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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

Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

Catalytic activityi

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

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
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1859815. Prdx4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • endoplasmic reticulum Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: Ensembl
  • mitochondrion Source: MGI
  • nucleus Source: MGI
  • smooth endoplasmic reticulum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Secreted

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
Disulfide bondi127Interchain (with C-248); in linked formBy similarity
Disulfide bondi248Interchain (with C-127); in linked formBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiO08807.
MaxQBiO08807.
PaxDbiO08807.
PeptideAtlasiO08807.
PRIDEiO08807.

2D gel databases

REPRODUCTION-2DPAGEO08807.

PTM databases

iPTMnetiO08807.
PhosphoSitePlusiO08807.
SwissPalmiO08807.

Expressioni

Gene expression databases

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

Interactioni

Subunit structurei

Homodimer or heterodimer with PRDX1; disulfide-linked, upon oxidation.

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

Belongs to the AhpC/TSA family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

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

Protein family/group databases

PeroxiBasei4532. Mm2CysPrx04.

PTM databases

iPTMnetiO08807.
PhosphoSitePlusiO08807.
SwissPalmiO08807.

2D gel databases

REPRODUCTION-2DPAGEO08807.

Proteomic databases

EPDiO08807.
MaxQBiO08807.
PaxDbiO08807.
PeptideAtlasiO08807.
PRIDEiO08807.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10549.
MGIiMGI:1859815. Prdx4.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiO08807.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRDX4_MOUSE
AccessioniPrimary (citable) accession number: O08807
Secondary accession number(s): B1AZS7, Q3U8E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: November 30, 2016
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The active site is the redox-active Cys-127 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-248-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin (By similarity).By similarity
Irreversibly inactivated by overoxidation of Cys-127 (to Cys-SO3H) upon oxidative stress.By similarity

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.