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Protein

Glutathione S-transferase DHAR1, mitochondrial

Gene

DHAR1

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

Functioni

Displays a dual function. As a soluble protein, 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, subsequently to biotic or abiotic inducers. As a peripheral membrane protein, could also function as voltage-gated ion channel.3 Publications

Catalytic activityi

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

Kineticsi

  1. KM=0.26 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 sitei20 – 201

    GO - Molecular functioni

    • copper ion binding Source: TAIR
    • glutathione dehydrogenase (ascorbate) activity Source: TAIR
    • glutathione transferase activity Source: UniProtKB-EC
    • voltage-gated ion channel activity Source: UniProtKB-KW

    GO - Biological processi

    • defense response Source: UniProtKB-KW
    • oxidation-reduction process Source: GOC
    • protein glutathionylation Source: TAIR
    • regulation of symbiosis, encompassing mutualism through parasitism Source: TAIR
    • response to jasmonic acid Source: TAIR
    • response to ozone Source: TAIR
    • response to symbiotic fungus Source: TAIR
    • response to toxic substance Source: UniProtKB-KW
    • response to zinc ion Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Ion channel, Transferase, Voltage-gated channel

    Keywords - Biological processi

    Detoxification, Ion transport, Plant defense, Stress response, Transport

    Enzyme and pathway databases

    BioCyciARA:AT1G19570-MONOMER.
    ARA:GQT-400-MONOMER.
    SABIO-RKQ9FWR4.

    Protein family/group databases

    TCDBi1.A.12.2.1. the intracellular chloride channel (clic) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase DHAR1, mitochondrial (EC:2.5.1.18)
    Alternative name(s):
    Chloride intracellular channel homolog 1
    Short name:
    CLIC homolog 1
    Glutathione-dependent dehydroascorbate reductase 1
    Short name:
    AtDHAR1
    Short name:
    GSH-dependent dehydroascorbate reductase 1
    Short name:
    mtDHAR
    Gene namesi
    Name:DHAR1
    Synonyms:DHAR5
    Ordered Locus Names:At1g19570
    ORF Names:F14P1.9, F18O14.22
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G19570.

    Subcellular locationi

    GO - Cellular componenti

    • apoplast Source: TAIR
    • chloroplast Source: TAIR
    • chloroplast stroma Source: TAIR
    • cytosol Source: TAIR
    • mitochondrion Source: TAIR
    • peroxisome Source: TAIR
    • plasma membrane Source: TAIR
    • vacuole Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion

    Pathology & Biotechi

    Disruption phenotypei

    Plants react normally to ozone.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi6 – 61C → S: Reduced activity by 50 percent. 1 Publication
    Mutagenesisi20 – 201C → S: No activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 213213Glutathione S-transferase DHAR1, mitochondrialPRO_0000363142Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201S-glutathionyl cysteine2 Publications

    Post-translational modificationi

    Spontaneous S-glutathionylation in the presence of oxidized glutathione (GSSG).2 Publications

    Keywords - PTMi

    Glutathionylation

    Proteomic databases

    PaxDbiQ9FWR4.
    PRIDEiQ9FWR4.

    Expressioni

    Tissue specificityi

    Expressed at least in roots and leaves.1 Publication

    Inductioni

    Induced by jasmonic acid (JA), oxidative chemical stresses (e.g. norflurazon, menadione, paraquat, and antimycin A), and during photosynthetic operation in the light. Also up-regulated by insects such as Pieris rapae in a JA-dependent manner.3 Publications

    Interactioni

    Subunit structurei

    Monomer. Interacts with copper (Cu).2 Publications

    Protein-protein interaction databases

    BioGridi23783. 3 interactions.
    IntActiQ9FWR4. 2 interactions.
    STRINGi3702.AT1G19570.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FWR4.
    SMRiQ9FWR4. Positions 16-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 8374GST N-terminalAdd
    BLAST
    Domaini84 – 213130GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni20 – 212Glutathione bindingBy similarity
    Regioni46 – 472Glutathione bindingBy similarity
    Regioni59 – 602Glutathione bindingBy similarity
    Regioni72 – 732Glutathione bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi20 – 256Glutathione-bindingSequence Analysis
    Motifi133 – 1375Copper-bindingSequence Analysis

    Domaini

    May change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as ion channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion (By similarity).By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiKOG1422.
    HOGENOMiHOG000272670.
    OMAiANGDDRD.
    PhylomeDBiQ9FWR4.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9FWR4-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MALEICVKAA VGAPDHLGDC PFSQRALLTL EEKSLTYKIH LINLSDKPQW
    60 70 80 90 100
    FLDISPQGKV PVLKIDDKWV TDSDVIVGIL EEKYPDPPLK TPAEFASVGS
    110 120 130 140 150
    NIFGTFGTFL KSKDSNDGSE HALLVELEAL ENHLKSHDGP FIAGERVSAV
    160 170 180 190 200
    DLSLAPKLYH LQVALGHFKS WSVPESFPHV HNYMKTLFSL DSFEKTKTEE
    210
    KYVISGWAPK VNP
    Length:213
    Mass (Da):23,641
    Last modified:March 1, 2001 - v1
    Checksum:i7CB29B43A79C97D5
    GO
    Isoform 2 (identifier: Q9FWR4-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         50-50: Missing.

