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Q8LE52 (DHAR3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Catalytic activity

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

Subunit structure

Monomer By similarity. Interacts with TRX3. Ref.12

Subcellular location

Plastidchloroplast 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Chloroplast Potential
Chain43 – 258216Glutathione S-transferase DHAR3, chloroplastic
PRO_0000395483

Regions

Domain56 – 12974GST N-terminal
Domain130 – 258129GST C-terminal
Region66 – 672Glutathione binding By similarity
Region92 – 932Glutathione binding By similarity
Region105 – 1062Glutathione binding By similarity
Region118 – 1192Glutathione binding By similarity
Motif66 – 716Glutathione-binding Potential

Sites

Active site661 By similarity

Amino acid modifications

Modified residue521S-glutathionyl cysteine
Disulfide bond66 ↔ 69In soluble form

Experimental info

Sequence conflict651D → Y in AAL38300. Ref.4
Sequence conflict651D → Y in AAN65072. Ref.4
Sequence conflict2311N → D in BAD43518. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q8LE52 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 35AC1A8EFDD3E77C

FASTA25828,514
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. 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]"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. expand/collapse author list , 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, GLUTATHIONYLATION AT CYS-52.
[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.
[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.
[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.
[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.
[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.
PIRT51503.
RefSeqNP_568336.1. NM_121676.3.
UniGeneAt.16881.

3D structure databases

ProteinModelPortalQ8LE52.
SMRQ8LE52. Positions 64-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8LE52. 1 interaction.
STRING3702.AT5G16710.1-P.

Proteomic databases

PaxDbQ8LE52.
PRIDEQ8LE52.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G16710.1; AT5G16710.1; AT5G16710.
GeneID831532.
KEGGath:AT5G16710.

Organism-specific databases

TAIRAT5G16710.

Phylogenomic databases

eggNOGCOG0625.
HOGENOMHOG000272670.
InParanoidQ8LE52.
OMAPKLHVIR.
PhylomeDBQ8LE52.

Enzyme and pathway databases

BioCycARA:AT5G16710-MONOMER.
SABIO-RKQ8LE52.

Gene expression databases

GenevestigatorQ8LE52.

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 nameDHAR3_ARATH
AccessionPrimary (citable) accession number: Q8LE52
Secondary accession number(s): Q67XJ9 expand/collapse secondary AC list , Q680W2, Q8VZA3, Q9FE30, Q9LFE6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: October 1, 2002
Last modified: June 11, 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