DHAR2_ARATH
ID DHAR2_ARATH Reviewed; 213 AA.
AC Q9FRL8; Q8LB28;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glutathione S-transferase DHAR2;
DE EC=2.5.1.18 {ECO:0000269|PubMed:12077129};
DE AltName: Full=Chloride intracellular channel homolog 2;
DE Short=CLIC homolog 2;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase 2 {ECO:0000303|PubMed:12077129};
DE Short=AtDHAR2 {ECO:0000303|PubMed:12077129};
DE Short=CytDHAR;
DE Short=GSH-dependent dehydroascorbate reductase 2;
DE EC=1.8.5.1 {ECO:0000269|PubMed:12077129};
GN Name=DHAR2; Synonyms=DHAR; OrderedLocusNames=At1g75270; ORFNames=F22H5.1;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12624189; DOI=10.1073/pnas.0635176100;
RA Chen Z., Young T.E., Ling J., Chang S.C., Gallie D.R.;
RT "Increasing vitamin C content of plants through enhanced ascorbate
RT recycling.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3525-3530(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND
RP GLUTATHIONYLATION AT CYS-6 AND CYS-20.
RX PubMed=12077129; DOI=10.1074/jbc.m202919200;
RA Dixon D.P., Davis B.G., Edwards R.;
RT "Functional divergence in the glutathione transferase superfamily in
RT plants. Identification of two classes with putative functions in redox
RT homeostasis in Arabidopsis thaliana.";
RL J. Biol. Chem. 277:30859-30869(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION BY SA.
RX PubMed=15159623; DOI=10.1023/b:plan.0000028786.57439.b3;
RA Sappl P.G., Onate-Sanchez L., Singh K.B., Millar A.H.;
RT "Proteomic analysis of glutathione S -transferases of Arabidopsis thaliana
RT reveals differential salicylic acid-induced expression of the plant-
RT specific phi and tau classes.";
RL Plant Mol. Biol. 54:205-219(2004).
RN [8]
RP FUNCTION, INDUCTION BY OZONE, AND DISRUPTION PHENOTYPE.
RX PubMed=16361320; DOI=10.1093/pcp/pci246;
RA Yoshida S., Tamaoki M., Shikano T., Nakajima N., Ogawa D., Ioki M.,
RA Aono M., Kubo A., Kamada H., Inoue Y., Saji H.;
RT "Cytosolic dehydroascorbate reductase is important for ozone tolerance in
RT Arabidopsis thaliana.";
RL Plant Cell Physiol. 47:304-308(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX PubMed=28195196; DOI=10.1038/srep42494;
RA Bodra N., Young D., Astolfi Rosado L., Pallo A., Wahni K., De Proft F.,
RA Huang J., Van Breusegem F., Messens J.;
RT "Arabidopsis thaliana dehydroascorbate reductase 2: Conformational
RT flexibility during catalysis.";
RL Sci. Rep. 7:42494-42494(2017).
CC -!- FUNCTION: Displays a dual function. As a soluble protein, exhibits
CC glutathione-dependent thiol transferase and dehydroascorbate (DHA)
CC reductase activities (PubMed:12077129). Exhibits glutathione-dependent
CC thiol transferase and dehydroascorbate (DHA) reductase activities. Key
CC component of the ascorbate recycling system. Involved in the redox
CC homeostasis, especially in scavenging of ROS under oxidative stresses.
CC Plays a role in ozone tolerance. {ECO:0000269|PubMed:12077129,
CC ECO:0000269|PubMed:16361320}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:12077129};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC Evidence={ECO:0000269|PubMed:12077129};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9FWR4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- INDUCTION: By ozone. By salicylic acid (SA) (at protein level).
CC {ECO:0000269|PubMed:15159623, ECO:0000269|PubMed:16361320}.
CC -!- PTM: Spontaneous S-glutathionylation in the presence of oxidized
CC glutathione (GSSG). {ECO:0000269|PubMed:12077129}.
CC -!- DISRUPTION PHENOTYPE: Mutant develops distinct foliar lesions under
CC ozone exposure. {ECO:0000269|PubMed:16361320}.
CC -!- SIMILARITY: Belongs to the GST superfamily. DHAR family. {ECO:0000305}.
