PRDX4_BOVIN
ID PRDX4_BOVIN Reviewed; 274 AA.
AC Q9BGI2; Q32L06;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peroxiredoxin-4;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q13162};
DE AltName: Full=Peroxiredoxin IV;
DE Short=Prx-IV;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 4 {ECO:0000305};
DE Flags: Precursor;
GN Name=PRDX4;
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].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-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. Regulates the activation of NF-kappa-B in the cytosol
CC by a modulation of I-kappa-B-alpha phosphorylation.
CC {ECO:0000250|UniProtKB:Q13162}.
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:Q13162};
CC -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
CC assemble to form a ring-like decamer. {ECO:0000250|UniProtKB:Q13162}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13162}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13162}.
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:Q13162}.
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:Q13162}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF305563; AAG53660.1; -; mRNA.
DR EMBL; BC109824; AAI09825.1; -; mRNA.
DR RefSeq; NP_776858.1; NM_174433.2.
DR AlphaFoldDB; Q9BGI2; -.
DR SMR; Q9BGI2; -.
DR BioGRID; 159288; 1.
DR STRING; 9913.ENSBTAP00000008107; -.
DR PeroxiBase; 4531; Bt2CysPrx04.
DR PaxDb; Q9BGI2; -.
DR PeptideAtlas; Q9BGI2; -.
DR PRIDE; Q9BGI2; -.
DR GeneID; 281999; -.
DR KEGG; bta:281999; -.
DR CTD; 10549; -.
DR eggNOG; KOG0852; Eukaryota.
DR HOGENOM; CLU_042529_21_1_1; -.
DR InParanoid; Q9BGI2; -.
DR OrthoDB; 1326484at2759; -.
DR TreeFam; TF105181; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
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 Antioxidant; Cytoplasm; Disulfide bond; Endoplasmic reticulum;
KW Oxidoreductase; Peroxidase; Redox-active center; Reference proteome;
KW Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000250"
FT CHAIN 41..274
FT /note="Peroxiredoxin-4"
FT /id="PRO_0000135097"
FT DOMAIN 82..240
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 127
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q13162"
FT DISULFID 127
FT /note="Interchain (with C-248); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q13162"
FT DISULFID 248
FT /note="Interchain (with C-127); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q13162"
SQ SEQUENCE 274 AA; 30741 MW; AE14176CF1C70E37 CRC64;
MEAPPPPPPL PATTLAPGRS RKLLLLPLLL FLLRAEAVRG FEAEERPRTR EEECHFYAGG
QVYPGEVSRV SVAEHSLHLS KAKISKPAPY WEGTAVINGE FKELKLTDYR GKYLVFFFYP
LDFTFVCPTE IIAFGDRIDE FRSINTEVVA CSVDSQFTHL AWINTPRRQG GLGSINIPLL
ADLNHQISKD YGVYLEDSGH TLRGLFIIDD KGILRQITLN DLPVGRSVDE TLRLVQAFQY
TDKHGEVCPA GWKPGSETII PDPAGKLKYF DKLN
