PRDX4_RAT
ID PRDX4_RAT Reviewed; 273 AA.
AC Q9Z0V5;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Peroxiredoxin-4;
DE EC=1.11.1.24 {ECO:0000250|UniProtKB:Q13162};
DE AltName: Full=Antioxidant enzyme AOE372;
DE AltName: Full=Peroxiredoxin IV;
DE Short=Prx-IV;
DE AltName: Full=Thioredoxin peroxidase AO372;
DE AltName: Full=Thioredoxin-dependent peroxide reductase A0372;
DE AltName: Full=Thioredoxin-dependent peroxiredoxin 4 {ECO:0000305};
DE Flags: Precursor;
GN Name=Prdx4; Synonyms=Rno2CysPrx04;
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 SUBCELLULAR LOCATION.
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].
RC TISSUE=Pituitary;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10731722; DOI=10.1093/oxfordjournals.jbchem.a022632;
RA Okado-Matsumoto A., Matsumoto A., Fujii J., Taniguchi N.;
RT "Peroxiredoxin IV is a secretable protein with heparin-binding properties
RT under reduced conditions.";
RL J. Biochem. 127:493-501(2000).
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}. Secreted
CC {ECO:0000269|PubMed:10025941, ECO:0000269|PubMed:10731722}.
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; AF106945; AAD17993.1; -; mRNA.
DR EMBL; BC059122; AAH59122.1; -; mRNA.
DR RefSeq; NP_445964.1; NM_053512.2.
DR AlphaFoldDB; Q9Z0V5; -.
DR SMR; Q9Z0V5; -.
DR IntAct; Q9Z0V5; 2.
DR STRING; 10116.ENSRNOP00000005014; -.
DR PeroxiBase; 4533; Rno2CysPrx04.
DR CarbonylDB; Q9Z0V5; -.
DR iPTMnet; Q9Z0V5; -.
DR PhosphoSitePlus; Q9Z0V5; -.
DR jPOST; Q9Z0V5; -.
DR PaxDb; Q9Z0V5; -.
DR PRIDE; Q9Z0V5; -.
DR GeneID; 85274; -.
DR KEGG; rno:85274; -.
DR CTD; 10549; -.
DR RGD; 620043; Prdx4.
DR VEuPathDB; HostDB:ENSRNOG00000003763; -.
DR eggNOG; KOG0852; Eukaryota.
DR HOGENOM; CLU_042529_21_1_1; -.
DR InParanoid; Q9Z0V5; -.
DR OMA; EDSESCY; -.
DR OrthoDB; 1326484at2759; -.
DR PhylomeDB; Q9Z0V5; -.
DR TreeFam; TF105181; -.
DR BRENDA; 1.11.1.24; 5301.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9Z0V5; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000003763; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q9Z0V5; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; ISO:RGD.
DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; ISO:RGD.
DR GO; GO:0018401; P:peptidyl-proline hydroxylation to 4-hydroxy-L-proline; ISO:RGD.
DR GO; GO:0022417; P:protein maturation by protein folding; ISO:RGD.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; 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 2: Evidence at transcript level;
KW Antioxidant; Cytoplasm; Disulfide bond; Endoplasmic reticulum;
KW Oxidoreductase; Peroxidase; Redox-active center; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000250"
FT CHAIN 41..273
FT /note="Peroxiredoxin-4"
FT /id="PRO_0000390877"
FT DOMAIN 81..239
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 126
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q13162"
FT DISULFID 126
FT /note="Interchain (with C-247); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q13162"
FT DISULFID 247
FT /note="Interchain (with C-126); in linked form"
FT /evidence="ECO:0000250|UniProtKB:Q13162"
SQ SEQUENCE 273 AA; 31007 MW; 09E614794F1DC6C2 CRC64;
METWSKLLDG TTPSRRWRKL VLLLPPLLLF LLQTEALQGL ESDDRFRTRE NECHFYAGGQ
VYPGEVSRVS VADHSLHLSK AKISKPAPYW EGTAVINGEF KELKLTDYRG KYLVFFFYPL
DFTFVCPTEI IAFGDRIEEF KSINTEVVAC SVDSQFTHLA WINTPRRQGG LGPIRIPLLS
DLNHQISKDY GVYLEDSGHT LRGLFIIDDK GVLRQITLND LPVGRSVDET LRLVQAFQYT
DKHGEVCPAG WKPGSETIIP DPAGKLKYFD KLN
