PRDX3_PONAB
ID PRDX3_PONAB Reviewed; 256 AA.
AC Q5REY3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30048};
DE AltName: Full=Peroxiredoxin-3;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 3 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRDX3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000250|UniProtKB:P30048}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-
CC disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
CC ChEBI:CHEBI:50058; EC=1.11.1.24;
CC Evidence={ECO:0000250|UniProtKB:P30048};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 6 homodimers
CC assemble to form a ring-like dodecamer. Interacts with NEK6. Interacts
CC with LRRK2. Interacts with RPS6KC1 (via PX domain).
CC {ECO:0000250|UniProtKB:P30048}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P35705}.
CC Cytoplasm {ECO:0000250|UniProtKB:P30048}. Early endosome
CC {ECO:0000250|UniProtKB:P30048}. Note=Localizes to early endosomes in a
CC RPS6KC1-dependent manner. {ECO:0000250|UniProtKB:P30048}.
CC -!- PTM: Phosphorylated by LRRK2; phosphorylation reduces perodixase
CC activity. {ECO:0000250|UniProtKB:P30048}.
CC -!- PTM: The enzyme can be inactivated by further oxidation of the cysteine
CC sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) and sulphonic
CC acid (C(P)-SO3H) instead of its condensation to a disulfide bond.
CC {ECO:0000250|UniProtKB:P30048}.
CC -!- PTM: S-palmitoylated. {ECO:0000250|UniProtKB:P20108}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this typical 2-Cys
CC peroxiredoxin, C(R) is provided by the other dimeric subunit to form an
CC intersubunit disulfide. The disulfide is subsequently reduced by
CC thioredoxin. {ECO:0000250|UniProtKB:P30048}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR857380; CAH89674.1; -; mRNA.
DR RefSeq; NP_001127184.1; NM_001133712.2.
DR AlphaFoldDB; Q5REY3; -.
DR SMR; Q5REY3; -.
DR STRING; 9601.ENSPPYP00000003152; -.
DR PeroxiBase; 4500; Pabe2CysPrx03.
DR PRIDE; Q5REY3; -.
DR Ensembl; ENSPPYT00000003258; ENSPPYP00000003152; ENSPPYG00000002700.
DR GeneID; 100174238; -.
DR KEGG; pon:100174238; -.
DR CTD; 10935; -.
DR eggNOG; KOG0852; Eukaryota.
DR GeneTree; ENSGT00940000153430; -.
DR HOGENOM; CLU_042529_21_0_1; -.
DR InParanoid; Q5REY3; -.
DR OMA; WWPKDFT; -.
DR OrthoDB; 1326484at2759; -.
DR TreeFam; TF105181; -.
DR Proteomes; UP000001595; Chromosome 10.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Antioxidant; Cytoplasm; Disulfide bond; Endosome; Lipoprotein;
KW Mitochondrion; Oxidoreductase; Palmitate; Peroxidase; Phosphoprotein;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P30048"
FT CHAIN 62..256
FT /note="Thioredoxin-dependent peroxide reductase,
FT mitochondrial"
FT /id="PRO_0000256858"
FT DOMAIN 63..221
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 108
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P35705"
FT MOD_RES 83
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20108"
FT MOD_RES 91
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30048"
FT MOD_RES 91
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20108"
FT MOD_RES 146
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30048"
FT DISULFID 108
FT /note="Interchain (with C-229); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P35705"
FT DISULFID 229
FT /note="Interchain (with C-108); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P35705"
SQ SEQUENCE 256 AA; 27700 MW; BF425B99C7794406 CRC64;
MAAAVGRLLR ASVARGVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ AKLFSTSSSY
HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY PLDFTFVCPT EIVAFSDKAN
EFHDVNCEVV AVSVDSHFSH LAWINTPRKN GGLGHMNIAL LSDLTKQISR DYGVLLEGSG
LALRGLFIID PNGVIKHLSV NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI
KPNPAASKEY FQKVNQ
