PRDX5_BOVIN
ID PRDX5_BOVIN Reviewed; 219 AA.
AC Q9BGI1; Q3SZ78;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Leyens G., Donnay I., Knoops B.;
RT "Cloning of 4 new bovine peroxiredoxins, and screening of the complete
RT peroxiredoxin family in different bovine tissues.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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=Q9BGI1-1; Sequence=Displayed;
CC Name=Cytoplasmic+peroxisomal;
CC IsoId=Q9BGI1-2; Sequence=VSP_018827;
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; AF305564; AAG53661.1; -; mRNA.
DR EMBL; BC103073; AAI03074.1; -; mRNA.
DR RefSeq; NP_777174.1; NM_174749.2.
DR AlphaFoldDB; Q9BGI1; -.
DR SMR; Q9BGI1; -.
DR STRING; 9913.ENSBTAP00000011403; -.
DR PeroxiBase; 4451; BtPrxV.
DR PaxDb; Q9BGI1; -.
DR PeptideAtlas; Q9BGI1; -.
DR PRIDE; Q9BGI1; -.
DR Ensembl; ENSBTAT00000011403; ENSBTAP00000011403; ENSBTAG00000008648. [Q9BGI1-1]
DR GeneID; 282885; -.
DR KEGG; bta:282885; -.
DR CTD; 25824; -.
DR VEuPathDB; HostDB:ENSBTAG00000008648; -.
DR eggNOG; KOG0541; Eukaryota.
DR GeneTree; ENSGT00390000018173; -.
DR HOGENOM; CLU_072440_3_1_1; -.
DR InParanoid; Q9BGI1; -.
DR OMA; GYINHPK; -.
DR OrthoDB; 1281610at2759; -.
DR TreeFam; TF105182; -.
DR Reactome; R-BTA-3299685; Detoxification of Reactive Oxygen Species.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000008648; Expressed in ruminant reticulum and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005782; C:peroxisomal matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0001016; F:RNA polymerase III transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
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; IEA:Ensembl.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IEA:Ensembl.
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 Reference proteome; Transit peptide.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 58..219
FT /note="Peroxiredoxin-5, mitochondrial"
FT /id="PRO_0000023788"
FT DOMAIN 61..219
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 217..219
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT ACT_SITE 105
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT MOD_RES 80
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 88
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT MOD_RES 88
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P99029"
FT LIPID 105
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P30044"
FT DISULFID 105..209
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform Cytoplasmic+peroxisomal)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_018827"
FT CONFLICT 76
FT /note="E -> G (in Ref. 1; AAG53661)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="A -> T (in Ref. 1; AAG53661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 23253 MW; B508132695B4B261 CRC64;
MRLGWLRVLG CRPGSVVSRA TIVEGASTTA AGTRGCLEGI LEWTFGGVRG FRSAAVAMAP
IKVGDAIPSV EVFEKEPGNK VNLAELFKGK KGVLFGLPGA FTPGCSKTHL PGFVEQADAL
KAKGIQVVAC LTVNDVFVTE EWARAHKAEG KVRLLADPSG TFGKETDLLL DDSLLFLFGN
HRLKRFSMVI EDGIVKSLNV EPDGTGLTCS LAPNILSQL
