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Protein

Peroxiredoxin-1

Gene

Prdx1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (PubMed:19766572).By similarity1 Publication

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 sitei52Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cell proliferation Source: MGI
  • cell redox homeostasis Source: InterPro
  • erythrocyte homeostasis Source: MGI
  • hydrogen peroxide catabolic process Source: MGI
  • natural killer cell activation Source: MGI
  • natural killer cell mediated cytotoxicity Source: MGI
  • regulation of NIK/NF-kappaB signaling Source: MGI
  • regulation of stress-activated MAPK cascade Source: MGI
  • removal of superoxide radicals Source: MGI
  • response to oxidative stress Source: MGI
  • response to reactive oxygen species 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

PeroxiBasei4555 Mm2CysPrx01-1

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-1 (EC:1.11.1.15)
Alternative name(s):
Macrophage 23 kDa stress protein
Osteoblast-specific factor 3
Short name:
OSF-3
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Gene namesi
Name:Prdx1
Synonyms:Msp23, Paga, Tdpx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:99523 Prdx1

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

Pathology & Biotechi

Disruption phenotypei

Mice embryos loss approximately 50% of Islet1/Islet2+ and HB9+ motor neurons, whereas dorsal-ventral patterning events and the numbers of Olig2+ progenitors are normal. Toward the end of the cell death phase they have equivalent numbers of motor neurons as wild type embryos.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001350772 – 199Peroxiredoxin-1Add BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei7N6-acetyllysine; alternateBy similarity1
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei16N6-acetyllysineBy similarity1
Modified residuei27N6-acetyllysineBy similarity1
Modified residuei32PhosphoserineBy similarity1
Modified residuei35N6-acetyllysine; alternateBy similarity1
Modified residuei35N6-succinyllysine; alternateCombined sources1
Disulfide bondi52Interchain (with C-173); in linked formBy similarity
Modified residuei90PhosphothreonineBy similarity1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei136N6-acetyllysineCombined sources1
Disulfide bondi173Interchain (with C-52; in linked form)By similarity
Cross-linki185Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Post-translational modificationi

Phosphorylated on Thr-90 during the M-phase, which leads to a decrease in enzymatic activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP35700
MaxQBiP35700
PaxDbiP35700
PeptideAtlasiP35700
PRIDEiP35700
TopDownProteomicsiP35700

2D gel databases

REPRODUCTION-2DPAGEiP35700
SWISS-2DPAGEiP35700

PTM databases

iPTMnetiP35700
PhosphoSitePlusiP35700
SwissPalmiP35700

Expressioni

Tissue specificityi

Found in various tissues; high concentration in liver.

Inductioni

By oxidative and sulfhydryl-reactive agents.

Gene expression databases

BgeeiENSMUSG00000028691
CleanExiMM_PRDX1
ExpressionAtlasiP35700 baseline and differential
GenevisibleiP35700 MM

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi202018, 14 interactors
IntActiP35700, 25 interactors
MINTiP35700
STRINGi10090.ENSMUSP00000102078

Structurei

3D structure databases

ProteinModelPortaliP35700
SMRiP35700
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 165ThioredoxinPROSITE-ProRule annotationAdd BLAST160

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiKOG0852 Eukaryota
COG0450 LUCA
GeneTreeiENSGT00390000004653
HOGENOMiHOG000022343
HOVERGENiHBG000286
InParanoidiP35700
KOiK13279
OMAiFAWTNTP
OrthoDBiEOG091G0IE5
PhylomeDBiP35700
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.

P35700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSGNAKIGY PAPNFKATAV MPDGQFKDIS LSEYKGKYVV FFFYPLDFTF
60 70 80 90 100
VCPTEIIAFS DRADEFKKLN CQVIGASVDS HFCHLAWINT PKKQGGLGPM
110 120 130 140 150
NIPLISDPKR TIAQDYGVLK ADEGISFRGL FIIDDKGILR QITINDLPVG
160 170 180 190
RSVDEIIRLV QAFQFTDKHG EVCPAGWKPG SDTIKPDVNK SKEYFSKQK
Length:199
Mass (Da):22,176
Last modified:June 1, 1994 - v1
Checksum:iBEF5C995A86124D1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti196S → F in BAB27120 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16142 mRNA Translation: BAA03713.1
D21252 mRNA Translation: BAA04796.1
AF157331, AF157329, AF157330 Genomic DNA Translation: AAD45323.1
AB023564 Genomic DNA Translation: BAA86992.1
AK002287 mRNA Translation: BAB21990.1
AK008711 mRNA Translation: BAB25847.1
AK010688 mRNA Translation: BAB27120.1
AK083243 mRNA Translation: BAC38827.1
AK145138 mRNA Translation: BAE26255.1
AK150797 mRNA Translation: BAE29860.1
AK151459 mRNA Translation: BAE30417.1
AK167624 mRNA Translation: BAE39676.1
AK169154 mRNA Translation: BAE40933.1
BC083348 mRNA Translation: AAH83348.1
BC086648 mRNA Translation: AAH86648.1
CCDSiCCDS18515.1
PIRiA48513
RefSeqiNP_035164.1, NM_011034.4
UniGeneiMm.30929

Genome annotation databases

EnsembliENSMUST00000106470; ENSMUSP00000102078; ENSMUSG00000028691
ENSMUST00000135573; ENSMUSP00000114159; ENSMUSG00000028691
GeneIDi18477
KEGGimmu:18477
UCSCiuc008uhd.1 mouse

Similar proteinsi

Entry informationi

Entry nameiPRDX1_MOUSE
AccessioniPrimary (citable) accession number: P35700
Secondary accession number(s): Q3UBV4, Q9CWI2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 18, 2018
This is version 184 of the entry and version 1 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

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