TSA1_YEAST
ID TSA1_YEAST Reviewed; 196 AA.
AC P34760; D6VZE6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Peroxiredoxin TSA1 {ECO:0000305};
DE Short=Prx;
DE EC=1.11.1.24 {ECO:0000269|PubMed:9888818};
DE AltName: Full=Cytoplasmic thiol peroxidase 1 {ECO:0000303|PubMed:10681558};
DE Short=cTPx 1 {ECO:0000303|PubMed:10681558};
DE AltName: Full=Protector protein {ECO:0000303|PubMed:2895105};
DE Short=PRP;
DE AltName: Full=Thiol-specific antioxidant protein 1 {ECO:0000303|PubMed:8344960};
DE AltName: Full=Thioredoxin peroxidase type Ia {ECO:0000303|PubMed:9888818};
DE Short=TPx type Ia;
DE AltName: Full=Thioredoxin-dependent peroxide reductase {ECO:0000303|PubMed:7961686};
DE AltName: Full=Thioredoxin-dependent peroxiredoxin TSA1 {ECO:0000305};
GN Name=TSA1 {ECO:0000303|PubMed:8344960}; Synonyms=TPX1, TSA, ZRG14;
GN OrderedLocusNames=YML028W {ECO:0000312|SGD:S000004490};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE OF 2-13; 62-66; 79-87; 90-94;
RP 137-143; 148-153; 155-161 AND 192-196, CLEAVAGE OF INITIATOR METHIONINE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=JD7-7C;
RX PubMed=8344960; DOI=10.1016/s0021-9258(19)85489-3;
RA Chae H.Z., Kim I.-H., Kim K., Rhee S.G.;
RT "Cloning, sequencing, and mutation of thiol-specific antioxidant gene of
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 268:16815-16821(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 15-19; 32-38; 155-159 AND 165-169, SUBUNIT, ACTIVE
RP SITE, DISULFIDE BOND, AND MUTAGENESIS OF CYS-48 AND CYS-171.
RX PubMed=8041739; DOI=10.1073/pnas.91.15.7022;
RA Chae H.Z., Uhm T.B., Rhee S.G.;
RT "Dimerization of thiol-specific antioxidant and the essential role of
RT cysteine 47.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:7022-7026(1994).
RN [5]
RP FUNCTION.
RX PubMed=2895105; DOI=10.1016/s0021-9258(18)68840-4;
RA Kim K., Kim I.H., Lee K.Y., Rhee S.G., Stadtman E.R.;
RT "The isolation and purification of a specific 'protector' protein which
RT inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation
RT system.";
RL J. Biol. Chem. 263:4704-4711(1988).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-48 AND CYS-171.
RX PubMed=7961686; DOI=10.1016/s0021-9258(18)47038-x;
RA Chae H.Z., Chung S.J., Rhee S.G.;
RT "Thioredoxin-dependent peroxide reductase from yeast.";
RL J. Biol. Chem. 269:27670-27678(1994).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9888818; DOI=10.1021/bi9817818;
RA Jeong J.S., Kwon S.J., Kang S.W., Rhee S.G., Kim K.;
RT "Purification and characterization of a second type thioredoxin peroxidase
RT (type II TPx) from Saccharomyces cerevisiae.";
RL Biochemistry 38:776-783(1999).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10681558; DOI=10.1074/jbc.275.8.5723;
RA Park S.G., Cha M.-K., Jeong W., Kim I.-H.;
RT "Distinct physiological functions of thiol peroxidase isoenzymes in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 275:5723-5732(2000).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP DISULFIDE BOND WITH SRX1.
RX PubMed=14586471; DOI=10.1038/nature02075;
RA Biteau B., Labarre J., Toledano M.B.;
RT "ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae
RT sulphiredoxin.";
RL Nature 425:980-984(2003).
RN [11]
RP FUNCTION.
