ID PRDX2_RAT Reviewed; 198 AA. AC P35704; Q6PDV3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 181. DE RecName: Full=Peroxiredoxin-2; DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P32119}; DE AltName: Full=Thiol-specific antioxidant protein; DE Short=TSA; DE AltName: Full=Thioredoxin peroxidase 1; DE AltName: Full=Thioredoxin-dependent peroxide reductase 1; DE AltName: Full=Thioredoxin-dependent peroxiredoxin 2 {ECO:0000305}; GN Name=Prdx2; Synonyms=Tdpx1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=8041738; DOI=10.1073/pnas.91.15.7017; RA Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.; RT "Cloning and sequencing of thiol-specific antioxidant from mammalian brain: RT alkyl hydroperoxide reductase and thiol-specific antioxidant define a large RT family of antioxidant enzymes."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pituitary; 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 [3] RP PROTEIN SEQUENCE OF 93-135 AND 140-157, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord; RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.; RL Submitted (JUL-2007) to UniProtKB. 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}. 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; U06099; AAA19959.1; -; mRNA. DR EMBL; BC058481; AAH58481.1; -; mRNA. DR PIR; A57716; A57716. DR RefSeq; NP_058865.2; NM_017169.2. DR RefSeq; XP_006255306.1; XM_006255244.3. DR AlphaFoldDB; P35704; -. DR SMR; P35704; -. DR BioGRID; 247997; 11. DR FunCoup; P35704; 1793. DR IntAct; P35704; 5. DR MINT; P35704; -. DR STRING; 10116.ENSRNOP00000004799; -. DR PeroxiBase; 4477; Rno2CysPrx02. DR GlyGen; P35704; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P35704; -. DR PhosphoSitePlus; P35704; -. DR SwissPalm; P35704; -. DR jPOST; P35704; -. DR PaxDb; 10116-ENSRNOP00000004799; -. DR GeneID; 29338; -. DR KEGG; rno:29338; -. DR AGR; RGD:3838; -. DR CTD; 7001; -. DR RGD; 3838; Prdx2. DR eggNOG; KOG0852; Eukaryota. DR InParanoid; P35704; -. DR OrthoDB; 185659at2759; -. DR PhylomeDB; P35704; -. DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species. DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes. DR PRO; PR:P35704; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:RGD. DR GO; GO:0016209; F:antioxidant activity; ISO:RGD. DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:RGD. DR GO; GO:0140824; F:thioredoxin-dependent peroxiredoxin activity; ISS:UniProtKB. DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD. DR GO; GO:0002357; P:defense response to tumor cell; ISO:RGD. DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:RGD. DR GO; GO:0042743; P:hydrogen peroxide metabolic process; ISO:RGD. DR GO; GO:0045321; P:leukocyte activation; IBA:GO_Central. DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; ISO:RGD. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD. DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD. DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; ISO:RGD. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD. DR GO; GO:0045581; P:negative regulation of T cell differentiation; ISO:RGD. DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:RGD. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD. DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; ISO:RGD. DR GO; GO:0019430; P:removal of superoxide radicals; ISO:RGD. DR GO; GO:0002536; P:respiratory burst involved in inflammatory response; ISO:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD. DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD. DR GO; GO:0042098; P:T cell proliferation; ISO:RGD. DR GO; GO:0048538; P:thymus development; ISO:RGD. 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 1: Evidence at protein level; KW Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing; KW Disulfide bond; Oxidoreductase; Peroxidase; Phosphoprotein; KW 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_0000135083" 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" FT CONFLICT 17 FT /note="G -> A (in Ref. 2; AAH58481)" FT /evidence="ECO:0000305" SQ SEQUENCE 198 AA; 21784 MW; FC6AD9B0E9C4447B CRC64; MASGNAHIGK PAPDFTGTAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN //