PRDX2_MOUSE
ID PRDX2_MOUSE Reviewed; 198 AA.
AC Q61171; O88376; Q60796; Q9CWJ4; Q9DB49;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 204.
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, Tpx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9115640; DOI=10.1089/dna.1997.16.311;
RA Ichimiya S., Davis J.G., O'Rourke D.M., Katsumata M., Greene M.I.;
RT "Murine thioredoxin peroxidase delays neuronal apoptosis and is expressed
RT in areas of the brain most susceptible to hypoxic and ischemic injury.";
RL DNA Cell Biol. 16:311-321(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129;
RA Oberbaeumer I.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Chae H.Z., Kim H., Rhee S.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RX PubMed=9714804; DOI=10.1016/s0378-1119(98)00290-x;
RA Lim M.J., Chae H.Z., Rhee S.G., Yu D.-Y., Lee K.-K., Yeom Y.I.;
RT "The type II peroxiredoxin gene family of the mouse: molecular structure,
RT expression and evolution.";
RL Gene 216:197-205(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Cerebellum, Small intestine, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and 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 PROTEIN SEQUENCE OF 2-10 AND 120-135, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 11-26; 92-109; 120-127 AND 140-150, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP INTERACTION WITH TIPIN.
RX PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097;
RA Gotter A.L., Suppa C., Emanuel B.S.;
RT "Mammalian TIMELESS and Tipin are evolutionarily conserved replication
RT fork-associated factors.";
RL J. Mol. Biol. 366:36-52(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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=[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:0000250|UniProtKB:P32119};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC assemble to form a ring-like decamer (By similarity). Interacts with
CC TIPIN (PubMed:17141802). {ECO:0000250|UniProtKB:P32119,
CC ECO:0000269|PubMed:17141802}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in bone
CC marrow. High levels also found in heart, brain, kidney and skeletal
CC muscle. Lower levels in liver, lung and thymus.
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 -!- 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; U51679; AAB01941.1; -; mRNA.
DR EMBL; X82067; CAA57566.1; -; mRNA.
DR EMBL; U20611; AAA69475.1; -; mRNA.
DR EMBL; AF032722; AAC35744.1; -; Genomic_DNA.
DR EMBL; AF032718; AAC35744.1; JOINED; Genomic_DNA.
DR EMBL; AF032719; AAC35744.1; JOINED; Genomic_DNA.
DR EMBL; AF032720; AAC35744.1; JOINED; Genomic_DNA.
DR EMBL; AF032721; AAC35744.1; JOINED; Genomic_DNA.
DR EMBL; AK005225; BAB23893.1; -; mRNA.
DR EMBL; AK008433; BAB25666.1; -; mRNA.
DR EMBL; AK010653; BAB27093.1; -; mRNA.
DR EMBL; AK088280; BAC40255.1; -; mRNA.
DR EMBL; BC002034; AAH02034.1; -; mRNA.
DR EMBL; BC081454; AAH81454.1; -; mRNA.
DR CCDS; CCDS40416.1; -.
DR RefSeq; NP_001304314.1; NM_001317385.1.
DR RefSeq; NP_035693.3; NM_011563.6.
DR AlphaFoldDB; Q61171; -.
DR SMR; Q61171; -.
DR BioGRID; 204094; 29.
DR IntAct; Q61171; 13.
DR MINT; Q61171; -.
DR STRING; 10090.ENSMUSP00000005292; -.
DR PeroxiBase; 4474; Mm2CysPrx02.
DR iPTMnet; Q61171; -.
DR PhosphoSitePlus; Q61171; -.
DR SwissPalm; Q61171; -.
DR REPRODUCTION-2DPAGE; Q61171; -.
DR SWISS-2DPAGE; Q61171; -.
DR UCD-2DPAGE; Q61171; -.
DR CPTAC; non-CPTAC-3401; -.
DR EPD; Q61171; -.
DR jPOST; Q61171; -.
DR MaxQB; Q61171; -.
DR PaxDb; Q61171; -.
DR PeptideAtlas; Q61171; -.
DR PRIDE; Q61171; -.
DR ProteomicsDB; 291866; -.
DR TopDownProteomics; Q61171; -.
DR Antibodypedia; 3283; 577 antibodies from 45 providers.
DR DNASU; 21672; -.
DR Ensembl; ENSMUST00000005292; ENSMUSP00000005292; ENSMUSG00000005161.
DR Ensembl; ENSMUST00000109733; ENSMUSP00000105355; ENSMUSG00000005161.
DR Ensembl; ENSMUST00000109734; ENSMUSP00000105356; ENSMUSG00000005161.
DR Ensembl; ENSMUST00000164807; ENSMUSP00000126451; ENSMUSG00000005161.
DR GeneID; 21672; -.
DR KEGG; mmu:21672; -.
DR UCSC; uc009mom.1; mouse.
DR CTD; 7001; -.
DR MGI; MGI:109486; Prdx2.
DR VEuPathDB; HostDB:ENSMUSG00000005161; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000155828; -.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; Q61171; -.
DR OMA; VCTKELC; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; Q61171; -.
DR TreeFam; TF105181; -.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR BioGRID-ORCS; 21672; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Prdx2; mouse.
DR PRO; PR:Q61171; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61171; protein.
DR Bgee; ENSMUSG00000005161; Expressed in cortical plate and 243 other tissues.
DR ExpressionAtlas; Q61171; baseline and differential.
DR Genevisible; Q61171; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; ISO:MGI.
DR GO; GO:0004601; F:peroxidase activity; TAS:MGI.
DR GO; GO:0008430; F:selenium binding; TAS:MGI.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISS:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:0002357; P:defense response to tumor cell; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:MGI.
DR GO; GO:0042743; P:hydrogen peroxide metabolic process; IMP:MGI.
DR GO; GO:0045321; P:leukocyte activation; IBA:GO_Central.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:MGI.
DR GO; GO:0045581; P:negative regulation of T cell differentiation; IMP:MGI.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IMP:BHF-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR GO; GO:0010310; P:regulation of hydrogen peroxide metabolic process; IMP:MGI.
DR GO; GO:0019430; P:removal of superoxide radicals; IMP:BHF-UCL.
DR GO; GO:0002536; P:respiratory burst involved in inflammatory response; IMP:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR GO; GO:0048538; P:thymus development; IMP:MGI.
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 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:0000269|Ref.7"
FT CHAIN 2..198
FT /note="Peroxiredoxin-2"
FT /id="PRO_0000135081"
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:0000269|Ref.7"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 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 38
FT /note="V -> M (in Ref. 5; BAB27093)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="V -> D (in Ref. 5; BAB23893)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="G -> R (in Ref. 5; BAB23893)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="G -> A (in Ref. 3; AAA69475)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Q -> H (in Ref. 5; BAB23893)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="I -> V (in Ref. 5; BAB23893)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="K -> S (in Ref. 5; BAB23893)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="T -> N (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 198 AA; 21779 MW; FE216F5426F7174D CRC64;
MASGNAQIGK SAPDFTATAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD
HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN
DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
DTIKPNVDDS KEYFSKHN
