PRDX3_RAT
ID PRDX3_RAT Reviewed; 257 AA.
AC Q9Z0V6; Q6P9W3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30048};
DE AltName: Full=PRx III;
DE AltName: Full=Peroxiredoxin-3;
DE Short=PRX-3;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 3 {ECO:0000305};
DE Flags: Precursor;
GN Name=Prdx3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10025941; DOI=10.1016/s0014-5793(98)01736-0;
RA Matsumoto A., Okado A., Fujii T., Fujii J., Egashira M., Niikawa N.,
RA Taniguchi N.;
RT "Cloning of the peroxiredoxin gene family in rats and characterization of
RT the fourth member.";
RL FEBS Lett. 443:246-250(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 171-208; 172-197 AND 209-239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
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 -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10025941}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF106944; AAD17992.1; -; mRNA.
DR EMBL; BC060567; AAH60567.1; -; mRNA.
DR RefSeq; NP_071985.1; NM_022540.1.
DR AlphaFoldDB; Q9Z0V6; -.
DR SMR; Q9Z0V6; -.
DR BioGRID; 249055; 1.
DR IntAct; Q9Z0V6; 3.
DR MINT; Q9Z0V6; -.
DR STRING; 10116.ENSRNOP00000015186; -.
DR PeroxiBase; 4507; Rno2CysPrx03.
DR iPTMnet; Q9Z0V6; -.
DR PhosphoSitePlus; Q9Z0V6; -.
DR World-2DPAGE; 0004:Q9Z0V6; -.
DR jPOST; Q9Z0V6; -.
DR PaxDb; Q9Z0V6; -.
DR PRIDE; Q9Z0V6; -.
DR GeneID; 64371; -.
DR KEGG; rno:64371; -.
DR CTD; 10935; -.
DR RGD; 620040; Prdx3.
DR eggNOG; KOG0852; Eukaryota.
DR InParanoid; Q9Z0V6; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; Q9Z0V6; -.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR PRO; PR:Q9Z0V6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:RGD.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:RGD.
DR GO; GO:0001893; P:maternal placenta development; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0030099; P:myeloid cell differentiation; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0033673; P:negative regulation of kinase activity; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0018171; P:peptidyl-cysteine oxidation; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Endosome; Lipoprotein; Mitochondrion; Oxidoreductase;
KW Palmitate; Peroxidase; Phosphoprotein; Redox-active center;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..62
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P30048"
FT CHAIN 63..257
FT /note="Thioredoxin-dependent peroxide reductase,
FT mitochondrial"
FT /id="PRO_0000256859"
FT DOMAIN 64..222
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 109
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P35705"
FT MOD_RES 84
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20108"
FT MOD_RES 92
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30048"
FT MOD_RES 92
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20108"
FT MOD_RES 147
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30048"
FT DISULFID 109
FT /note="Interchain (with C-230); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P35705"
FT DISULFID 230
FT /note="Interchain (with C-109); in linked form"
FT /evidence="ECO:0000250|UniProtKB:P35705"
FT CONFLICT 207..216
FT /note="Missing (in Ref. 2; AAH60567)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="A -> P (in Ref. 1; AAD17992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 28295 MW; 752198F5918206AE CRC64;
MAAAAGRLLW SSVARPASTI FRSISASTVL RPVASRRTCL TDMLWSACPQ AKFAFSTSSS
FHTPAVTQHA PHFKGTAVVN GEFKELSLDD FKGKYLVLFF YPLDFTFVCP TEIVAFSDKA
NEFHDVNCEV VAVSVDSHFS HLAWINTPRK NGGLGHMNIT LLSDLTKQIS RDYGVLLESA
GIALRGLFII DPNGVIKHLS VNDLPVGRSV EEPLRLVKAF QFVETHGEVC PANWTPESPT
IKPSPTASKE YFEKVHQ
