DHAR1_ARATH
ID DHAR1_ARATH Reviewed; 213 AA.
AC Q9FWR4; A8MRM5; Q9LN37;
DT 10-FEB-2009, 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 DHAR1, mitochondrial;
DE EC=2.5.1.18 {ECO:0000269|PubMed:12077129};
DE AltName: Full=Chloride intracellular channel homolog 1;
DE Short=CLIC homolog 1;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase 1 {ECO:0000303|PubMed:12077129};
DE Short=AtDHAR1 {ECO:0000303|PubMed:12077129};
DE Short=GSH-dependent dehydroascorbate reductase 1;
DE Short=mtDHAR;
DE EC=1.8.5.1 {ECO:0000269|PubMed:12077129};
GN Name=DHAR1 {ECO:0000303|PubMed:12077129}; Synonyms=DHAR5;
GN OrderedLocusNames=At1g19570; ORFNames=F14P1.9, F18O14.22;
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] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, FUNCTION, MUTAGENESIS OF CYS-6 AND CYS-20, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, GLUTATHIONYLATION AT CYS-20, AND GENE FAMILY.
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 [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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP PROTEIN SEQUENCE OF 9-25, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=12954611; DOI=10.1074/jbc.m307525200;
RA Chew O., Whelan J., Millar A.H.;
RT "Molecular definition of the ascorbate-glutathione cycle in Arabidopsis
RT mitochondria reveals dual targeting of antioxidant defenses in plants.";
RL J. Biol. Chem. 278:46869-46877(2003).
RN [8]
RP INDUCTION BY INSECTS.
RX PubMed=15494554; DOI=10.1105/tpc.104.026120;
RA Reymond P., Bodenhausen N., Van Poecke R.M.P., Krishnamurthy V., Dicke M.,
RA Farmer E.E.;
RT "A conserved transcript pattern in response to a specialist and a
RT generalist herbivore.";
RL Plant Cell 16:3132-3147(2004).
RN [9]
RP FUNCTION, AND INDUCTION BY JA.
RX PubMed=16262714; DOI=10.1111/j.1365-313x.2005.02560.x;
RA Sasaki-Sekimoto Y., Taki N., Obayashi T., Aono M., Matsumoto F.,
RA Sakurai N., Suzuki H., Hirai M.Y., Noji M., Saito K., Masuda T.,
RA Takamiya K., Shibata D., Ohta H.;
RT "Coordinated activation of metabolic pathways for antioxidants and defence
RT compounds by jasmonates and their roles in stress tolerance in
RT Arabidopsis.";
RL Plant J. 44:653-668(2005).
RN [10]
RP MASS SPECTROMETRY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP GLUTATHIONYLATION AT CYS-20.
RX PubMed=16055689; DOI=10.1104/pp.104.058917;
RA Dixon D.P., Skipsey M., Grundy N.M., Edwards R.;
RT "Stress-induced protein S-glutathionylation in Arabidopsis.";
RL Plant Physiol. 138:2233-2244(2005).
RN [11]
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH COPPER.
RX PubMed=16526091; DOI=10.1002/pmic.200500108;
RA Kung C.-C.S., Huang W.-N., Huang Y.-C., Yeh K.-C.;
RT "Proteomic survey of copper-binding proteins in Arabidopsis roots by
RT immobilized metal affinity chromatography and mass spectrometry.";
RL Proteomics 6:2746-2758(2006).
RN [13]
RP FUNCTION.
RX PubMed=17267397; DOI=10.1074/jbc.m607241200;
RA Elter A., Hartel A., Sieben C., Hertel B., Fischer-Schliebs E., Luttge U.,
RA Moroni A., Thiel G.;
RT "A plant homolog of animal chloride intracellular channels (CLICs)
RT generates an ion conductance in heterologous systems.";
RL J. Biol. Chem. 282:8786-8792(2007).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=19329564; DOI=10.1104/pp.109.137703;
RA Reumann S., Quan S., Aung K., Yang P., Manandhar-Shrestha K., Holbrook D.,
RA Linka N., Switzenberg R., Wilkerson C.G., Weber A.P., Olsen L.J., Hu J.;
RT "In-depth proteome analysis of Arabidopsis leaf peroxisomes combined with
RT in vivo subcellular targeting verification indicates novel metabolic and
RT regulatory functions of peroxisomes.";
RL Plant Physiol. 150:125-143(2009).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RA Menault M., Roszak A.W., Lapthorn A.J.;
RT "Arabidopsis thaliana DHAR1 apo structure.";
RL Submitted (NOV-2015) to the PDB data bank.