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DR EMBL; AY074785; AAL71855.1; -; mRNA.
DR EMBL; AC025814; AAG12679.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35696.1; -; Genomic_DNA.
DR EMBL; AY140019; AAM98161.1; -; mRNA.
DR EMBL; BT006257; AAP13365.1; -; mRNA.
DR EMBL; AY087460; AAM65005.1; -; mRNA.
DR PIR; B96783; B96783.
DR RefSeq; NP_177662.1; NM_106182.4.
DR PDB; 5LOL; X-ray; 2.30 A; A=1-213.
DR PDBsum; 5LOL; -.
DR AlphaFoldDB; Q9FRL8; -.
DR SMR; Q9FRL8; -.
DR IntAct; Q9FRL8; 1.
DR STRING; 3702.AT1G75270.1; -.
DR iPTMnet; Q9FRL8; -.
DR SwissPalm; Q9FRL8; -.
DR PaxDb; Q9FRL8; -.
DR PRIDE; Q9FRL8; -.
DR ProteomicsDB; 224116; -.
DR EnsemblPlants; AT1G75270.1; AT1G75270.1; AT1G75270.
DR GeneID; 843864; -.
DR Gramene; AT1G75270.1; AT1G75270.1; AT1G75270.
DR KEGG; ath:AT1G75270; -.
DR Araport; AT1G75270; -.
DR TAIR; locus:2025162; AT1G75270.
DR eggNOG; KOG1422; Eukaryota.
DR HOGENOM; CLU_011226_1_0_1; -.
DR InParanoid; Q9FRL8; -.
DR OMA; EEIHIAY; -.
DR OrthoDB; 974249at2759; -.
DR PhylomeDB; Q9FRL8; -.
DR BioCyc; ARA:AT1G75270-MON; -.
DR PRO; PR:Q9FRL8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FRL8; baseline and differential.
DR Genevisible; Q9FRL8; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0043295; F:glutathione binding; IDA:TAIR.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:TAIR.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0140547; P:acquisition of seed longevity; IGI:TAIR.
DR GO; GO:0033355; P:ascorbate glutathione cycle; IEA:InterPro.
DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IGI:TAIR.
DR GO; GO:0080151; P:positive regulation of salicylic acid mediated signaling pathway; IGI:TAIR.
DR GO; GO:0010731; P:protein glutathionylation; IDA:TAIR.
DR InterPro; IPR044627; DHAR1/2/3/4.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR44420; PTHR44420; 1.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Detoxification; Glutathionylation; Oxidoreductase;
KW Reference proteome; Stress response; Transferase.
FT CHAIN 1..213
FT /note="Glutathione S-transferase DHAR2"
FT /id="PRO_0000395482"
FT DOMAIN 10..83
FT /note="GST N-terminal"
FT DOMAIN 84..213
FT /note="GST C-terminal"
FT MOTIF 20..25
FT /note="Glutathione-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 8
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 19
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 19
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 47
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:28195196,
FT ECO:0007744|PDB:5LOL"
FT BINDING 60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:28195196,
FT ECO:0007744|PDB:5LOL"
FT BINDING 73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:28195196,
FT ECO:0007744|PDB:5LOL"
FT BINDING 160
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 207
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT BINDING 210
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q65XA0"
FT MOD_RES 6
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000269|PubMed:12077129"
FT MOD_RES 20
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000269|PubMed:12077129"
FT CONFLICT 195
FT /note="N -> K (in Ref. 5; AAM65005)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:5LOL"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:5LOL"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:5LOL"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5LOL"
FT TURN 96..101
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:5LOL"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5LOL"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:5LOL"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5LOL"
SQ SEQUENCE 213 AA; 23407 MW; 23543B0F81F96041 CRC64;
MALDICVKVA VGAPDVLGDC PFSQRVLLTL EEKKLPYKTH LINVSDKPQW FLDISPEGKV
PVVKLDGKWV ADSDVIVGLL EEKYPEPSLK TPPEFASVGS KIFGAFVTFL KSKDANDGSE
KALVDELEAL ENHLKTHSGP FVAGEKITAV DLSLAPKLYH LEVALGHYKN WSVPESLTSV
RNYAKALFSR ESFENTKAKK EIVVAGWESK VNA
