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Q9FWR4

- DHAR1_ARATH

UniProt

Q9FWR4 - DHAR1_ARATH

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Protein

Glutathione S-transferase DHAR1, mitochondrial

Gene

DHAR1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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

  1. copper ion binding Source: TAIR
  2. glutathione dehydrogenase (ascorbate) activity Source: TAIR
  3. glutathione transferase activity Source: UniProtKB-EC
  4. voltage-gated ion channel activity Source: UniProtKB-KW

GO - Biological processi

  1. defense response Source: UniProtKB-KW
  2. oxidation-reduction process Source: GOC
  3. protein glutathionylation Source: TAIR
  4. regulation of symbiosis, encompassing mutualism through parasitism Source: TAIR
  5. response to jasmonic acid Source: TAIR
  6. response to ozone Source: TAIR
  7. response to symbiotic fungus Source: TAIR
  8. response to toxic substance Source: UniProtKB-KW
  9. 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: Chromosome 1

Organism-specific databases

TAIRiAT1G19570.

Subcellular locationi

Mitochondrion 1 Publication. Cytoplasmcytosol Curated. Membrane Curated; Peripheral membrane protein Curated
Note: Exists both as soluble protein and as membrane protein.

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. chloroplast stroma Source: TAIR
  4. cytosol Source: TAIR
  5. mitochondrion Source: TAIR
  6. peroxisome Source: TAIR
  7. plasma membrane Source: TAIR
  8. 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

Gene expression databases

GenevestigatoriQ9FWR4.

Interactioni

Subunit structurei

Monomer. Interacts with copper (Cu).2 Publications

Protein-protein interaction databases

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

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.
OMAiGNAYERD.
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. Align

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.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi D86328.
RefSeqi NP_001077564.1. NM_001084095.1. [Q9FWR4-2 ]
NP_173387.1. NM_101814.4. [Q9FWR4-1 ]
UniGenei At.24135.
At.46960.

3D structure databases

ProteinModelPortali Q9FWR4.
SMRi Q9FWR4. Positions 16-199.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 23783. 3 interactions.
IntActi Q9FWR4. 2 interactions.
STRINGi 3702.AT1G19570.1-P.

Protein family/group databases

TCDBi 1.A.12.2.1. the intracellular chloride channel (clic) family.

Proteomic databases

PaxDbi Q9FWR4.
PRIDEi Q9FWR4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G19570.1 ; AT1G19570.1 ; AT1G19570 . [Q9FWR4-1 ]
GeneIDi 838544.
KEGGi ath:AT1G19570.

Organism-specific databases

TAIRi AT1G19570.

Phylogenomic databases

eggNOGi KOG1422.
HOGENOMi HOG000272670.
OMAi GNAYERD.
PhylomeDBi Q9FWR4.

Enzyme and pathway databases

BioCyci ARA:AT1G19570-MONOMER.
ARA:GQT-400-MONOMER.
SABIO-RK Q9FWR4.

Gene expression databases

Genevestigatori Q9FWR4.

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. "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: October 29, 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, 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