CC -!- FUNCTION: Displays a dual function. As a soluble protein, exhibits
CC glutathione-dependent thiol transferase and dehydroascorbate (DHA)
CC reductase activities (PubMed:12077129). Key component of the ascorbate
CC recycling system. Involved in the redox homeostasis, especially in
CC scavenging of ROS under oxidative stresses, subsequently to biotic or
CC abiotic inducers (PubMed:16262714). As a peripheral membrane protein,
CC could also function as voltage-gated ion channel (PubMed:17267397).
CC {ECO:0000269|PubMed:12077129, ECO:0000269|PubMed:16262714,
CC ECO:0000269|PubMed:17267397}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.26 mM for DHA (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:12077129};
CC KM=10 mM for GSH (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:12077129};
CC -!- SUBUNIT: Monomer (PubMed:12077129). Interacts with copper (Cu)
CC (PubMed:16526091). {ECO:0000269|PubMed:12077129,
CC ECO:0000269|PubMed:16526091}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12954611}.
CC Cytoplasm, cytosol {ECO:0000305}. Peroxisome
CC {ECO:0000269|PubMed:19329564}. Membrane {ECO:0000305}; Peripheral
CC membrane protein {ECO:0000305}. Note=Exists both as soluble protein and
CC as membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FWR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FWR4-2; Sequence=VSP_036254;
CC -!- TISSUE SPECIFICITY: Expressed at least in roots and leaves.
CC {ECO:0000269|PubMed:12954611}.
CC -!- INDUCTION: Induced by jasmonic acid (JA), oxidative chemical stresses
CC (e.g. norflurazon, menadione, paraquat, and antimycin A), and during
CC photosynthetic operation in the light. Also up-regulated by insects
CC such as Pieris rapae in a JA-dependent manner.
CC {ECO:0000269|PubMed:12954611, ECO:0000269|PubMed:15494554,
CC ECO:0000269|PubMed:16262714}.
CC -!- DOMAIN: May change from a globular, soluble state to a state where the
CC N-terminal domain is inserted into the membrane and functions as ion
CC channel. A conformation change of the N-terminal domain is thought to
CC expose hydrophobic surfaces that trigger membrane insertion (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Spontaneous S-glutathionylation in the presence of oxidized
CC glutathione (GSSG). {ECO:0000269|PubMed:12077129,
CC ECO:0000269|PubMed:16055689}.
CC -!- MASS SPECTROMETRY: Mass=24.561; Method=Electrospray; Note=Reduced
CC form.; Evidence={ECO:0000269|PubMed:16055689};
CC -!- MASS SPECTROMETRY: Mass=25.319; Method=Electrospray; Note=S-
CC glutathionylated form.; Evidence={ECO:0000269|PubMed:16055689};
CC -!- DISRUPTION PHENOTYPE: Plants react normally to ozone.
CC {ECO:0000269|PubMed:16361320}.
CC -!- SIMILARITY: Belongs to the GST superfamily. DHAR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79440.1; Type=Erroneous gene model prediction; Note=The predicted gene At1g19570 has been split into 2 genes: At1g19565 and At1g19570.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC024609; AAF98403.1; -; Genomic_DNA.
DR EMBL; AC025808; AAF79440.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29868.1; -; Genomic_DNA.
DR EMBL; AY039590; AAK62645.1; -; mRNA.
DR EMBL; AY052211; AAK97681.1; -; mRNA.
DR EMBL; AY055790; AAL06957.1; -; mRNA.
DR EMBL; AY085426; AAM62653.1; -; mRNA.
DR EMBL; AK117865; BAC42506.1; -; mRNA.
DR PIR; D86328; D86328.
DR RefSeq; NP_173387.1; NM_101814.5. [Q9FWR4-1]
DR PDB; 5EL8; X-ray; 2.30 A; A=1-213.
DR PDB; 5ELA; X-ray; 2.28 A; A=1-213.
DR PDB; 5ELG; X-ray; 1.81 A; A=1-213.
DR PDBsum; 5EL8; -.
DR PDBsum; 5ELA; -.
