710 and At5g16715.

Ontologies

Keywords
Biological process	Detoxification
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Transferase
PTM	Disulfide bond Glutathionylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glutathionylation Inferred from direct assay Ref.9. Source: TAIR response to toxin Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast envelope Inferred from direct assay Ref.10. Source: TAIR chloroplast stroma Inferred from direct assay Ref.13PubMed 18633119PubMed 20061580. Source: TAIR
Molecular_function	glutathione dehydrogenase (ascorbate) activity Inferred from direct assay Ref.9. Source: TAIR glutathione transferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 42	42	Chloroplast Potential
	Chain	43 – 258	216	Glutathione S-transferase DHAR3, chloroplastic		PRO_0000395483
Regions
	Domain	56 – 129	74	GST N-terminal
	Domain	130 – 258	129	GST C-terminal
	Region	66 – 67	2	Glutathione binding By similarity
	Region	92 – 93	2	Glutathione binding By similarity
	Region	105 – 106	2	Glutathione binding By similarity
	Region	118 – 119	2	Glutathione binding By similarity
	Motif	66 – 71	6	Glutathione-binding Potential
Sites
	Active site	66	1	By similarity
Amino acid modifications
	Modified residue	52	1	S-glutathionyl cysteine
	Disulfide bond	66 ↔ 69		In soluble form
Experimental info
	Sequence conflict	65	1	D → Y in AAL38300. Ref.4
	Sequence conflict	65	1	D → Y in AAN65072. Ref.4
	Sequence conflict	231	1	N → D in BAD43518. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8LE52 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 35AC1A8EFDD3E77C	FASTA	258	28,514
	10 20 30 40 50 60 MISLRFQPST TAGVLSASVS RAGFIKRCGS TKPGRVGRFV TMATAASPLE ICVKASITTP 70 80 90 100 110 120 NKLGDCPFCQ KVLLTMEEKN VPYDMKMVDL SNKPEWFLKI SPEGKVPVVK FDEKWVPDSD 130 140 150 160 170 180 VITQALEEKY PEPPLATPPE KASVGSKIFS TFVGFLKSKD SGDGTEQVLL DELTTFNDYI 190 200 210 220 230 240 KDNGPFINGE KISAADLSLA PKLYHMKIAL GHYKNWSVPD SLPFVKSYME NVFSRESFTN 250 TRAETEDVIA GWRPKVMG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]	"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs." Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K. Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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].
[7]	"Purification and characterization of chloroplast dehydroascorbate reductase from spinach leaves." Shimaoka T., Yokota A., Miyake C. Plant Cell Physiol. 41:1110-1118(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-258. Strain: cv. Columbia.
[8]	"Cloning of a chloroplast dehydroascorbate reductase from Arabidopsis thaliana." Creissen G. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-258.
[9]	"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, BIOPHYSICOCHEMICAL PROPERTIES, S-GLUTATHIONYLATION.
[10]	"Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis." Froehlich J.E., Wilkerson C.G., Ray W.K., McAndrew R.S., Osteryoung K.W., Gage D.A., Phinney B.S. J. Proteome Res. 2:413-425(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions." Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S. Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"New targets of Arabidopsis thioredoxins revealed by proteomic analysis." Marchand C., Le Marechal P., Meyer Y., Miginiac-Maslow M., Issakidis-Bourguet E., Decottignies P. Proteomics 4:2696-2706(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TRX3.
[13]	"The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts." Peltier J.-B., Cai Y., Sun Q., Zabrouskov V., Giacomelli L., Rudella A., Ytterberg A.J., Rutschow H., van Wijk K.J. Mol. Cell. Proteomics 5:114-133(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Sorting signals, N-terminal modifications and abundance of the chloroplast proteome." Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J. PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"Enzyme activities and subcellular localization of members of the Arabidopsis glutathione transferase superfamily." Dixon D.P., Hawkins T., Hussey P.J., Edwards R. J. Exp. Bot. 60:1207-1218(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL391147 Genomic DNA. Translation: CAC01835.1. Sequence problems. CP002688 Genomic DNA. Translation: AED92328.1. AK118603 mRNA. Translation: BAC43202.1. AY065124 mRNA. Translation: AAL38300.1. BT001185 mRNA. Translation: AAN65072.1. AK175537 mRNA. Translation: BAD43300.1. AK175755 mRNA. Translation: BAD43518.1. AK175798 mRNA. Translation: BAD43561.1. AK176039 mRNA. Translation: BAD43802.1. AK176071 mRNA. Translation: BAD43834.1. AK176708 mRNA. Translation: BAD44471.1. AK176820 mRNA. Translation: BAD44583.1. AK176870 mRNA. Translation: BAD44633.1. AY085616 mRNA. Translation: AAM62837.1. AF195887 mRNA. Translation: AAG24946.1. AF301597 mRNA. Translation: AAG40196.1.
IPI	IPI00540932.
PIR	T51503.
RefSeq	NP_568336.1. NM_121676.3.
UniGene	At.16881.
3D structure databases
HSSP	HSSP built from PDB template 1OYJ based on UniProtKB O65032.
ProteinModelPortal	Q8LE52.
SMR	Q8LE52. Positions 67-241.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8LE52. 1 interaction.
STRING	3702.AT5G16710.1-P.
Proteomic databases
PaxDb	Q8LE52.
PRIDE	Q8LE52.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G16710.1; AT5G16710.1; AT5G16710.
GeneID	831532.
KEGG	ath:AT5G16710.
Organism-specific databases
TAIR	At5g16710.
Phylogenomic databases
eggNOG	COG0625.
HOGENOM	HOG000272670.
InParanoid	Q8LE52.
OMA	NGDDRDP.
PhylomeDB	Q8LE52.
ProtClustDB	PLN02817.
Gene expression databases
ArrayExpress	Q8LE52.
Genevestigator	Q8LE52.
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

DHAR3_ARATH

Accession

Primary (citable) accession number: Q8LE52
Secondary accession number(s): Q67XJ9 , Q680W2, Q8VZA3, Q9FE30, Q9LFE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 13, 2010
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program