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Protein

Thioredoxin-dependent peroxide reductase, mitochondrial

Gene

PRDX3

Organism
Bos taurus (Bovine)
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)DescriptionActionsGraphical viewLength
Active sitei109Cysteine sulfenic acid (-SOH) intermediateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

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

Protein family/group databases

PeroxiBasei4502. Bt2CysPrx03.

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
Peroxiredoxin-3
Protein SP-222 Publications
Gene namesi
Name:PRDX3
Synonyms:AOP1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 26

Subcellular locationi

  • Mitochondrion 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 62Mitochondrion1 PublicationAdd BLAST62
ChainiPRO_000002378163 – 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-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

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

PaxDbiP35705.
PeptideAtlasiP35705.
PRIDEiP35705.

Expressioni

Tissue specificityi

Predominantly expressed in adrenal cortex. Also detected in liver, renal cortex and medulla, and adrenal medulla (at protein level).1 Publication

Gene expression databases

BgeeiENSBTAG00000008731.

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. Interacts with NEK6 (By similarity). Interacts with LRRK2 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-48458N.
STRINGi9913.ENSBTAP00000011505.

Structurei

Secondary structure

1257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi74 – 79Combined sources6
Beta strandi82 – 87Combined sources6
Helixi88 – 91Combined sources4
Beta strandi94 – 100Combined sources7
Beta strandi107 – 109Combined sources3
Helixi110 – 118Combined sources9
Helixi120 – 124Combined sources5
Turni125 – 127Combined sources3
Beta strandi128 – 136Combined sources9
Helixi138 – 145Combined sources8
Helixi149 – 151Combined sources3
Beta strandi158 – 163Combined sources6
Helixi168 – 172Combined sources5
Turni178 – 181Combined sources4
Beta strandi185 – 190Combined sources6
Beta strandi194 – 202Combined sources9
Helixi210 – 225Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZYEX-ray3.30A/B/C/D/E/F/G/H/I/J/K/L63-257[»]
4MH2X-ray2.20A/B/C/D/E/F/G/H/I/J/K/L63-257[»]
4MH3X-ray2.40A/B/C/D/E/F/G/H/I/J/K/L63-257[»]
ProteinModelPortaliP35705.
SMRiP35705.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35705.

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.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP35705.
KOiK20011.
OMAiTQHAPAF.
OrthoDBiEOG091G0IE5.
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.

P35705-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAGRLFR ASLIRHVSAI PWGISASAAL RPAASRRMCL TNALWSGSDQ
60 70 80 90 100
AKFAFSTSSS YHAPAVTQHA PYFKGTAVVS GEFKEISLDD FKGKYLVLFF
110 120 130 140 150
YPLDFTFVCP TEIIAFSDKA SEFHDVNCEV VAVSVDSHFS HLAWINTPRK
160 170 180 190 200
NGGLGHMNIA LLSDLTKQIS RDYGVLLEGP GLALRGLFII DPNGVIKHLS
210 220 230 240 250
VNDLPVGRSV EETLRLVKAF QFVEAHGEVC PANWTPESPT IKPHPTASRE

YFEKVNQ
Length:257
Mass (Da):28,195
Last modified:November 1, 1997 - v2
Checksum:iF2E89EE2F172A42D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82025 mRNA. Translation: BAA11511.1.
BC103009 mRNA. Translation: AAI03010.1.
PIRiJC2258.
RefSeqiNP_776857.1. NM_174432.2.
UniGeneiBt.103308.
Bt.62827.

Genome annotation databases

EnsembliENSBTAT00000011505; ENSBTAP00000011505; ENSBTAG00000008731.
GeneIDi281998.
KEGGibta:281998.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D82025 mRNA. Translation: BAA11511.1.
BC103009 mRNA. Translation: AAI03010.1.
PIRiJC2258.
RefSeqiNP_776857.1. NM_174432.2.
UniGeneiBt.103308.
Bt.62827.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZYEX-ray3.30A/B/C/D/E/F/G/H/I/J/K/L63-257[»]
4MH2X-ray2.20A/B/C/D/E/F/G/H/I/J/K/L63-257[»]
4MH3X-ray2.40A/B/C/D/E/F/G/H/I/J/K/L63-257[»]
ProteinModelPortaliP35705.
SMRiP35705.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48458N.
STRINGi9913.ENSBTAP00000011505.

Protein family/group databases

PeroxiBasei4502. Bt2CysPrx03.

Proteomic databases

PaxDbiP35705.
PeptideAtlasiP35705.
PRIDEiP35705.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000011505; ENSBTAP00000011505; ENSBTAG00000008731.
GeneIDi281998.
KEGGibta:281998.

Organism-specific databases

CTDi10935.

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP35705.
KOiK20011.
OMAiTQHAPAF.
OrthoDBiEOG091G0IE5.
TreeFamiTF105181.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP35705.

Gene expression databases

BgeeiENSBTAG00000008731.

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_BOVIN
AccessioniPrimary (citable) accession number: P35705
Secondary accession number(s): Q3SZA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 124 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

Caution

It is uncertain whether transit peptide cleavage occurs after His-62 or Ala-63. Peptides have been found for both N-termini in roughly equal amounts.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.