GLRX2_HUMAN
ID GLRX2_HUMAN Reviewed; 164 AA.
AC Q9NS18; Q3LR69; Q7L1N7; Q96JC0; Q9Y3D4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Glutaredoxin-2, mitochondrial;
DE Flags: Precursor;
GN Name=GLRX2; Synonyms=GRX2; ORFNames=CGI-133;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Colon, and Testis;
RX PubMed=11297543; DOI=10.1074/jbc.m011605200;
RA Lundberg M., Johansson C., Chandra J., Enoksson M., Jacobsson G., Ljung J.,
RA Johansson M., Holmgren A.;
RT "Cloning and expression of a novel human glutaredoxin (Grx2) with
RT mitochondrial and nuclear isoforms.";
RL J. Biol. Chem. 276:26269-26275(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11397793; DOI=10.1074/jbc.m100020200;
RA Gladyshev V.N., Liu A., Novoselov S.V., Krysan K., Sun Q.-A., Kryukov V.M.,
RA Kryukov G.V., Lou M.F.;
RT "Identification and characterization of a new mammalian glutaredoxin
RT (thioltransferase), Grx2.";
RL J. Biol. Chem. 276:30374-30380(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-95.
RG NIEHS SNPs program;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-164 (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-164 (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=15184054; DOI=10.1016/j.bbrc.2004.04.199;
RA Lundberg M., Fernandes A.P., Kumar S., Holmgren A.;
RT "Cellular and plasma levels of human glutaredoxin 1 and 2 detected by
RT sensitive ELISA systems.";
RL Biochem. Biophys. Res. Commun. 319:801-809(2004).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=15297967; DOI=10.1016/j.humpath.2004.04.009;
RA Peltoniemi M., Kaarteenaho-Wiik R., Saily M., Sormunen R., Paakko P.,
RA Holmgren A., Soini Y., Kinnula V.L.;
RT "Expression of glutaredoxin is highly cell specific in human lung and is
RT decreased by transforming growth factor-beta in vitro and in interstitial
RT lung diseases in vivo.";
RL Hum. Pathol. 35:1000-1007(2004).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF SER-78 AND
RP CYS-80.
RX PubMed=14676218; DOI=10.1074/jbc.m312719200;
RA Johansson C., Lillig C.H., Holmgren A.;
RT "Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with
RT high affinity accepting electrons from either glutathione or thioredoxin
RT reductase.";
RL J. Biol. Chem. 279:7537-7543(2004).
RN [10]
RP FUNCTION.
RX PubMed=15328416; DOI=10.1073/pnas.0401896101;
RA Lillig C.H., Loenn M.E., Enoksson M., Fernandes A.P., Holmgren A.;
RT "Short interfering RNA-mediated silencing of glutaredoxin 2 increases the
RT sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13227-13232(2004).
RN [11]
RP FUNCTION.
RX PubMed=15649413; DOI=10.1016/j.bbrc.2004.12.067;
RA Enoksson M., Fernandes A.P., Prast S., Lillig C.H., Holmgren A.,
RA Orrenius S.;
RT "Overexpression of glutaredoxin 2 attenuates apoptosis by preventing
RT cytochrome c release.";
RL Biochem. Biophys. Res. Commun. 327:774-779(2005).
RN [12]
RP SUBUNIT, ACTIVITY REGULATION, METAL-BINDING, AND MUTAGENESIS OF CYS-68 AND
RP CYS-153.
RX PubMed=15917333; DOI=10.1073/pnas.0500735102;
RA Lillig C.H., Berndt C., Vergnolle O., Loenn M.E., Hudemann C., Bill E.,
RA Holmgren A.;
RT "Characterization of human glutaredoxin 2 as iron-sulfur protein: a
RT possible role as redox sensor.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8168-8173(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP STRUCTURE BY NMR OF 48-164.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-044, an N-terminal 2 domain of glutaredoxin
RT 2 from human cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 50-164 IN COMPLEX WITH
RP GLUTATHIONE, GLUTATHIONYLATION AT CYS-77, AND DISULFIDE BOND.
RX PubMed=17121859; DOI=10.1074/jbc.m608179200;
RA Johansson C., Kavanagh K.L., Gileadi O., Oppermann U.;
RT "Reversible sequestration of active site cysteines in a 2Fe-2S-bridged
RT dimer provides a mechanism for glutaredoxin 2 regulation in human
RT mitochondria.";
RL J. Biol. Chem. 282:3077-3082(2007).
CC -!- FUNCTION: Glutathione-dependent oxidoreductase that facilitates the
CC maintenance of mitochondrial redox homeostasis upon induction of
CC apoptosis by oxidative stress. Involved in response to hydrogen
CC peroxide and regulation of apoptosis caused by oxidative stress. Acts
CC as a very efficient catalyst of monothiol reactions because of its high
CC affinity for protein glutathione-mixed disulfides. Can receive
CC electrons not only from glutathione (GSH), but also from thioredoxin
CC reductase supporting both monothiol and dithiol reactions. Efficiently
CC catalyzes both glutathionylation and deglutathionylation of
CC mitochondrial complex I, which in turn regulates the superoxide
CC production by the complex. Overexpression decreases the susceptibility
CC to apoptosis and prevents loss of cardiolipin and cytochrome c release.