DR PDBsum; 5ELG; -.
DR AlphaFoldDB; Q9FWR4; -.
DR SMR; Q9FWR4; -.
DR BioGRID; 23783; 49.
DR IntAct; Q9FWR4; 48.
DR STRING; 3702.AT1G19570.1; -.
DR TCDB; 1.A.12.2.1; the intracellular chloride channel (clic) family.
DR PaxDb; Q9FWR4; -.
DR PRIDE; Q9FWR4; -.
DR ProteomicsDB; 222016; -. [Q9FWR4-1]
DR EnsemblPlants; AT1G19570.1; AT1G19570.1; AT1G19570. [Q9FWR4-1]
DR GeneID; 838544; -.
DR Gramene; AT1G19570.1; AT1G19570.1; AT1G19570. [Q9FWR4-1]
DR KEGG; ath:AT1G19570; -.
DR Araport; AT1G19570; -.
DR TAIR; locus:2013119; AT1G19570.
DR eggNOG; KOG1422; Eukaryota.
DR HOGENOM; CLU_011226_1_0_1; -.
DR OMA; HYRRFGI; -.
DR PhylomeDB; Q9FWR4; -.
DR BioCyc; ARA:AT1G19570-MON; -.
DR BRENDA; 1.8.5.1; 399.
DR SABIO-RK; Q9FWR4; -.
DR PRO; PR:Q9FWR4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FWR4; baseline and differential.
DR Genevisible; Q9FWR4; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA: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:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0140547; P:acquisition of seed longevity; IGI:TAIR.
DR GO; GO:0033355; P:ascorbate glutathione cycle; IEA:InterPro.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IGI:TAIR.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 GO; GO:0043903; P:regulation of biological process involved in symbiotic interaction; IMP:TAIR.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:TAIR.
DR GO; GO:0010043; P:response to zinc ion; IEP: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; Alternative splicing; Cytoplasm; Detoxification;
KW Direct protein sequencing; Glutathionylation; Ion channel; Ion transport;
KW Membrane; Mitochondrion; Oxidoreductase; Peroxisome; Plant defense;
KW Reference proteome; Stress response; Transferase; Transport;
KW Voltage-gated channel.
FT CHAIN 1..213
FT /note="Glutathione S-transferase DHAR1, mitochondrial"
FT /id="PRO_0000363142"
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 MOTIF 133..137
FT /note="Copper-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|Ref.15, ECO:0007744|PDB:5ELG"
FT BINDING 60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PDB:5ELG"
FT BINDING 73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|Ref.15, ECO:0007744|PDB:5ELG"
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 20
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000269|PubMed:12077129,
FT ECO:0000269|PubMed:16055689"
FT VAR_SEQ 50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_036254"
FT MUTAGEN 6
FT /note="C->S: Reduced activity by 50 percent."
FT /evidence="ECO:0000269|PubMed:12077129"
FT MUTAGEN 20
FT /note="C->S: No activity."
FT /evidence="ECO:0000269|PubMed:12077129"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:5ELG"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:5ELG"
FT HELIX 21..32
FT /evidence="ECO:0007829|PDB:5ELG"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5ELG"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5EL8"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:5ELG"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:5ELG"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5ELG"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:5ELG"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5ELG"
FT TURN 96..101
FT /evidence="ECO:0007829|PDB:5ELG"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:5ELG"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5EL8"
FT HELIX 119..136
FT /evidence="ECO:0007829|PDB:5ELG"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5EL8"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:5ELG"
FT HELIX 149..169
FT /evidence="ECO:0007829|PDB:5ELG"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:5ELG"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:5ELG"
FT HELIX 200..207
FT /evidence="ECO:0007829|PDB:5ELG"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:5ELG"
SQ SEQUENCE 213 AA; 23641 MW; 7CB29B43A79C97D5 CRC64;
MALEICVKAA VGAPDHLGDC PFSQRALLTL EEKSLTYKIH LINLSDKPQW FLDISPQGKV
PVLKIDDKWV TDSDVIVGIL EEKYPDPPLK TPAEFASVGS NIFGTFGTFL KSKDSNDGSE
HALLVELEAL ENHLKSHDGP FIAGERVSAV DLSLAPKLYH LQVALGHFKS WSVPESFPHV
HNYMKTLFSL DSFEKTKTEE KYVISGWAPK VNP
