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Peroxiredoxin 1 (EC 1.11.1.15) (Cytosolic thioredoxin peroxidase) (DPx-4783) (DmTPx-1) (Thioredoxin peroxidase)

 PRDX1_DROME             Reviewed;         194 AA.
Q9V3P0; Q0KHT0;
10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
03-JUL-2019, entry version 162.
RecName: Full=Peroxiredoxin 1;
EC=1.11.1.15 {ECO:0000269|PubMed:11677042};
AltName: Full=Cytosolic thioredoxin peroxidase;
Short=DPx-4783;
Short=DmTPx-1;
AltName: Full=Thioredoxin peroxidase;
Name=Jafrac1; Synonyms=TPX-1; ORFNames=CG1633;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10632718; DOI=10.1046/j.1432-1327.2000.01022.x;
Rodriguez J., Agudo M., Van Damme J., Vandekerckhove J.,
Santaren J.F.;
"Polypeptides differentially expressed in imaginal discs define the
peroxiredoxin family of genes in Drosophila.";
Eur. J. Biochem. 267:487-497(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
AND DEVELOPMENTAL STAGE.
PubMed=11677042; DOI=10.1016/S0891-5849(01)00692-X;
Radyuk S.N., Klichko V.I., Spinola B., Sohal R.S., Orr W.C.;
"The peroxiredoxin gene family in Drosophila melanogaster.";
Free Radic. Biol. Med. 31:1090-1100(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Ovary;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=11877442; DOI=10.1074/jbc.M200636200;
Bauer H., Kanzok S.M., Schirmer R.H.;
"Thioredoxin-2 but not thioredoxin-1 is a substrate of thioredoxin
peroxidase-1 from Drosophila melanogaster: isolation and
characterization of a second thioredoxin in D.melanogaster and
evidence for distinct biological functions of Trx-1 and Trx-2.";
J. Biol. Chem. 277:17457-17463(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-193 AND SER-194, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[9]
DISRUPTION PHENOTYPE.
PubMed=26715182; DOI=10.1007/s00018-015-2121-x;
Khoshnood B., Dacklin I., Grabbe C.;
"Urm1: an essential regulator of JNK signaling and oxidative stress in
Drosophila melanogaster.";
Cell. Mol. Life Sci. 73:1939-1954(2016).
[10]
URMYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=28953965; DOI=10.1371/journal.pone.0185611;
Khoshnood B., Dacklin I., Grabbe C.;
"A proteomics approach to identify targets of the ubiquitin-like
molecule Urm1 in Drosophila melanogaster.";
PLoS ONE 12:E0185611-E0185611(2017).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events. Might participate in
the signaling cascades of growth factors and tumor necrosis
factor-alpha by regulating the intracellular concentrations of
H(2)O(2) (By similarity). Reduces an intramolecular disulfide bond
in GDPD5 that gates the ability to GDPD5 to drive postmitotic
motor neuron differentiation (By similarity).
{ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-dithiol + a hydroperoxide = [protein]-disulfide
+ an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-COMP:10593,
Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058;
EC=1.11.1.15; Evidence={ECO:0000269|PubMed:11677042};
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
assemble to form a ring-like decamer (By similarity). Interacts
with GDPD5; forms a mixed-disulfide with GDPD5 (By similarity).
Interacts with SESN1 and SESN2 (By similarity).
{ECO:0000250|UniProtKB:P0CB50, ECO:0000250|UniProtKB:Q06830}.
-!- INTERACTION:
P11956:MtnB; NbExp=2; IntAct=EBI-82319, EBI-88468;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11677042}.
-!- DEVELOPMENTAL STAGE: Highly expressed during embryogenesis, weakly
expressed during larval stages. {ECO:0000269|PubMed:11677042,
ECO:0000269|PubMed:11877442}.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
instead of its condensation to a disulfide bond. It can be
reactivated by forming a transient disulfide bond with
sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an
ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:Q06830}.
-!- PTM: Conjugated to URM1, a ubiquitin-like protein.
{ECO:0000269|PubMed:28953965}.