    Note: Derived from EST data. No experimental confirmation available.
    Show »
    Length:212
    Mass (Da):23,455
    Checksum:i0508DD9167467BBB
    GO

    Sequence cautioni

    The sequence AAF79440.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene At1g19570 has been split into 2 genes: At1g19565 and At1g19570.Curated

    Mass spectrometryi

    Molecular mass is 24.561 Da from positions 1 - 213. Determined by ESI. Reduced form.1 Publication
    Molecular mass is 25.319 Da from positions 1 - 213. Determined by ESI. S-glutathionylated form.1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei50 – 501Missing in isoform 2. CuratedVSP_036254

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC024609 Genomic DNA. Translation: AAF98403.1.
    AC025808 Genomic DNA. Translation: AAF79440.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE29868.1.
    CP002684 Genomic DNA. Translation: AEE29869.1.
    AY039590 mRNA. Translation: AAK62645.1.
    AY052211 mRNA. Translation: AAK97681.1.
    AY055790 mRNA. Translation: AAL06957.1.
    AY085426 mRNA. Translation: AAM62653.1.
    AK117865 mRNA. Translation: BAC42506.1.
    PIRiD86328.
    RefSeqiNP_001077564.1. NM_001084095.1. [Q9FWR4-2]
    NP_173387.1. NM_101814.4. [Q9FWR4-1]
    UniGeneiAt.24135.
    At.46960.

    Genome annotation databases

    EnsemblPlantsiAT1G19570.1; AT1G19570.1; AT1G19570. [Q9FWR4-1]
    GeneIDi838544.
    KEGGiath:AT1G19570.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AC024609 Genomic DNA. Translation: AAF98403.1.
    AC025808 Genomic DNA. Translation: AAF79440.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE29868.1.
    CP002684 Genomic DNA. Translation: AEE29869.1.
    AY039590 mRNA. Translation: AAK62645.1.
    AY052211 mRNA. Translation: AAK97681.1.
    AY055790 mRNA. Translation: AAL06957.1.
    AY085426 mRNA. Translation: AAM62653.1.
    AK117865 mRNA. Translation: BAC42506.1.
    PIRiD86328.
    RefSeqiNP_001077564.1. NM_001084095.1. [Q9FWR4-2]
    NP_173387.1. NM_101814.4. [Q9FWR4-1]
    UniGeneiAt.24135.
    At.46960.

    3D structure databases

    ProteinModelPortaliQ9FWR4.
    SMRiQ9FWR4. Positions 16-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi23783. 3 interactions.
    IntActiQ9FWR4. 2 interactions.
    STRINGi3702.AT1G19570.1.

    Protein family/group databases

    TCDBi1.A.12.2.1. the intracellular chloride channel (clic) family.

    Proteomic databases

    PaxDbiQ9FWR4.
    PRIDEiQ9FWR4.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G19570.1; AT1G19570.1; AT1G19570. [Q9FWR4-1]
    GeneIDi838544.
    KEGGiath:AT1G19570.

    Organism-specific databases

    TAIRiAT1G19570.

    Phylogenomic databases

    eggNOGiKOG1422.
    HOGENOMiHOG000272670.
    OMAiANGDDRD.
    PhylomeDBiQ9FWR4.

    Enzyme and pathway databases

    BioCyciARA:AT1G19570-MONOMER.
    ARA:GQT-400-MONOMER.
    SABIO-RKQ9FWR4.

    Miscellaneous databases

    PROiQ9FWR4.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, MUTAGENESIS OF CYS-6 AND CYS-20, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, GLUTATHIONYLATION AT CYS-20, GENE FAMILY.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    5. "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] (ISOFORM 1).
      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] (ISOFORM 1).
    7. "Molecular definition of the ascorbate-glutathione cycle in Arabidopsis mitochondria reveals dual targeting of antioxidant defenses in plants."
      Chew O., Whelan J., Millar A.H.
      J. Biol. Chem. 278:46869-46877(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 9-25, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
    8. "A conserved transcript pattern in response to a specialist and a generalist herbivore."
      Reymond P., Bodenhausen N., Van Poecke R.M.P., Krishnamurthy V., Dicke M., Farmer E.E.
      Plant Cell 16:3132-3147(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY INSECTS.
    9. "Coordinated activation of metabolic pathways for antioxidants and defence compounds by jasmonates and their roles in stress tolerance in Arabidopsis."
      Sasaki-Sekimoto Y., Taki N., Obayashi T., Aono M., Matsumoto F., Sakurai N., Suzuki H., Hirai M.Y., Noji M., Saito K., Masuda T., Takamiya K., Shibata D., Ohta H.
      Plant J. 44:653-668(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION BY JA.
    10. "Stress-induced protein S-glutathionylation in Arabidopsis."
      Dixon D.P., Skipsey M., Grundy N.M., Edwards R.
      Plant Physiol. 138:2233-2244(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, GLUTATHIONYLATION AT CYS-20.
    11. "Cytosolic dehydroascorbate reductase is important for ozone tolerance in Arabidopsis thaliana."
      Yoshida S., Tamaoki M., Shikano T., Nakajima N., Ogawa D., Ioki M., Aono M., Kubo A., Kamada H., Inoue Y., Saji H.
      Plant Cell Physiol. 47:304-308(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    12. "Proteomic survey of copper-binding proteins in Arabidopsis roots by immobilized metal affinity chromatography and mass spectrometry."
      Kung C.-C.S., Huang W.-N., Huang Y.-C., Yeh K.-C.
      Proteomics 6:2746-2758(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH COPPER.
    13. "A plant homolog of animal chloride intracellular channels (CLICs) generates an ion conductance in heterologous systems."
      Elter A., Hartel A., Sieben C., Hertel B., Fischer-Schliebs E., Luttge U., Moroni A., Thiel G.
      J. Biol. Chem. 282:8786-8792(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiDHAR1_ARATH
    AccessioniPrimary (citable) accession number: Q9FWR4
    Secondary accession number(s): A8MRM5, Q9LN37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 10, 2009
    Last sequence update: March 1, 2001
    Last modified: July 22, 2015
    This is version 106 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, Direct protein sequencing, 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.