RX PubMed=15163410; DOI=10.1016/j.cell.2004.05.002;
RA Jang H.H., Lee K.O., Chi Y.H., Jung B.G., Park S.K., Park J.H., Lee J.R.,
RA Lee S.S., Moon J.C., Yun J.W., Choi Y.O., Kim W.Y., Kang J.S., Cheong G.W.,
RA Yun D.J., Rhee S.G., Cho M.J., Lee S.Y.;
RT "Two enzymes in one; two yeast peroxiredoxins display oxidative stress-
RT dependent switching from a peroxidase to a molecular chaperone function.";
RL Cell 117:625-635(2004).
RN [12]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15210711; DOI=10.1074/jbc.m313773200;
RA Munhoz D.C., Netto L.E.;
RT "Cytosolic thioredoxin peroxidase I and II are important defenses of yeast
RT against organic hydroperoxide insult: catalases and peroxiredoxins
RT cooperate in the decomposition of H2O2 by yeast.";
RL J. Biol. Chem. 279:35219-35227(2004).
RN [13]
RP FUNCTION.
RX PubMed=15706081; DOI=10.1089/ars.2005.7.327;
RA Okazaki S., Naganuma A., Kuge S.;
RT "Peroxiredoxin-mediated redox regulation of the nuclear localization of
RT Yap1, a transcription factor in budding yeast.";
RL Antioxid. Redox Signal. 7:327-334(2005).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18271751; DOI=10.1042/bj20071634;
RA Trotter E.W., Rand J.D., Vickerstaff J., Grant C.M.;
RT "The yeast Tsa1 peroxiredoxin is a ribosome-associated antioxidant.";
RL Biochem. J. 412:73-80(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP FUNCTION, AND INTERACTION WITH YAP1.
RX PubMed=19106090; DOI=10.1074/jbc.m807583200;
RA Tachibana T., Okazaki S., Murayama A., Naganuma A., Nomoto A., Kuge S.;
RT "A major peroxiredoxin-induced activation of Yap1 transcription factor is
RT mediated by reduction-sensitive disulfide bonds and reveals a low level of
RT transcriptional activation.";
RL J. Biol. Chem. 284:4464-4472(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [18]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-89 AND LYS-132, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24424024; DOI=10.1242/jcs.144022;
RA Weids A.J., Grant C.M.;
RT "The yeast peroxiredoxin Tsa1 protects against protein-aggregate-induced
RT oxidative stress.";
RL J. Cell Sci. 127:1327-1335(2014).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF MUTANT SER-48 IN COMPLEX WITH
RP DITHIOTHREITOL.
RX PubMed=22985967; DOI=10.1016/j.jmb.2012.09.008;
RA Tairum C.A. Jr., de Oliveira M.A., Horta B.B., Zara F.J., Netto L.E.;
RT "Disulfide biochemistry in 2-cys peroxiredoxin: requirement of Glu50 and
RT Arg146 for the reduction of yeast Tsa1 by thioredoxin.";
RL J. Mol. Biol. 424:28-41(2012).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides and as sensor of hydrogen peroxide-mediated
CC signaling events (PubMed:2895105, PubMed:7961686, PubMed:10681558,
CC PubMed:15210711, PubMed:19106090). Protects the cell against the
CC oxidative stress caused by nascent-protein misfolding and aggregation
CC (PubMed:24424024). Relays hydrogen peroxide as a signal to the
CC transcription factor YAP1 by inducing the formation of intramolecular
CC disulfide bonds in YAP1, which causes its nuclear accumulation and
CC activation (PubMed:15706081, PubMed:19106090). Can act alternatively as
CC peroxidase and molecular chaperone. Oxidative stress and heat shock
CC exposure cause a reversible shift of the protein structure from low MW
CC species to high MW complexes, triggering a peroxidase-to-chaperone
CC functional switch. The chaperone function of the protein enhances
CC resistance to heat shock (PubMed:15163410).