-!- DISRUPTION PHENOTYPE: Results in reduced resistance to oxidative
stress (PubMed:26715182). Simultaneous knockout of Urm1 restores
normal sensitivity to oxidative stress (PubMed:26715182).
{ECO:0000269|PubMed:26715182}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by thioredoxin (By similarity).
As a reducing substrate, thioredoxin 2 is preferred over
thioredoxin 1 (PubMed:11877442). {ECO:0000250|UniProtKB:Q06830,
ECO:0000269|PubMed:11877442}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF167098; AAF42985.1; -; mRNA.
EMBL; AF321615; AAK06770.1; -; mRNA.
EMBL; AF321616; AAK06771.1; -; mRNA.
EMBL; AE014298; AAF48253.1; -; Genomic_DNA.
EMBL; AY070534; AAL48005.1; -; mRNA.
EMBL; BT014630; AAT27254.1; -; mRNA.
RefSeq; NP_001285202.1; NM_001298273.1.
RefSeq; NP_001285203.1; NM_001298274.1.
RefSeq; NP_001285204.1; NM_001298275.1.
RefSeq; NP_477510.1; NM_058162.3.
RefSeq; NP_727689.1; NM_167359.2.
SMR; Q9V3P0; -.
BioGrid; 72802; 23.
DIP; DIP-17916N; -.
IntAct; Q9V3P0; 16.
MINT; Q9V3P0; -.
STRING; 7227.FBpp0073594; -.
iPTMnet; Q9V3P0; -.
PaxDb; Q9V3P0; -.
PRIDE; Q9V3P0; -.
EnsemblMetazoa; FBtr0073763; FBpp0073594; FBgn0040309.
EnsemblMetazoa; FBtr0073764; FBpp0073595; FBgn0040309.
EnsemblMetazoa; FBtr0339699; FBpp0308756; FBgn0040309.
EnsemblMetazoa; FBtr0339700; FBpp0308757; FBgn0040309.
EnsemblMetazoa; FBtr0345161; FBpp0311371; FBgn0040309.
GeneID; 53578; -.
KEGG; dme:Dmel_CG1633; -.
CTD; 53578; -.
FlyBase; FBgn0040309; Jafrac1.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
InParanoid; Q9V3P0; -.
KO; K13279; -.
OMA; WYPKDFT; -.
OrthoDB; 1326484at2759; -.
PhylomeDB; Q9V3P0; -.
Reactome; R-DME-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
GenomeRNAi; 53578; -.
PRO; PR:Q9V3P0; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0040309; Expressed in 45 organ(s), highest expression level in embryo.
ExpressionAtlas; Q9V3P0; differential.
Genevisible; Q9V3P0; DM.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IMP:FlyBase.
GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
GO; GO:0007281; P:germ cell development; IMP:FlyBase.
GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:FlyBase.
GO; GO:0045321; P:leukocyte activation; IBA:GO_Central.
GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
GO; GO:0042594; P:response to starvation; IMP:FlyBase.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Antioxidant; Complete proteome; Cytoplasm; Disulfide bond;
Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
Reference proteome; Ubl conjugation.
CHAIN 1 194 Peroxiredoxin 1.
/FTId=PRO_0000135085.
DOMAIN 2 160 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 47 47 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:Q06830}.
MOD_RES 193 193 Phosphothreonine.
{ECO:0000269|PubMed:18327897}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
DISULFID 47 47 Interchain (with C-168); in linked form.
{ECO:0000250|UniProtKB:Q06830}.
DISULFID 168 168 Interchain (with C-47); in linked form.
{ECO:0000250|UniProtKB:Q06830}.
