ID   PRDX2_MACFA             Reviewed;         198 AA.
AC   Q2PFZ3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2026, entry version 93.
DE   RecName: Full=Peroxiredoxin-2;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:P32119};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin 2 {ECO:0000305};
GN   Name=PRDX2; ORFNames=QccE-19689;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque cDNA
RT   oligo-chips.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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. Might participate in the signaling cascades of growth
CC       factors and tumor necrosis factor-alpha by regulating the intracellular
CC       concentrations of H(2)O(2). {ECO:0000250|UniProtKB:P32119}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol +
CC         [thioredoxin]-disulfide + 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:0000250|UniProtKB:P32119};
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC       assemble to form a ring-like decamer. Interacts with TIPIN.
CC       {ECO:0000250|UniProtKB:P32119}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}.
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 SRXN1, which reduces the
CC       cysteine sulfinic acid in an ATP- and Mg-dependent manner.
CC       {ECO:0000250|UniProtKB:P32119, ECO:0000250|UniProtKB:Q06830}.
CC   -!- PTM: Acetylation increases resistance to transition to high molecular-
CC       mass complexes. Deacetylated by HDAC6 which decreases reducing
CC       activity. {ECO:0000250|UniProtKB:P32119}.
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:0000250|UniProtKB:P32119}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AB220444; BAE72977.1; -; mRNA.
DR   RefSeq; XP_045236146.1; XM_045380211.2.
DR   AlphaFoldDB; Q2PFZ3; -.
DR   SMR; Q2PFZ3; -.
DR   STRING; 9541.ENSMFAP00000016916; -.
DR   PeroxiBase; 4482; Mfa2CysPrx02.
DR   Ensembl; ENSMFAT00000067500.2; ENSMFAP00000016962.2; ENSMFAG00000031614.2.
DR   GeneID; 102146129; -.
DR   KEGG; mcf:102146129; -.
DR   CTD; 7001; -.
DR   VEuPathDB; HostDB:ENSMFAG00000031614; -.
DR   eggNOG; KOG0852; Eukaryota.
DR   GeneTree; ENSGT00940000155828; -.
DR   OMA; AADHAQM; -.
DR   Proteomes; UP000233100; Chromosome 19.
DR   Bgee; ENSMFAG00000031614; Expressed in bone marrow and 13 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:TreeGrafter.
DR   GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; ISS:UniProtKB.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter.
DR   GO; GO:0045321; P:leukocyte activation; IEA:TreeGrafter.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:TreeGrafter.
DR   CDD; cd03015; PRX_Typ2cys; 1.
DR   FunFam; 3.40.30.10:FF:000003; Peroxiredoxin 1; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR050217; Peroxiredoxin.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681:SF161; PEROXIREDOXIN-2; 1.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase;
KW   Peroxidase; Phosphoprotein; Redox-active center; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P32119"
FT   CHAIN           2..198
FT                   /note="Peroxiredoxin-2"
FT                   /id="PRO_0000256856"
FT   DOMAIN          6..164
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        51
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P32119"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P32119"
FT   MOD_RES         112
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P32119"
FT   MOD_RES         182
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P32119"
FT   MOD_RES         196
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P32119"
FT   DISULFID        51
FT                   /note="Interchain (with C-172); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P32119"
FT   DISULFID        172
FT                   /note="Interchain (with C-51); in linked form"
FT                   /evidence="ECO:0000250|UniProtKB:P32119"
SQ   SEQUENCE   198 AA;  21892 MW;  1AC781D908B32B46 CRC64;
     MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN
     RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT
     DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
     DTIKPNVDDS KEYFSKHN
//