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Q8LE52

- DHAR3_ARATH

UniProt

Q8LE52 - DHAR3_ARATH

Protein

Glutathione S-transferase DHAR3, chloroplastic

Gene

DHAR3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    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 toxic substance Source: UniProtKB-KW

    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

    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.
    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.

    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. 1 PublicationCurated

    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

    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: October 1, 2014
    This is version 100 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