Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9FRL8

- DHAR2_ARATH

UniProt

Q9FRL8 - DHAR2_ARATH

Protein

Glutathione S-transferase DHAR2

Gene

DHAR2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Plays a role in ozone tolerance.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei20 – 201By similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Detoxification, Stress response

    Enzyme and pathway databases

    BioCyciARA:AT1G75270-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase DHAR2 (EC:2.5.1.18)
    Alternative name(s):
    Chloride intracellular channel homolog 2
    Short name:
    CLIC homolog 2
    Glutathione-dependent dehydroascorbate reductase 2
    Short name:
    AtDHAR2
    Short name:
    CytDHAR
    Short name:
    GSH-dependent dehydroascorbate reductase 2
    Gene namesi
    Name:DHAR2
    Synonyms:DHAR
    Ordered Locus Names:At1g75270
    ORF Names:F22H5.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G75270.

    Subcellular locationi

    Cytoplasmcytosol Curated

    GO - Cellular componenti

    1. cytosol Source: TAIR
    2. plasma membrane Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mutant develops distinct foliar lesions under ozone exposure.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 213213Glutathione S-transferase DHAR2PRO_0000395482Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61S-glutathionyl cysteine1 Publication
    Modified residuei20 – 201S-glutathionyl cysteine1 Publication

    Post-translational modificationi

    Spontaneous S-glutathionylation in the presence of oxidized glutathione (GSSG).1 Publication

    Keywords - PTMi

    Glutathionylation

    Proteomic databases

    PaxDbiQ9FRL8.
    PRIDEiQ9FRL8.

    Expressioni

    Inductioni

    By ozone. By salicylic acid (SA) (at protein level).2 Publications

    Gene expression databases

    GenevestigatoriQ9FRL8.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    IntActiQ9FRL8. 1 interaction.
    STRINGi3702.AT1G75270.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FRL8.
    SMRiQ9FRL8. Positions 17-205.
    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

    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

    eggNOGiCOG0625.
    HOGENOMiHOG000272670.
    InParanoidiQ9FRL8.
    OMAiKDANDGS.
    PhylomeDBiQ9FRL8.

    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.

    Q9FRL8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALDICVKVA VGAPDVLGDC PFSQRVLLTL EEKKLPYKTH LINVSDKPQW    50
    FLDISPEGKV PVVKLDGKWV ADSDVIVGLL EEKYPEPSLK TPPEFASVGS 100
    KIFGAFVTFL KSKDANDGSE KALVDELEAL ENHLKTHSGP FVAGEKITAV 150
    DLSLAPKLYH LEVALGHYKN WSVPESLTSV RNYAKALFSR ESFENTKAKK 200
    EIVVAGWESK VNA 213
    Length:213
    Mass (Da):23,407
    Last modified:March 1, 2001 - v1
    Checksum:i23543B0F81F96041
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti195 – 1951N → K in AAM65005. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY074785 mRNA. Translation: AAL71855.1.
    AC025814 Genomic DNA. Translation: AAG12679.1.
    CP002684 Genomic DNA. Translation: AEE35696.1.
    AY140019 mRNA. Translation: AAM98161.1.
    BT006257 mRNA. Translation: AAP13365.1.
    AY087460 mRNA. Translation: AAM65005.1.
    PIRiB96783.
    RefSeqiNP_177662.1. NM_106182.3.
    UniGeneiAt.27979.

    Genome annotation databases

    EnsemblPlantsiAT1G75270.1; AT1G75270.1; AT1G75270.
    GeneIDi843864.
    KEGGiath:AT1G75270.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY074785 mRNA. Translation: AAL71855.1 .
    AC025814 Genomic DNA. Translation: AAG12679.1 .
    CP002684 Genomic DNA. Translation: AEE35696.1 .
    AY140019 mRNA. Translation: AAM98161.1 .
    BT006257 mRNA. Translation: AAP13365.1 .
    AY087460 mRNA. Translation: AAM65005.1 .
    PIRi B96783.
    RefSeqi NP_177662.1. NM_106182.3.
    UniGenei At.27979.

    3D structure databases

    ProteinModelPortali Q9FRL8.
    SMRi Q9FRL8. Positions 17-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9FRL8. 1 interaction.
    STRINGi 3702.AT1G75270.1-P.

    Proteomic databases

    PaxDbi Q9FRL8.
    PRIDEi Q9FRL8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G75270.1 ; AT1G75270.1 ; AT1G75270 .
    GeneIDi 843864.
    KEGGi ath:AT1G75270.

    Organism-specific databases

    TAIRi AT1G75270.

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000272670.
    InParanoidi Q9FRL8.
    OMAi KDANDGS.
    PhylomeDBi Q9FRL8.

    Enzyme and pathway databases

    BioCyci ARA:AT1G75270-MONOMER.

    Gene expression databases

    Genevestigatori Q9FRL8.

    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. "Increasing vitamin C content of plants through enhanced ascorbate recycling."
      Chen Z., Young T.E., Ling J., Chang S.C., Gallie D.R.
      Proc. Natl. Acad. Sci. U.S.A. 100:3525-3530(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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. "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. "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].
    6. "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, GLUTATHIONYLATION AT CYS-6 AND CYS-20.
    7. "Proteomic analysis of glutathione S -transferases of Arabidopsis thaliana reveals differential salicylic acid-induced expression of the plant-specific phi and tau classes."
      Sappl P.G., Onate-Sanchez L., Singh K.B., Millar A.H.
      Plant Mol. Biol. 54:205-219(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION BY SA.
    8. "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: INDUCTION BY OZONE, FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiDHAR2_ARATH
    AccessioniPrimary (citable) accession number: Q9FRL8
    Secondary accession number(s): Q8LB28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 13, 2010
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    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