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Protein

Peroxiredoxin-2

Gene

Prdx2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 H2O2.By similarity

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

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei51Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

  • antioxidant activity Source: MGI
  • peroxidase activity Source: MGI
  • selenium binding Source: MGI
  • thioredoxin peroxidase activity Source: MGI

GO - Biological processi

  • activation of MAPK activity Source: MGI
  • cell redox homeostasis Source: InterPro
  • cellular response to oxidative stress Source: MGI
  • homeostasis of number of cells Source: MGI
  • hydrogen peroxide catabolic process Source: MGI
  • hydrogen peroxide metabolic process Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
  • negative regulation of lipopolysaccharide-mediated signaling pathway Source: MGI
  • negative regulation of NF-kappaB transcription factor activity Source: MGI
  • negative regulation of reactive oxygen species metabolic process Source: MGI
  • negative regulation of T cell differentiation Source: MGI
  • positive regulation of blood coagulation Source: BHF-UCL
  • regulation of apoptotic process Source: MGI
  • regulation of hydrogen peroxide metabolic process Source: MGI
  • removal of superoxide radicals Source: BHF-UCL
  • respiratory burst involved in inflammatory response Source: MGI
  • response to lipopolysaccharide Source: MGI
  • response to oxidative stress Source: MGI
  • T cell proliferation Source: MGI
  • thymus development Source: MGI

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiR-MMU-3299685. Detoxification of Reactive Oxygen Species.
R-MMU-5628897. TP53 Regulates Metabolic Genes.

Protein family/group databases

PeroxiBasei4474. Mm2CysPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-2 (EC:1.11.1.15)
Alternative name(s):
Thiol-specific antioxidant protein
Short name:
TSA
Thioredoxin peroxidase 1
Thioredoxin-dependent peroxide reductase 1
Gene namesi
Name:Prdx2
Synonyms:Tdpx1, Tpx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:109486. Prdx2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001350812 – 198Peroxiredoxin-2Add BLAST197

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei11PhosphoserineCombined sources1
Disulfide bondi51Interchain (with C-172); in linked formBy similarity
Modified residuei112PhosphoserineBy similarity1
Disulfide bondi172Interchain (with C-51); in linked formBy similarity
Modified residuei182PhosphothreonineBy similarity1

Post-translational modificationi

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.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ61171.
MaxQBiQ61171.
PaxDbiQ61171.
PeptideAtlasiQ61171.
PRIDEiQ61171.
TopDownProteomicsiQ61171.

2D gel databases

REPRODUCTION-2DPAGEiQ61171.
SWISS-2DPAGEiQ61171.
UCD-2DPAGEiQ61171.

PTM databases

iPTMnetiQ61171.
PhosphoSitePlusiQ61171.
SwissPalmiQ61171.

Expressioni

Tissue specificityi

Widely expressed with highest levels in bone marrow. High levels also found in heart, brain, kidney and skeletal muscle. Lower levels in liver, lung and thymus.

Gene expression databases

BgeeiENSMUSG00000005161.
CleanExiMM_PRDX2.
ExpressionAtlasiQ61171. baseline and differential.
GenevisibleiQ61171. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (By similarity). Interacts with TIPIN (PubMed:17141802).By similarity1 Publication

Protein-protein interaction databases

BioGridi204094. 5 interactors.
IntActiQ61171. 14 interactors.
MINTiMINT-1862390.
STRINGi10090.ENSMUSP00000005292.

Structurei

3D structure databases

ProteinModelPortaliQ61171.
SMRiQ61171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 164ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ61171.
KOiK03386.
OMAiFKEVKLC.
OrthoDBiEOG091G0IE5.
PhylomeDBiQ61171.
TreeFamiTF105181.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR036249. Thioredoxin-like_sf.
IPR013766. Thioredoxin_domain.
PfamiView protein in Pfam
PF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
PIRSFiPIRSF000239. AHPC. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiView protein in PROSITE
PS51352. THIOREDOXIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q61171-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGNAQIGK SAPDFTATAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV
60 70 80 90 100
CPTEIIAFSD HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN
110 120 130 140 150
IPLLADVTKS LSQNYGVLKN DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR
160 170 180 190
SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN
Length:198
Mass (Da):21,779
Last modified:January 23, 2007 - v3
Checksum:iFE216F5426F7174D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38V → M in BAB27093 (PubMed:16141072).Curated1
Sequence conflicti39V → D in BAB23893 (PubMed:16141072).Curated1
Sequence conflicti69G → R in BAB23893 (PubMed:16141072).Curated1
Sequence conflicti97G → A in AAA69475 (Ref. 3) Curated1
Sequence conflicti113Q → H in BAB23893 (PubMed:16141072).Curated1
Sequence conflicti124I → V in BAB23893 (PubMed:16141072).Curated1
Sequence conflicti135K → S in BAB23893 (PubMed:16141072).Curated1
Sequence conflicti182T → N (Ref. 3) Curated1
Sequence conflicti182T → N (PubMed:9714804).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51679 mRNA. Translation: AAB01941.1.
X82067 mRNA. Translation: CAA57566.1.
U20611 mRNA. Translation: AAA69475.1.
AF032722
, AF032718, AF032719, AF032720, AF032721 Genomic DNA. Translation: AAC35744.1.
AK005225 mRNA. Translation: BAB23893.1.
AK008433 mRNA. Translation: BAB25666.1.
AK010653 mRNA. Translation: BAB27093.1.
AK088280 mRNA. Translation: BAC40255.1.
BC002034 mRNA. Translation: AAH02034.1.
BC081454 mRNA. Translation: AAH81454.1.
CCDSiCCDS40416.1.
RefSeqiNP_001304314.1. NM_001317385.1.
NP_035693.3. NM_011563.6.
UniGeneiMm.347009.
Mm.393373.

Genome annotation databases

EnsembliENSMUST00000005292; ENSMUSP00000005292; ENSMUSG00000005161.
ENSMUST00000109733; ENSMUSP00000105355; ENSMUSG00000005161.
ENSMUST00000109734; ENSMUSP00000105356; ENSMUSG00000005161.
ENSMUST00000164807; ENSMUSP00000126451; ENSMUSG00000005161.
GeneIDi21672.
KEGGimmu:21672.
UCSCiuc009mom.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiPRDX2_MOUSE
AccessioniPrimary (citable) accession number: Q61171
Secondary accession number(s): O88376
, Q60796, Q9CWJ4, Q9DB49
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 175 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families