CC {ECO:0000269|PubMed:10681558, ECO:0000269|PubMed:15163410,
CC ECO:0000269|PubMed:15210711, ECO:0000269|PubMed:15706081,
CC ECO:0000269|PubMed:19106090, ECO:0000269|PubMed:24424024,
CC ECO:0000269|PubMed:2895105, ECO:0000269|PubMed:7961686}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000269|PubMed:9888818};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 uM for H(2)O(2) {ECO:0000269|PubMed:9888818};
CC KM=4 uM for cumene hydroperoxide {ECO:0000269|PubMed:9888818};
CC KM=10 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:9888818};
CC KM=2 uM for TRX1 {ECO:0000269|PubMed:9888818};
CC KM=3 uM for TRX2 {ECO:0000269|PubMed:9888818};
CC KM=12 uM for H(2)O(2) {ECO:0000269|PubMed:15210711};
CC KM=17.1 uM for cumene hydroperoxide {ECO:0000269|PubMed:15210711};
CC KM=7.9 uM for tert-butyl hydroperoxide {ECO:0000269|PubMed:15210711};
CC Vmax=4.8 umol/min/mg enzyme for H(2)O(2)
CC {ECO:0000269|PubMed:9888818};
CC Vmax=2.2 umol/min/mg enzyme for cumene hydroperoxide
CC {ECO:0000269|PubMed:9888818};
CC Vmax=2.4 umol/min/mg enzyme for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:9888818};
CC Vmax=5.5 umol/min/mg enzyme for TRX1 {ECO:0000269|PubMed:9888818};
CC Vmax=5.5 umol/min/mg enzyme for TRX2 {ECO:0000269|PubMed:9888818};
CC Vmax=0.66 uM/sec/mg enzyme for H(2)O(2)
CC {ECO:0000269|PubMed:15210711};
CC Vmax=0.56 uM/sec/mg enzyme for cumene hydroperoxide
CC {ECO:0000269|PubMed:15210711};
CC Vmax=0.61 uM/sec/mg enzyme for tert-butyl hydroperoxide
CC {ECO:0000269|PubMed:15210711};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (PubMed:8041739).
CC Interacts with YAP1 via transient disulfide linkages (PubMed:19106090).
CC {ECO:0000269|PubMed:19106090, ECO:0000269|PubMed:8041739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10681558,
CC ECO:0000269|PubMed:18271751, ECO:0000269|PubMed:24424024,
CC ECO:0000269|PubMed:8344960}. Note=Associates with ribosomes
CC (PubMed:18271751). Colocalizes with sites of protein aggregation
CC adjacent to active mitochondria (PubMed:24424024).
CC {ECO:0000269|PubMed:18271751, ECO:0000269|PubMed:24424024}.
CC -!- PTM: The enzyme can be inactivated by further oxidation of the cysteine
CC sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its
CC condensation to a disulfide bond. It can be reactivated by forming a
CC transient disulfide bond with sulfiredoxin SRX1, which reduces the
CC cysteine sulfinic acid in an ATP- and Mg-dependent manner.
CC {ECO:0000269|PubMed:14586471}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000305|PubMed:8041739}.
CC -!- MISCELLANEOUS: Present with 378000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; L14640; AAA16374.1; -; Unassigned_DNA.
DR EMBL; Z46659; CAA86627.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09870.1; -; Genomic_DNA.
DR PIR; A47362; A47362.
DR RefSeq; NP_013684.1; NM_001182386.1.
DR PDB; 3SBC; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J=1-196.
DR PDBsum; 3SBC; -.
DR AlphaFoldDB; P34760; -.
DR SMR; P34760; -.
DR BioGRID; 35141; 626.
DR DIP; DIP-1667N; -.
DR IntAct; P34760; 38.
DR MINT; P34760; -.
DR STRING; 4932.YML028W; -.
DR MoonProt; P34760; -.
DR PeroxiBase; 4465; Sce2CysPrx01.
DR CarbonylDB; P34760; -.
DR iPTMnet; P34760; -.
DR SWISS-2DPAGE; P34760; -.
DR MaxQB; P34760; -.
