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Protein

Peroxiredoxin-4

Gene

Prdx4

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 (PubMed:11229364). Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation (By similarity).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 sitei127Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

  • peroxidase activity Source: UniProtKB-KW
  • peroxiredoxin activity Source: UniProtKB-EC
  • protein homodimerization activity Source: MGI

GO - Biological processi

  • 4-hydroxyproline metabolic process Source: MGI
  • cell redox homeostasis Source: MGI
  • extracellular matrix organization Source: MGI
  • male gonad development Source: MGI
  • negative regulation of male germ cell proliferation Source: MGI
  • oxidation-reduction process Source: MGI
  • protein maturation by protein folding Source: MGI
  • reactive oxygen species metabolic process Source: MGI
  • spermatogenesis Source: MGI

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Protein family/group databases

PeroxiBasei4532. Mm2CysPrx04.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxiredoxin-4 (EC:1.11.1.15)
Alternative name(s):
Antioxidant enzyme AOE372
Peroxiredoxin IV
Short name:
Prx-IV
Thioredoxin peroxidase AO372
Thioredoxin-dependent peroxide reductase A0372
Gene namesi
Name:Prdx4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1859815. Prdx4.

Subcellular locationi

  • Cytoplasm By similarity
  • Endoplasmic reticulum By similarity

  • Note: Not secreted.1 Publication

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • endoplasmic reticulum Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
  • smooth endoplasmic reticulum Source: Ensembl

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 40By similarityAdd BLAST40
ChainiPRO_000013509941 – 274Peroxiredoxin-4Add BLAST234

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei102N6-succinyllysineBy similarity1
Disulfide bondi127Interchain (with C-248); in linked formCombined sources1 Publication
Disulfide bondi248Interchain (with C-127); in linked formCombined sources1 Publication

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) and sulphonic acid (C(P)-SO3H) instead of its condensation to a disulfide bond.By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiO08807.
MaxQBiO08807.
PaxDbiO08807.
PeptideAtlasiO08807.
PRIDEiO08807.

2D gel databases

REPRODUCTION-2DPAGEiO08807.

PTM databases

iPTMnetiO08807.
PhosphoSitePlusiO08807.
SwissPalmiO08807.

Expressioni

Gene expression databases

BgeeiENSMUSG00000025289.
CleanExiMM_PRDX4.
ExpressionAtlasiO08807. baseline and differential.
GenevisibleiO08807. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer.By similarity

GO - Molecular functioni

  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi207303. 2 interactors.
DIPiDIP-34137N.
IntActiO08807. 7 interactors.
MINTiMINT-1862981.
STRINGi10090.ENSMUSP00000026328.

Structurei

Secondary structure

1274
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi92 – 97Combined sources6
Beta strandi100 – 105Combined sources6
Helixi106 – 109Combined sources4
Beta strandi112 – 118Combined sources7
Beta strandi122 – 126Combined sources5
Helixi129 – 136Combined sources8
Helixi138 – 143Combined sources6
Beta strandi146 – 154Combined sources9
Helixi156 – 163Combined sources8
Helixi167 – 169Combined sources3
Beta strandi179 – 181Combined sources3
Helixi186 – 190Combined sources5
Turni196 – 199Combined sources4
Beta strandi204 – 208Combined sources5
Beta strandi212 – 219Combined sources8
Helixi226 – 244Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3VWUX-ray3.30A/B/C/D/E/F/G/H/I/J41-274[»]
3VWVX-ray1.80A/B87-274[»]
3W8JX-ray2.10C/D244-263[»]
3WGXX-ray0.92C/D244-263[»]
ProteinModelPortaliO08807.
SMRiO08807.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 240ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiO08807.
KOiK03386.
OrthoDBiEOG091G0IE5.
PhylomeDBiO08807.
TreeFamiTF105181.

Family and domain databases

InterProiView protein in InterPro
IPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
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.

O08807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEARSKLLDG TTASRRWTRK LVLLLPPLLL FLLRTESLQG LESDERFRTR
60 70 80 90 100
ENECHFYAGG QVYPGEASRV SVADHSLHLS KAKISKPAPY WEGTAVINGE
110 120 130 140 150
FKELKLTDYR GKYLVFFFYP LDFTFVCPTE IIAFGDRIEE FKSINTEVVA
160 170 180 190 200
CSVDSQFTHL AWINTPRRQG GLGPIRIPLL SDLNHQISKD YGVYLEDSGH
210 220 230 240 250
TLRGLFIIDD KGVLRQITLN DLPVGRSVDE TLRLVQAFQY TDKHGEVCPA
260 270
GWKPGSETII PDPAGKLKYF DKLN
Length:274
Mass (Da):31,053
Last modified:July 1, 1997 - v1
Checksum:i73DB5374EC46241C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96746 mRNA. Translation: AAB57846.1.
AK005031 mRNA. Translation: BAB23758.1.
AK146402 mRNA. Translation: BAE27143.1.
AK152255 mRNA. Translation: BAE31074.1.
BX005263 Genomic DNA. Translation: CAM23139.1.
BC003349 mRNA. Translation: AAH03349.1.
BC019578 mRNA. Translation: AAH19578.1.
CCDSiCCDS30496.1.
RefSeqiNP_001300640.1. NM_001313711.1.
NP_058044.1. NM_016764.5.
UniGeneiMm.247542.

Genome annotation databases

EnsembliENSMUST00000026328; ENSMUSP00000026328; ENSMUSG00000025289.
GeneIDi53381.
KEGGimmu:53381.
UCSCiuc009uru.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiPRDX4_MOUSE
AccessioniPrimary (citable) accession number: O08807
Secondary accession number(s): B1AZS7, Q3U8E4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: August 30, 2017
This is version 159 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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