PRDX5_PAPHA
ID PRDX5_PAPHA Reviewed; 215 AA.
AC Q9GLW9;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Peroxiredoxin-5, mitochondrial;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:P30044};
DE AltName: Full=Peroxiredoxin V;
DE Short=Prx-V;
DE AltName: Full=Thioredoxin peroxidase;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRDX5;
OS Papio hamadryas (Hamadryas baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9557;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Knoops B., Cherif H.;
RT "Cloning and characterization of baboon AOEB166/PRDX5.";
RL Submitted (SEP-2000) 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 and as sensor of hydrogen peroxide-mediated
CC signaling events. {ECO:0000250|UniProtKB:P30044}.
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=Q9GLW9-1; Sequence=Displayed;
CC Name=Cytoplasmic+peroxisomal;
CC IsoId=Q9GLW9-2; Sequence=VSP_018831;
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; AF110734; AAG13451.2; -; mRNA.
DR AlphaFoldDB; Q9GLW9; -.
DR SMR; Q9GLW9; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Acetylation; Alternative initiation; Antioxidant; Cytoplasm;
KW Disulfide bond; Lipoprotein; Mitochondrion; Oxidoreductase; Palmitate;
KW Peroxidase; Peroxisome; Phosphoprotein; Redox-active center;
KW Transit peptide.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 54..215
FT /note="Peroxiredoxin-5, mitochondrial"
FT /id="PRO_0000023797"
FT DOMAIN 57..215
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 213..215
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT ACT_SITE 101
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT MOD_RES 76
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 84
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT MOD_RES 84
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 117
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R063"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT LIPID 101
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT DISULFID 101..205
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform Cytoplasmic+peroxisomal)"
FT /evidence="ECO:0000305"
FT /id="VSP_018831"
SQ SEQUENCE 215 AA; 22166 MW; 65183A24535C1617 CRC64;
MGLAGVCVLR RSAGYILGGA AGQSVAATAA ARRRSEGGWA SGGVRSFSRA AAAMAPIKVG
DAIPAVEVFE GEPGNKVNLA ELFKGKKGVL FGVPGAFTPG CSKTHLPGFV EQAEALKAKG
VQVLACLSVN DAFVTGEWGR AHKVEGKVRL LADPTGAFGK ETDLLLDDSL VSIFGNRRLK
RFSMVVQDGI VKALNVEPDG TGLTCSLAPS IISQL