DR PaxDb; P34760; -.
DR PRIDE; P34760; -.
DR TopDownProteomics; P34760; -.
DR EnsemblFungi; YML028W_mRNA; YML028W; YML028W.
DR GeneID; 854980; -.
DR KEGG; sce:YML028W; -.
DR SGD; S000004490; TSA1.
DR VEuPathDB; FungiDB:YML028W; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000153430; -.
DR HOGENOM; CLU_042529_21_1_1; -.
DR InParanoid; P34760; -.
DR OMA; FWYPKDF; -.
DR BioCyc; YEAST:YML028W-MON; -.
DR Reactome; R-SCE-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:P34760; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P34760; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IMP:CAFA.
DR GO; GO:0019207; F:kinase regulator activity; IMP:SGD.
DR GO; GO:0051920; F:peroxiredoxin activity; IDA:SGD.
DR GO; GO:0043022; F:ribosome binding; IDA:SGD.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:SGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:CAFA.
DR GO; GO:0071447; P:cellular response to hydroperoxide; IMP:CAFA.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:SGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:CAFA.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IGI:SGD.
DR GO; GO:0042262; P:DNA protection; IMP:SGD.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:CAFA.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:CAFA.
DR GO; GO:0006457; P:protein folding; IDA:SGD.
DR GO; GO:0051258; P:protein polymerization; IMP:CAFA.
DR GO; GO:0050821; P:protein stabilization; IMP:CAFA.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IMP:SGD.
DR GO; GO:0033194; P:response to hydroperoxide; IMP:SGD.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Isopeptide bond; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Redox-active center; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8344960"
FT CHAIN 2..196
FT /note="Peroxiredoxin TSA1"
FT /id="PRO_0000135095"
FT DOMAIN 3..161
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 48
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000305|PubMed:8041739"
FT BINDING 45..47
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22985967,
FT ECO:0007744|PDB:3SBC"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22985967,
FT ECO:0007744|PDB:3SBC"
FT SITE 45
FT /note="Important for catalytic activity, helps activating
FT the peroxidatic cysteine through H-bonding"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT DISULFID 48
FT /note="Interchain (with C-171); in linked form"
FT /evidence="ECO:0000305|PubMed:7961686"
FT DISULFID 48
FT /note="Interchain (with C-84 in SRX1); transient"
FT /evidence="ECO:0000269|PubMed:14586471"
FT DISULFID 171
FT /note="Interchain (with C-48); in linked form"
FT /evidence="ECO:0000305|PubMed:7961686"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 48
FT /note="C->S: Exists mainly as monomer. Has no peroxiredoxin
FT activity. Fails to protect glutamine synthetase against
FT damage by DTT oxidation."
FT /evidence="ECO:0000269|PubMed:7961686,
FT ECO:0000269|PubMed:8041739"
FT MUTAGEN 171
FT /note="C->S: Exists mainly as monomer. Has no peroxiredoxin
FT activity."
FT /evidence="ECO:0000269|PubMed:7961686,
FT ECO:0000269|PubMed:8041739"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:3SBC"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:3SBC"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:3SBC"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:3SBC"
FT HELIX 47..64
FT /evidence="ECO:0007829|PDB:3SBC"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:3SBC"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:3SBC"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3SBC"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3SBC"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:3SBC"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:3SBC"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:3SBC"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:3SBC"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:3SBC"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3SBC"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:3SBC"
SQ SEQUENCE 196 AA; 21590 MW; 9ACF40E410F2C04A CRC64;
MVAQVQKQAP TFKKTAVVDG VFDEVSLDKY KGKYVVLAFI PLAFTFVCPT EIIAFSEAAK
KFEEQGAQVL FASTDSEYSL LAWTNIPRKE GGLGPINIPL LADTNHSLSR DYGVLIEEEG
VALRGLFIID PKGVIRHITI NDLPVGRNVD EALRLVEAFQ WTDKNGTVLP CNWTPGAATI
KPTVEDSKEY FEAANK
