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Protein

Glutathione S-transferase DHAR3, chloroplastic

Gene

DHAR3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Kineticsi

  1. KM=0.50 mM for DHA (at pH 6.5 and 30 degrees Celsius)1 Publication
  2. KM=10 mM for GSH (at pH 6.5 and 30 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661By similarity

GO - Molecular functioni

  1. glutathione dehydrogenase (ascorbate) activity Source: TAIR
  2. glutathione transferase activity Source: UniProtKB-EC

GO - Biological processi

  1. oxidation-reduction process Source: GOC
  2. protein glutathionylation Source: TAIR
  3. response to cytokinin Source: TAIR
  4. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Detoxification

Enzyme and pathway databases

BioCyciARA:AT5G16710-MONOMER.
SABIO-RKQ8LE52.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DHAR3
Ordered Locus Names:At5g16710
ORF Names:F5E19.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G16710.

Subcellular locationi

Plastidchloroplast stroma 5 Publications

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast envelope Source: TAIR
  3. chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4242ChloroplastSequence AnalysisAdd
BLAST
Chaini43 – 258216Glutathione S-transferase DHAR3, chloroplasticPRO_0000395483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521S-glutathionyl cysteine1 Publication
Disulfide bondi66 ↔ 69In soluble form

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Disulfide bond, Glutathionylation

Proteomic databases

PaxDbiQ8LE52.
PRIDEiQ8LE52.

Expressioni

Gene expression databases

GenevestigatoriQ8LE52.

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with TRX3.By similarity1 Publication

Protein-protein interaction databases

IntActiQ8LE52. 1 interaction.
STRINGi3702.AT5G16710.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ8LE52.
SMRiQ8LE52. Positions 64-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 12974GST N-terminalAdd
BLAST
Domaini130 – 258129GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 672Glutathione bindingBy similarity
Regioni92 – 932Glutathione bindingBy similarity
Regioni105 – 1062Glutathione bindingBy similarity
Regioni118 – 1192Glutathione bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi66 – 716Glutathione-bindingSequence Analysis

Sequence similaritiesi

Belongs to the GST superfamily. DHAR family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000272670.
InParanoidiQ8LE52.
OMAiHLPYDMK.
PhylomeDBiQ8LE52.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8LE52-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISLRFQPST TAGVLSASVS RAGFIKRCGS TKPGRVGRFV TMATAASPLE
60 70 80 90 100
ICVKASITTP NKLGDCPFCQ KVLLTMEEKN VPYDMKMVDL SNKPEWFLKI
110 120 130 140 150
SPEGKVPVVK FDEKWVPDSD VITQALEEKY PEPPLATPPE KASVGSKIFS
160 170 180 190 200
TFVGFLKSKD SGDGTEQVLL DELTTFNDYI KDNGPFINGE KISAADLSLA
210 220 230 240 250
PKLYHMKIAL GHYKNWSVPD SLPFVKSYME NVFSRESFTN TRAETEDVIA

GWRPKVMG
Length:258
Mass (Da):28,514
Last modified:October 1, 2002 - v1
Checksum:i35AC1A8EFDD3E77C
GO

Sequence cautioni

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.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651D → Y in AAL38300 (PubMed:14593172).Curated
Sequence conflicti65 – 651D → Y in AAN65072 (PubMed:14593172).Curated
Sequence conflicti231 – 2311N → D in BAD43518 (Ref. 5) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT51503.
RefSeqiNP_568336.1. NM_121676.3.
UniGeneiAt.16881.

Genome annotation databases

EnsemblPlantsiAT5G16710.1; AT5G16710.1; AT5G16710.
GeneIDi831532.
KEGGiath:AT5G16710.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiT51503.
RefSeqiNP_568336.1. NM_121676.3.
UniGeneiAt.16881.

3D structure databases

ProteinModelPortaliQ8LE52.
SMRiQ8LE52. Positions 64-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8LE52. 1 interaction.
STRINGi3702.AT5G16710.1-P.

Proteomic databases

PaxDbiQ8LE52.
PRIDEiQ8LE52.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G16710.1; AT5G16710.1; AT5G16710.
GeneIDi831532.
KEGGiath:AT5G16710.

Organism-specific databases

TAIRiAT5G16710.

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000272670.
InParanoidiQ8LE52.
OMAiHLPYDMK.
PhylomeDBiQ8LE52.

Enzyme and pathway databases

BioCyciARA:AT5G16710-MONOMER.
SABIO-RKQ8LE52.

Gene expression databases

GenevestigatoriQ8LE52.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH TRX3.
  13. 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.

Entry informationi

Entry nameiDHAR3_ARATH
AccessioniPrimary (citable) accession number: Q8LE52
Secondary accession number(s): Q67XJ9
, Q680W2, Q8VZA3, Q9FE30, Q9LFE6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: October 1, 2002
Last modified: January 7, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.