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Protein

Thioredoxin-dependent peroxide reductase, mitochondrial

Gene

Prdx3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (By similarity).By similarity

Catalytic activityi

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

Sites

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

GO - Molecular functioni

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • negative regulation of neuron apoptotic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.

Protein family/group databases

PeroxiBasei4507. Rno2CysPrx03.

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-dependent peroxide reductase, mitochondrial (EC:1.11.1.15)
Alternative name(s):
PRx III
Peroxiredoxin-3
Short name:
PRX-3
Gene namesi
Name:Prdx3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620040. Prdx3.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 62MitochondrionBy similarityAdd BLAST62
ChainiPRO_000025685963 – 257Thioredoxin-dependent peroxide reductase, mitochondrialAdd BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei84N6-succinyllysineBy similarity1
Modified residuei92N6-acetyllysine; alternateBy similarity1
Modified residuei92N6-succinyllysine; alternateBy similarity1
Disulfide bondi109Interchain (with C-229); in linked formBy similarity
Disulfide bondi230Interchain (with C-108); in linked formBy similarity

Post-translational modificationi

Phosphorylated by LRRK2; phosphorylation reduces perodixase activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiQ9Z0V6.
PRIDEiQ9Z0V6.

2D gel databases

World-2DPAGE0004:Q9Z0V6.

PTM databases

iPTMnetiQ9Z0V6.
PhosphoSitePlusiQ9Z0V6.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

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

Protein-protein interaction databases

BioGridi249055. 1 interactor.
IntActiQ9Z0V6. 3 interactors.
MINTiMINT-4621394.
STRINGi10116.ENSRNOP00000015186.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0V6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

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.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ9Z0V6.
KOiK20011.
PhylomeDBiQ9Z0V6.

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.

Q9Z0V6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAGRLLW SSVARPASTI FRSISASTVL RPVASRRTCL TDMLWSACPQ
60 70 80 90 100
AKFAFSTSSS FHTPAVTQHA PHFKGTAVVN GEFKELSLDD FKGKYLVLFF
110 120 130 140 150
YPLDFTFVCP TEIVAFSDKA NEFHDVNCEV VAVSVDSHFS HLAWINTPRK
160 170 180 190 200
NGGLGHMNIT LLSDLTKQIS RDYGVLLESA GIALRGLFII DPNGVIKHLS
210 220 230 240 250
VNDLPVGRSV EEPLRLVKAF QFVETHGEVC PANWTPESPT IKPSPTASKE

YFEKVHQ
Length:257
Mass (Da):28,295
Last modified:October 31, 2006 - v2
Checksum:i752198F5918206AE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti207 – 216Missing in AAH60567 (PubMed:15489334).Curated10
Sequence conflicti232A → P in AAD17992 (PubMed:10025941).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106944 mRNA. Translation: AAD17992.1.
BC060567 mRNA. Translation: AAH60567.1.
RefSeqiNP_071985.1. NM_022540.1.
UniGeneiRn.2011.

Genome annotation databases

GeneIDi64371.
KEGGirno:64371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106944 mRNA. Translation: AAD17992.1.
BC060567 mRNA. Translation: AAH60567.1.
RefSeqiNP_071985.1. NM_022540.1.
UniGeneiRn.2011.

3D structure databases

ProteinModelPortaliQ9Z0V6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249055. 1 interactor.
IntActiQ9Z0V6. 3 interactors.
MINTiMINT-4621394.
STRINGi10116.ENSRNOP00000015186.

Protein family/group databases

PeroxiBasei4507. Rno2CysPrx03.

PTM databases

iPTMnetiQ9Z0V6.
PhosphoSitePlusiQ9Z0V6.

2D gel databases

World-2DPAGE0004:Q9Z0V6.

Proteomic databases

PaxDbiQ9Z0V6.
PRIDEiQ9Z0V6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64371.
KEGGirno:64371.

Organism-specific databases

CTDi10935.
RGDi620040. Prdx3.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ9Z0V6.
KOiK20011.
PhylomeDBiQ9Z0V6.

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.

Miscellaneous databases

PROiQ9Z0V6.

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_RAT
AccessioniPrimary (citable) accession number: Q9Z0V6
Secondary accession number(s): Q6P9W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: November 2, 2016
This is version 103 of the entry and version 2 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. 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.