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 24-JAN-2024, entry version 156. 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.Q9FWR4; -. DR TCDB; 1.A.12.2.1; the intracellular chloride channel (clic) family. DR PaxDb; 3702-AT1G19570-1; -. 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; AT1G19570; DHAR1. DR eggNOG; KOG1422; Eukaryota. DR HOGENOM; CLU_011226_1_0_1; -. DR InParanoid; Q9FWR4; -. DR OMA; ERHIMKH; -. DR OrthoDB; 103277at2759; -. DR PhylomeDB; Q9FWR4; -. DR BioCyc; ARA:AT1G19570-MONOMER; -. 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 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:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW. 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: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:0034220; P:monoatomic ion transmembrane transport; IEA:UniProtKB-KW. 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: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 CDD; cd00570; GST_N_family; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. 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:SF4; F18O14.31-RELATED; 1. DR PANTHER; PTHR44420; GLUTATHIONE S-TRANSFERASE DHAR2-RELATED; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF13409; GST_N_2; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG00358; Main_(cytGST); 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. DR Genevisible; Q9FWR4; AT. 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 //