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

GO - Molecular functioni

GO - Biological processi

  • 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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6262MitochondrionBy similarityAdd
BLAST
Chaini63 – 257195Thioredoxin-dependent peroxide reductase, mitochondrialBy similarityPRO_0000256859Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841N6-succinyllysineBy similarity
Modified residuei92 – 921N6-acetyllysine; alternateBy similarity
Modified residuei92 – 921N6-succinyllysine; alternateBy similarity
Disulfide bondi109 – 109Interchain (with C-229); in linked formBy similarity
Disulfide bondi230 – 230Interchain (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.

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 interaction.
IntActiQ9Z0V6. 3 interactions.
MINTiMINT-4621394.
STRINGi10116.ENSRNOP00000015186.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0V6.
SMRiQ9Z0V6. 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.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiQ9Z0V6.
KOiK03386.
PhylomeDBiQ9Z0V6.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 21610Missing in AAH60567 (PubMed:15489334).Curated
Sequence conflicti232 – 2321A → P in AAD17992 (PubMed:10025941).Curated

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.
SMRiQ9Z0V6. Positions 64-254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249055. 1 interaction.
IntActiQ9Z0V6. 3 interactions.
MINTiMINT-4621394.
STRINGi10116.ENSRNOP00000015186.

Protein family/group databases

PeroxiBasei4507. Rno2CysPrx03.

PTM databases

iPTMnetiQ9Z0V6.

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.
KOiK03386.
PhylomeDBiQ9Z0V6.

Enzyme and pathway databases

BRENDAi1.11.1.15. 5301.

Miscellaneous databases

NextBioi613116.
PROiQ9Z0V6.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000866. AhpC/TSA.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the peroxiredoxin gene family in rats and characterization of the fourth member."
    Matsumoto A., Okado A., Fujii T., Fujii J., Egashira M., Niikawa N., Taniguchi N.
    FEBS Lett. 443:246-250(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 171-208; 172-197 AND 209-239, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.

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: January 20, 2016
This is version 98 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.