ID   PRDX4_CROAT             Reviewed;          36 AA.
AC   P0CV91;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Peroxiredoxin-4;
DE            EC=1.11.1.24 {ECO:0000250|UniProtKB:Q13162};
DE   AltName: Full=Thioredoxin-dependent peroxiredoxin 4 {ECO:0000305};
DE   Flags: Fragments;
OS   Crotalus atrox (Western diamondback rattlesnake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Crotalus.
OX   NCBI_TaxID=8730;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=19371136; DOI=10.1021/pr900249q;
RA   Calvete J.J., Fasoli E., Sanz L., Boschetti E., Righetti P.G.;
RT   "Exploring the venom proteome of the western diamondback rattlesnake,
RT   Crotalus atrox, via snake venomics and combinatorial peptide ligand library
RT   approaches.";
RL   J. Proteome Res. 8:3055-3067(2009).
CC   -!- FUNCTION: Venom peroxiredoxin enzyme that may play a role as part of a
CC       redox pathway leading to the structural/functional diversification of
CC       toxins through a disulfide bond engineering mechanism.
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.
CC       {ECO:0000250|UniProtKB:Q13162}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19371136}.
CC   -!- TISSUE SPECIFICITY: Venom gland.
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   AlphaFoldDB; P0CV91; -.
DR   SMR; P0CV91; -.
DR   PRIDE; P0CV91; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   1: Evidence at protein level;
KW   Antioxidant; Direct protein sequencing; Oxidoreductase; Peroxidase;
KW   Redox-active center; Secreted.
FT   CHAIN           <1..>36
FT                   /note="Peroxiredoxin-4"
FT                   /id="PRO_0000407591"
FT   NON_CONS        8..9
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         36
SQ   SEQUENCE   36 AA;  4141 MW;  91762F6756A07C50 CRC64;
     GLFIIDDKQI TMNDLPVGRS VDETLRLVQA FQYTDK