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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

Involved in redox regulation of the cell. Protects radical-sensitive enzymes from oxidative damage by a radical-generating system.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei109 – 1091Cysteine sulfenic acid (-SOH) intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, 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:1.11.1.15)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:88034. Prdx3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • early endosome Source: MGI
  • extracellular exosome Source: MGI
  • IkappaB kinase complex Source: Ensembl
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6262MitochondrionBy similarityAdd
BLAST
Chaini63 – 257195Thioredoxin-dependent peroxide reductase, mitochondrialPRO_0000023783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841N6-succinyllysineCombined sources
Modified residuei92 – 921N6-acetyllysine; alternateCombined sources
Modified residuei92 – 921N6-succinyllysine; alternateCombined sources
Disulfide bondi109 – 109Interchain (with C-230); in linked formBy similarity
Disulfide bondi230 – 230Interchain (with C-109); in linked formBy similarity

Post-translational modificationi

Phosphorylated by LRRK2; phosphorylation reduces perodixase activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

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

2D gel databases

REPRODUCTION-2DPAGEIPI00116192.
P20108.

PTM databases

iPTMnetiP20108.
PhosphoSiteiP20108.
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

Dodecameric ring assembled from homodimeric units; disulfide-linked, upon oxidation. The rings have an approximate diameter of 150 A and a central hole of 70 A. 3-5% of the rings are interlocked by pairs. Binds MAP3K13 (By similarity). Interacts with NEK6 (By similarity). Interacts with LRRK2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198117. 1 interaction.
IntActiP20108. 5 interactions.
MINTiMINT-217585.
STRINGi10090.ENSMUSP00000025961.

Structurei

3D structure databases

ProteinModelPortaliP20108.
SMRiP20108. Positions 64-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 222159ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

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

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP20108.
SMRiP20108. Positions 64-254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198117. 1 interaction.
IntActiP20108. 5 interactions.
MINTiMINT-217585.
STRINGi10090.ENSMUSP00000025961.

Protein family/group databases

PeroxiBasei4499. Mm2CysPrx03.

PTM databases

iPTMnetiP20108.
PhosphoSiteiP20108.
SwissPalmiP20108.

2D gel databases

REPRODUCTION-2DPAGEIPI00116192.
P20108.

Proteomic databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10935.
MGIiMGI:88034. Prdx3.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP20108.
KOiK20011.
OMAiTQHAPAF.
OrthoDBiEOG091G0IE5.
PhylomeDBiP20108.
TreeFamiTF105181.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP20108.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024997.
CleanExiMM_PRDX3.
GenevisibleiP20108. 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 nameiPRDX3_MOUSE
AccessioniPrimary (citable) accession number: P20108
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: September 7, 2016
This is version 162 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-109 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-230-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-109 (to Cys-SO3H) upon oxidative stress.By similarity

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

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.