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Q8LE52

- DHAR3_ARATH

UniProt

Q8LE52 - DHAR3_ARATH

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Protein
Glutathione S-transferase DHAR3, chloroplastic
Gene
DHAR3, At5g16710, F5E19.50
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei66 – 661 By 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 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 – 4242Chloroplast Reviewed prediction
Add
BLAST
Chaini43 – 258216Glutathione S-transferase DHAR3, chloroplastic
PRO_0000395483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521S-glutathionyl cysteine
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.

Keywords - PTMi

Disulfide bond, Glutathionylation

Proteomic databases

PaxDbiQ8LE52.
PRIDEiQ8LE52.

Expressioni

Gene expression databases

GenevestigatoriQ8LE52.

Interactioni

Subunit structurei

Monomer By similarity. Interacts with TRX3.1 Publication

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ8LE52.
SMRiQ8LE52. Positions 64-241.

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi66 – 716Glutathione-binding Reviewed prediction

Sequence similaritiesi

Belongs to the GST superfamily. DHAR family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0625.
HOGENOMiHOG000272670.
InParanoidiQ8LE52.
OMAiPKLHVIR.
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

MISLRFQPST TAGVLSASVS RAGFIKRCGS TKPGRVGRFV TMATAASPLE    50
ICVKASITTP NKLGDCPFCQ KVLLTMEEKN VPYDMKMVDL SNKPEWFLKI 100
SPEGKVPVVK FDEKWVPDSD VITQALEEKY PEPPLATPPE KASVGSKIFS 150
TFVGFLKSKD SGDGTEQVLL DELTTFNDYI KDNGPFINGE KISAADLSLA 200
PKLYHMKIAL GHYKNWSVPD SLPFVKSYME NVFSRESFTN TRAETEDVIA 250
GWRPKVMG 258
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651D → Y in AAL38300. 1 Publication
Sequence conflicti65 – 651D → Y in AAN65072. 1 Publication
Sequence conflicti231 – 2311N → D in BAD43518. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi T51503.
RefSeqi NP_568336.1. NM_121676.3.
UniGenei At.16881.

3D structure databases

ProteinModelPortali Q8LE52.
SMRi Q8LE52. Positions 64-241.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8LE52. 1 interaction.
STRINGi 3702.AT5G16710.1-P.

Proteomic databases

PaxDbi Q8LE52.
PRIDEi Q8LE52.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G16710.1 ; AT5G16710.1 ; AT5G16710 .
GeneIDi 831532.
KEGGi ath:AT5G16710.

Organism-specific databases

TAIRi AT5G16710.

Phylogenomic databases

eggNOGi COG0625.
HOGENOMi HOG000272670.
InParanoidi Q8LE52.
OMAi PKLHVIR.
PhylomeDBi Q8LE52.

Enzyme and pathway databases

BioCyci ARA:AT5G16710-MONOMER.
SABIO-RK Q8LE52.

Gene expression databases

Genevestigatori Q8LE52.

Family and domain databases

Gene3Di 1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF13417. GST_N_3. 1 hit.
[Graphical view ]
SUPFAMi SSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 99 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

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