SEQUENCE 194 AA; 21738 MW; 93ED319BE144E8D1 CRC64;
MPQLQKPAPA FAGTAVVNGV FKDIKLSDYK GKYLVLFFYP LDFTFVCPTE IIAFSESAAE
FRKINCEVIG CSTDSQFTHL AWINTPRKQG GLGSMDIPLL ADKSMKVARD YGVLDEETGI
PFRGLFIIDD KQNLRQITVN DLPVGRSVEE TLRLVQAFQY TDKYGEVCPA NWKPGQKTMV
ADPTKSKEYF ETTS


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[ahpC Rv2428] Alkyl hydroperoxide reductase C (MtAhpC) (EC 1.11.1.15) (Peroxiredoxin) (Thioredoxin peroxidase)
[PRDX6 AOP2 GPX PHGPX] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Ciliary body glutathione peroxidase) (Non-selenium glutathione peroxidase) (NSGPx) (PHGPx)
[PRDX6 AOP2 KIAA0106] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (24 kDa protein) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Liver 2D page spot 40) (Non-selenium glutathione peroxidase) (NSGPx) (Red blood cells page spot 12)
[Prdx6 Aop2 Ltw4 Prdx5] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx)
[Prdx6 Aipla2 Aop2 Tsa] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx) (Thiol-specific antioxidant protein)
[HYR1 GPX3 ORP1 YIR037W] Glutathione peroxidase-like peroxiredoxin HYR1 (EC 1.11.1.15) (Glutathione peroxidase homolog 3) (GPx 3) (Hydrogen peroxide resistance protein 1) (Oxidant receptor peroxidase 1) (Phospholipid hydroperoxide glutathione peroxidase 3) (PHGPx3)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[GPX1 YKL026C] Glutathione peroxidase-like peroxiredoxin 1 (EC 1.11.1.15) (Glutathione peroxidase homolog 1) (GPx 1)
[PRDX3 AOP1] Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (HBC189) (Peroxiredoxin III) (Prx-III) (Peroxiredoxin-3) (Protein MER5 homolog)
[ahpE Rv2238c MTCY427.19c] Alkyl hydroperoxide reductase E (EC 1.11.1.15) (Peroxiredoxin AhpE) (Prx) (Thioredoxin peroxidase) (TPx)
[GPX2 YBR244W YBR1632] Glutathione peroxidase-like peroxiredoxin 2 (EC 1.11.1.15) (Glutathione peroxidase homolog 2) (GPx 2)
[PRDX3 AOP1] Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (Peroxiredoxin-3) (Protein SP-22)
[PER1 At1g48130 F21D18.15] 1-Cys peroxiredoxin PER1 (EC 1.11.1.15) (Rehydrin homolog) (Thioredoxin peroxidase)
[PRDX6 RCJMB04_18k11] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[] Peroxiredoxin-2 (Prx) (EC 1.11.1.15) (1-Cys D-peroxiredoxin) (Peroxiredoxin II) (Thioredoxin peroxidase)
[PRXIIC TPX2 At1g65970 F12P19.13] Peroxiredoxin-2C (EC 1.11.1.15) (Peroxiredoxin IIC) (Peroxiredoxin TPx2) (Thioredoxin peroxidase 2C) (Thioredoxin-dependent peroxidase 2)
[APX1 At1g07890 F24B9.2] L-ascorbate peroxidase 1, cytosolic (AP) (AtAPx01) (EC 1.11.1.11)
[APX2 SS622 Os07g0694700 LOC_Os07g49400 OsJ_25704 P0627E10.14] L-ascorbate peroxidase 2, cytosolic (EC 1.11.1.11) (APXb) (OsAPx2)
[APX1 Os03g0285700 LOC_Os03g17690 OsJ_009999 OSJNBa0013D02.10] L-ascorbate peroxidase 1, cytosolic (APXa) (EC 1.11.1.11) (OsAPx1)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[katG cat-2 NCU05770] Catalase-peroxidase (CP) (EC 1.11.1.21) (Catalase-2) (Peroxidase/catalase)
[GPX3 CAALFM_C107350CA orf19.4436] Glutathione peroxidase-like peroxiredoxin GPX3 (EC 1.11.1.15) (Glutathione peroxidase homolog 3) (GPx 3)
[PRDX6 QtsA-11939] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[PRXIIC Os01g0675100 LOC_Os01g48420 OJ1117_G01.9 OsJ_002891 P0485G01.43] Peroxiredoxin-2C (EC 1.11.1.15) (Peroxiredoxin IIC) (Thioredoxin peroxidase 2C)

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