| IED ID | IndEnz0018001230 |
| Enzyme Type ID | peroxidase001230 |
| Protein Name |
Peroxiredoxin-4 EC 1.11.1.24 Antioxidant enzyme AOE372 Peroxiredoxin IV Prx-IV Thioredoxin peroxidase AO372 Thioredoxin-dependent peroxide reductase A0372 Thioredoxin-dependent peroxiredoxin 4 |
| Gene Name | Prdx4 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MEARSKLLDGTTASRRWTRKLVLLLPPLLLFLLRTESLQGLESDERFRTRENECHFYAGGQVYPGEASRVSVADHSLHLSKAKISKPAPYWEGTAVINGEFKELKLTDYRGKYLVFFFYPLDFTFVCPTEIIAFGDRIEEFKSINTEVVACSVDSQFTHLAWINTPRRQGGLGPIRIPLLSDLNHQISKDYGVYLEDSGHTLRGLFIIDDKGVLRQITLNDLPVGRSVDETLRLVQAFQYTDKHGEVCPAGWKPGSETIIPDPAGKLKYFDKLN |
| Enzyme Length | 274 |
| Uniprot Accession Number | O08807 |
| Absorption | |
| Active Site | ACT_SITE 127; /note=Cysteine sulfenic acid (-SOH) intermediate; /evidence=ECO:0000250|UniProtKB:Q13162 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000250|UniProtKB:Q13162}; |
| DNA Binding | |
| EC Number | 1.11.1.24 |
| Enzyme Function | FUNCTION: 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). {ECO:0000250|UniProtKB:Q13162, ECO:0000269|PubMed:11229364}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (8); Chain (1); Disulfide bond (2); Domain (1); Helix (7); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Antioxidant;Cytoplasm;Direct protein sequencing;Disulfide bond;Endoplasmic reticulum;Oxidoreductase;Peroxidase;Redox-active center;Reference proteome;Signal |
| Interact With | Q8NBS9-1 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13162}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}. Note=Not secreted. {ECO:0000269|PubMed:11229364}. |
| Modified Residue | |
| Post Translational Modification | PTM: 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. {ECO:0000250|UniProtKB:Q13162}. |
| Signal Peptide | SIGNAL 1..40; /evidence=ECO:0000250 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 3VWU; 3VWV; 3W8J; 3WGX; |
| Mapped Pubmed ID | 10501973; 10548725; 11217851; 12050118; 12466851; 12904583; 14651853; 15627969; 15858817; 16615898; 17697936; 17962088; 19105792; 21267068; 21677750; 21835919; 22916164; 22967998; 22981861; 23477499; 23589496; 23909438; 24462249; 25943695; 25975898; 26917265; 27035833; 27689697; 30050648; 30097850; 30149550; 30578917; 31544965; 32185676; 33087733; 33311472; 33456675; 34029576; 34130124; |
| Motif | |
| Gene Encoded By | |
| Mass | 31,053 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:62620 |
| Cross Reference Brenda |