PRDX5_RAT
ID PRDX5_RAT Reviewed; 213 AA.
AC Q9R063; Q68G22;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Peroxiredoxin-5, mitochondrial;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30044};
DE AltName: Full=Antioxidant enzyme B166;
DE Short=AOEB166;
DE AltName: Full=PLP;
DE AltName: Full=Peroxiredoxin V;
DE Short=Prx-V;
DE AltName: Full=Peroxisomal antioxidant enzyme;
DE AltName: Full=Thioredoxin peroxidase PMP20;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=Prdx5 {ECO:0000312|RGD:71007};
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 FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10521424; DOI=10.1074/jbc.274.43.30451;
RA Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C.,
RA Duconseille E., Falmagne P., Bernard A.;
RT "Cloning and characterization of AOEB166, a novel mammalian antioxidant
RT enzyme of the peroxiredoxin family.";
RL J. Biol. Chem. 274:30451-30458(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-130.
RC TISSUE=Heart;
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 75-82; 86-115 AND 159-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000269|PubMed:10521424}.
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:P30044};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P30044}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC {ECO:0000250|UniProtKB:P30044}.
CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic+peroxisomal]: Cytoplasm
CC {ECO:0000250|UniProtKB:P30044}. Peroxisome matrix
CC {ECO:0000250|UniProtKB:P30044}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=Q9R063-1; Sequence=Displayed;
CC Name=Cytoplasmic+peroxisomal;
CC IsoId=Q9R063-2; Sequence=VSP_018832;
CC -!- PTM: S-palmitoylated. Palmitoylation occurs on the active site,
CC inhibiting its reactivity; therefore PRDX5 palmitoylation status
CC determines its antioxidant capacity. {ECO:0000250|UniProtKB:P30044}.
CC -!- PTM: [Isoform Mitochondrial]: S-palmitoylated. Depalmitoylated by
CC ABHD10. {ECO:0000250|UniProtKB:P30044}.
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 atypical 2-Cys
CC Prx, C(R) is present in the same subunit to form an intramolecular
CC disulfide. The disulfide is subsequently reduced by thioredoxin.
CC {ECO:0000250|UniProtKB:P30044}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF110732; AAF03751.1; -; mRNA.
DR EMBL; BC078771; AAH78771.1; -; mRNA.
DR RefSeq; NP_446062.1; NM_053610.1. [Q9R063-1]
DR AlphaFoldDB; Q9R063; -.
DR SMR; Q9R063; -.
DR BioGRID; 250207; 2.
DR IntAct; Q9R063; 3.
DR MINT; Q9R063; -.
DR STRING; 10116.ENSRNOP00000028687; -.
DR PeroxiBase; 4452; RnoPrxV.
DR iPTMnet; Q9R063; -.
DR PhosphoSitePlus; Q9R063; -.
DR SwissPalm; Q9R063; -.
DR jPOST; Q9R063; -.
DR PaxDb; Q9R063; -.
DR PRIDE; Q9R063; -.
DR GeneID; 113898; -.
DR KEGG; rno:113898; -.
DR UCSC; RGD:71007; rat. [Q9R063-1]
DR CTD; 25824; -.
DR RGD; 71007; Prdx5.
DR eggNOG; KOG0541; Eukaryota.
DR InParanoid; Q9R063; -.
DR OrthoDB; 1281610at2759; -.
DR PhylomeDB; Q9R063; -.
DR TreeFam; TF105182; -.
DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR PRO; PR:Q9R063; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0004601; F:peroxidase activity; ISO:RGD.
DR GO; GO:0001016; F:RNA polymerase III transcription regulatory region sequence-specific DNA 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; IBA:GO_Central.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR CDD; cd03013; PRX5_like; 1.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10430; PTHR10430; 1.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Antioxidant; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Lipoprotein; Mitochondrion;
KW Oxidoreductase; Palmitate; Peroxidase; Peroxisome; Phosphoprotein;
KW Redox-active center; Reference proteome; Transit peptide.
FT TRANSIT 1..51
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 52..213
FT /note="Peroxiredoxin-5, mitochondrial"
FT /id="PRO_0000023799"
FT DOMAIN 55..213
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 211..213
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT ACT_SITE 99
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT MOD_RES 74
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 82
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT MOD_RES 82
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 115
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT LIPID 99
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT DISULFID 99..203
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 1..51
FT /note="Missing (in isoform Cytoplasmic+peroxisomal)"
FT /evidence="ECO:0000305"
FT /id="VSP_018832"
FT VARIANT 68
FT /note="E -> G"
FT VARIANT 114
FT /note="L -> P"
FT VARIANT 130
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:15489334"
SQ SEQUENCE 213 AA; 22179 MW; 9F0D03A4CC87708A CRC64;
MVQLRFCVLG SIAGSVLRAS ATWTCVAGRA GRKGAGWECG GARSFSSAAV TMAPIKVGDT
IPSVEVFEGE PGKKVNLAEL FKDKKGVLFG VPGAFTPGCS KTHLPGFVEQ AGALKAKGAQ
VVACLSVNDA FVTAEWGRAH QAEGKVQLLA DPTGAFGKET DLLLDDSLVS LFGNRRLKRF
SMVIDKGVVK ALNVEPDGTG LTCSLAPNIL SQL
