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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

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.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei109Cysteine sulfenic acid (-SOH) intermediate1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntioxidant, 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

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 – 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 formCombined sources1 Publication
Disulfide bondi230Interchain (with C-109); in linked formCombined sources1 Publication

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

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

Homodimer; disulfide-linked, upon oxidation. 6 homodimers assemble to form a ring-like dodecamer (PubMed:16271889, PubMed:25906064). Interacts with NEK6 (By similarity). Interacts with LRRK2 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-15559045,EBI-15559045

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: Ensembl
  • protein kinase binding Source: Ensembl

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

Keywords - Domaini

Redox-active center, Transit peptide

Phylogenomic databases

eggNOGiKOG0852. Eukaryota.
COG0450. LUCA.
GeneTreeiENSGT00390000004653.
HOGENOMiHOG000022343.
HOVERGENiHBG000286.
InParanoidiP35705.
KOiK20011.
OMAiTAVHNGE.
OrthoDBiEOG091G0IE5.
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.

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.

Similar proteinsi

Entry informationi

Entry nameiPRDX3_BOVIN
AccessioniPrimary (citable) accession number: P35705
Secondary accession number(s): Q3SZA8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: October 25, 2017
This is version 131 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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