CC {ECO:0000269|PubMed:11297543, ECO:0000269|PubMed:14676218,
CC ECO:0000269|PubMed:15328416, ECO:0000269|PubMed:15649413}.
CC -!- ACTIVITY REGULATION: The 2Fe-2S present in the homodimer leads to
CC inactivation of the enzyme. The 2Fe-2S may serve as a redox sensor: the
CC presence of one-electron oxidants or reductants leading to the loss of
CC the 2Fe-2S cluster, subsequent monomerization and activation of the
CC enzyme. Unlike other glutaredoxins, it is not inhibited by oxidation of
CC structural Cys residues. {ECO:0000269|PubMed:15917333}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.9 mM for GSH {ECO:0000269|PubMed:14676218};
CC KM=0.77 mM for glutathionylated ribonuclease A
CC {ECO:0000269|PubMed:14676218};
CC KM=4.3 mM for glutathionylated BSA {ECO:0000269|PubMed:14676218};
CC KM=0.11 mM for glutathionylated beta-mercaptoethanol
CC {ECO:0000269|PubMed:14676218};
CC -!- SUBUNIT: Monomer; active form. Homodimer; inactive form. The homodimer
CC is probably linked by 1 2Fe-2S cluster. {ECO:0000269|PubMed:15917333,
CC ECO:0000269|PubMed:17121859}.
CC -!- INTERACTION:
CC Q9NS18; Q7Z4W1: DCXR; NbExp=3; IntAct=EBI-12102178, EBI-1044712;
CC Q9NS18; Q9UKW6: ELF5; NbExp=3; IntAct=EBI-12102178, EBI-747605;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Grx2a;
CC IsoId=Q9NS18-1; Sequence=Displayed;
CC Name=2; Synonyms=Grx2b;
CC IsoId=Q9NS18-2; Sequence=VSP_015221;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
CC skeletal muscle, colon, thymus, spleen, kidney, liver, small intestine,
CC placenta and lung. Not expressed in peripheral blood leukocytes.
CC {ECO:0000269|PubMed:11297543, ECO:0000269|PubMed:15184054,
CC ECO:0000269|PubMed:15297967}.
CC -!- MISCELLANEOUS: The absence of GLRX2 dramatically sensitizes cells to
CC cell death induced by doxorubicin/adriamycin and phenylarsine oxide.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34128.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH28113.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/glrx2/";
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DR EMBL; AF132495; AAF37320.2; -; mRNA.
DR EMBL; AF290514; AAK83089.1; -; mRNA.
DR EMBL; AY038988; AAK72499.1; -; mRNA.
DR EMBL; DQ194815; ABA03170.1; -; Genomic_DNA.
DR EMBL; AL136370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF151891; AAD34128.1; ALT_FRAME; mRNA.
DR EMBL; BC028113; AAH28113.1; ALT_INIT; mRNA.
DR CCDS; CCDS1380.1; -. [Q9NS18-2]
DR CCDS; CCDS1381.1; -. [Q9NS18-1]
DR RefSeq; NP_001230328.1; NM_001243399.1.
DR RefSeq; NP_001306220.1; NM_001319291.1.
DR RefSeq; NP_057150.2; NM_016066.4. [Q9NS18-2]
DR RefSeq; NP_932066.1; NM_197962.2. [Q9NS18-1]
DR RefSeq; XP_016856886.1; XM_017001397.1.
DR PDB; 2CQ9; NMR; -; A=48-164.
DR PDB; 2FLS; X-ray; 2.05 A; A=56-164.
DR PDB; 2HT9; X-ray; 1.90 A; A/B=41-164.
DR PDBsum; 2CQ9; -.
DR PDBsum; 2FLS; -.
DR PDBsum; 2HT9; -.
DR AlphaFoldDB; Q9NS18; -.
DR SMR; Q9NS18; -.
DR BioGRID; 119228; 10.
DR IntAct; Q9NS18; 3.
DR STRING; 9606.ENSP00000356410; -.
DR DrugBank; DB00143; Glutathione.
DR iPTMnet; Q9NS18; -.
DR PhosphoSitePlus; Q9NS18; -.
DR BioMuta; GLRX2; -.
DR DMDM; 73919686; -.
DR EPD; Q9NS18; -.
DR jPOST; Q9NS18; -.
DR MassIVE; Q9NS18; -.
DR MaxQB; Q9NS18; -.
DR PeptideAtlas; Q9NS18; -.
DR PRIDE; Q9NS18; -.
DR ProteomicsDB; 82463; -. [Q9NS18-1]
DR ProteomicsDB; 82464; -. [Q9NS18-2]
DR Antibodypedia; 20620; 185 antibodies from 28 providers.
DR DNASU; 51022; -.
DR Ensembl; ENST00000367439.8; ENSP00000356409.3; ENSG00000023572.10. [Q9NS18-1]
DR Ensembl; ENST00000367440.3; ENSP00000356410.3; ENSG00000023572.10. [Q9NS18-2]
DR Ensembl; ENST00000608166.2; ENSP00000494652.1; ENSG00000023572.10. [Q9NS18-1]
DR GeneID; 51022; -.
