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Protein

Thioredoxin-dependent peroxide reductase, mitochondrial

Gene

Prdx3

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.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.1 Publication

Catalytic activityi

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei109Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

ReactomeiR-MMU-3299685. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei4499. Mm2CysPrx03.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-dependent peroxide reductase, mitochondrial (EC:1.11.1.151 Publication)
Alternative name(s):
Antioxidant protein 1
Short name:
AOP-1
PRX III
Perioredoxin-3
Protein MER5
Gene namesi
Name:Prdx3
Synonyms:Aop1, Mer5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:88034. Prdx3.

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

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 62MitochondrionBy similarityAdd BLAST62
ChainiPRO_000002378363 – 257Thioredoxin-dependent peroxide reductase, mitochondrialAdd BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei84N6-succinyllysineCombined sources1
Modified residuei92N6-acetyllysine; alternateCombined sources1
Modified residuei92N6-succinyllysine; alternateCombined sources1
Disulfide bondi109Interchain (with C-230); in linked formBy similarity
Disulfide bondi230Interchain (with C-109); in linked formBy similarity

Post-translational modificationi

Phosphorylated by LRRK2; phosphorylation reduces perodixase activity.By similarity
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

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP20108.
MaxQBiP20108.
PaxDbiP20108.
PeptideAtlasiP20108.
PRIDEiP20108.
TopDownProteomicsiP20108.

2D gel databases

REPRODUCTION-2DPAGEiIPI00116192.
P20108.

PTM databases

iPTMnetiP20108.
PhosphoSitePlusiP20108.
SwissPalmiP20108.

Expressioni

Tissue specificityi

Housekeeping-type gene preferentially expressed in murine erythroleukemia (MEL) cells.

Inductioni

Expression is increased after induction of MEL cells to differentiation by DMSO.

Gene expression databases

BgeeiENSMUSG00000024997.
CleanExiMM_PRDX3.
GenevisibleiP20108. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked, upon oxidation. 6 homodimers assemble to form a ring-like dodecamer. Interacts with NEK6. Interacts with LRRK2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198117. 1 interactor.
IntActiP20108. 5 interactors.
MINTiMINT-217585.
STRINGi10090.ENSMUSP00000025961.

Structurei

3D structure databases

ProteinModelPortaliP20108.
SMRiP20108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini64 – 222ThioredoxinPROSITE-ProRule annotationAdd BLAST159

Sequence similaritiesi

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP20108.
KOiK20011.
OMAiTAVHNGE.
OrthoDBiEOG091G0IE5.
PhylomeDBiP20108.
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.

P20108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAGRLLW SSVARHASAI SRSISASTVL RPVASRRTCL TDILWSASAQ
60 70 80 90 100
GKSAFSTSSS FHTPAVTQHA PYFKGTAVVN GEFKELSLDD FKGKYLVLFF
110 120 130 140 150
YPLDFTFVCP TEIVAFSDKA NEFHDVNCEV VAVSVDSHFS HLAWINTPRK
160 170 180 190 200
NGGLGHMNIT LLSDITKQIS RDYGVLLESA GIALRGLFII DPNGVVKHLS
210 220 230 240 250
VNDLPVGRSV EETLRLVKAF QFVETHGEVC PANWTPESPT IKPSPTASKE

YFEKVHQ
Length:257
Mass (Da):28,127
Last modified:February 1, 1991 - v1
Checksum:i66513F2C5F1D56C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28723 mRNA. Translation: AAA39524.1.
AF211938
, AF211933, AF211934, AF211935, AF211936, AF211937 Genomic DNA. Translation: AAF63705.1.
AK002448 mRNA. Translation: BAB22108.1.
BC005626 mRNA. Translation: AAH05626.1.
CCDSiCCDS29944.1.
PIRiJQ0064.
RefSeqiNP_031478.1. NM_007452.2.
UniGeneiMm.29821.

Genome annotation databases

EnsembliENSMUST00000025961; ENSMUSP00000025961; ENSMUSG00000024997.
GeneIDi11757.
KEGGimmu:11757.
UCSCiuc008icd.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiPRDX3_MOUSE
AccessioniPrimary (citable) accession number: P20108
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 25, 2017
This is version 171 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