DR KEGG; hsa:51022; -.
DR MANE-Select; ENST00000367439.8; ENSP00000356409.3; NM_197962.3; NP_932066.1.
DR UCSC; uc001gsz.3; human. [Q9NS18-1]
DR CTD; 51022; -.
DR DisGeNET; 51022; -.
DR GeneCards; GLRX2; -.
DR HGNC; HGNC:16065; GLRX2.
DR HPA; ENSG00000023572; Low tissue specificity.
DR MIM; 606820; gene.
DR neXtProt; NX_Q9NS18; -.
DR OpenTargets; ENSG00000023572; -.
DR PharmGKB; PA28732; -.
DR VEuPathDB; HostDB:ENSG00000023572; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00940000162420; -.
DR HOGENOM; CLU_026126_7_0_1; -.
DR InParanoid; Q9NS18; -.
DR OMA; DSTHAQF; -.
DR OrthoDB; 1535999at2759; -.
DR PhylomeDB; Q9NS18; -.
DR TreeFam; TF319627; -.
DR PathwayCommons; Q9NS18; -.
DR SABIO-RK; Q9NS18; -.
DR SignaLink; Q9NS18; -.
DR BioGRID-ORCS; 51022; 14 hits in 1082 CRISPR screens.
DR EvolutionaryTrace; Q9NS18; -.
DR GeneWiki; GLRX2; -.
DR GenomeRNAi; 51022; -.
DR Pharos; Q9NS18; Tbio.
DR PRO; PR:Q9NS18; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NS18; protein.
DR Bgee; ENSG00000023572; Expressed in sperm and 206 other tissues.
DR Genevisible; Q9NS18; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; TAS:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; NAS:UniProtKB.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; TAS:UniProtKB.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003756; F:protein disulfide isomerase activity; TAS:UniProtKB.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; TAS:UniProtKB.
DR GO; GO:0071451; P:cellular response to superoxide; IEA:Ensembl.
DR GO; GO:0042262; P:DNA protection; NAS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; TAS:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0010033; P:response to organic substance; IDA:UniProtKB.
DR GO; GO:0051775; P:response to redox state; TAS:UniProtKB.
DR GO; GO:0009266; P:response to temperature stimulus; NAS:UniProtKB.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Alternative splicing; Disulfide bond;
KW Electron transport; Glutathionylation; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Nucleus; Phosphoprotein; Redox-active center;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..164
FT /note="Glutaredoxin-2, mitochondrial"
FT /id="PRO_0000011628"
FT DOMAIN 57..157
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 68
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in inactive form"
FT /evidence="ECO:0000305"
FT BINDING 74
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:17121859"
FT BINDING 109
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:17121859"
FT BINDING 121
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:17121859"
FT BINDING 153
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in inactive form"
FT /evidence="ECO:0000305"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 77
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:17121859"
FT DISULFID 77..80
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..40
FT /note="MIWRRAALAGTRLVWSRSGSAGWLDRAAGAAGAAAAAASG -> MNPRDKQV
FT SRFSPLKDVYTWVALAGIQRSGSPGRTRSAARR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11297543"
FT /id="VSP_015221"
FT VARIANT 95
FT /note="K -> E (in dbSNP:rs34237236)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_025234"
FT MUTAGEN 68
FT /note="C->S: Abolishes absorption at 320 nm and 420 nm
FT suggesting the loss of 2Fe-2S-binding."
FT /evidence="ECO:0000269|PubMed:15917333"
FT MUTAGEN 78
FT /note="S->P: Specifically increases the specific activity
FT but decreases affinity for glutathionylated substrates."
FT /evidence="ECO:0000269|PubMed:14676218"
FT MUTAGEN 80
FT /note="C->S: Strongly impairs enzymatic activity."
FT /evidence="ECO:0000269|PubMed:14676218"
FT MUTAGEN 153
FT /note="C->S: Abolishes absorption at 320 nm and 420 nm
FT suggesting the loss of 2Fe-2S-binding."
FT /evidence="ECO:0000269|PubMed:15917333"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:2HT9"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2HT9"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:2HT9"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:2HT9"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2HT9"
FT HELIX 105..116
FT /evidence="ECO:0007829|PDB:2HT9"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2HT9"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:2HT9"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:2HT9"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:2HT9"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:2CQ9"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2HT9"
FT VARIANT Q9NS18-2:40
FT /note="R -> W (in dbSNP:rs10921310)"
FT /evidence="ECO:0000305"
FT /id="VAR_082825"
SQ SEQUENCE 164 AA; 18052 MW; D9798A01BB532A5D CRC64;
MIWRRAALAG TRLVWSRSGS AGWLDRAAGA AGAAAAAASG MESNTSSSLE NLATAPVNQI
QETISDNCVV IFSKTSCSYC TMAKKLFHDM NVNYKVVELD LLEYGNQFQD ALYKMTGERT
VPRIFVNGTF IGGATDTHRL HKEGKLLPLV HQCYLKKSKR KEFQ
