ID   GPX3_HYLLA              Reviewed;         226 AA.
AC   Q4AEH5;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   23-FEB-2022, entry version 56.
DE   RecName: Full=Glutathione peroxidase 3 {ECO:0000250|UniProtKB:P22352};
DE            Short=GPx-3;
DE            Short=GSHPx-3;
DE            EC=1.11.1.9 {ECO:0000250|UniProtKB:P22352};
DE   AltName: Full=Plasma glutathione peroxidase;
DE            Short=GPx-P;
DE            Short=GSHPx-P;
DE   Flags: Precursor;
GN   Name=GPX3 {ECO:0000250|UniProtKB:P22352};
OS   Hylobates lar (Common gibbon) (White-handed gibbon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Hylobates.
OX   NCBI_TaxID=9580;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15967696; DOI=10.1016/j.cbpc.2005.05.002;
RA   Fukuhara R., Kageyama T.;
RT   "Structure, gene expression, and evolution of primate glutathione
RT   peroxidases.";
RL   Comp. Biochem. Physiol. 141B:428-436(2005).
CC   -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC       catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC       organic hydroperoxide, by glutathione. {ECO:0000250|UniProtKB:P22352}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC         Evidence={ECO:0000250|UniProtKB:P22352};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + tert-butyl hydroperoxide = glutathione
CC         disulfide + H2O + tert-butanol; Xref=Rhea:RHEA:69412,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:45895, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58297, ChEBI:CHEBI:64090;
CC         Evidence={ECO:0000250|UniProtKB:P22352};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Secreted in plasma.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AB121007; BAE17015.1; -; mRNA.
DR   PeroxiBase; 3698; HlGPx03.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0008430; F:selenium binding; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase; Peroxidase; Secreted; Selenocysteine; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..226
FT                   /note="Glutathione peroxidase 3"
FT                   /id="PRO_0000042605"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
FT   NON_STD         73
FT                   /note="Selenocysteine"
SQ   SEQUENCE   226 AA;  25598 MW;  6CAF43D76B9BF681 CRC64;
     MARLLQASCL LSLLLAGFVP QSRGQEKSKM DCHGGMSSTI YEYGALTIDG EEYIPFKQYA
     GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVILGFP CNQFGKQEPG ENSEILPTLK
     YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR
     WNFEKFLVGP DGTPIMRWHH RTTVSNVKMD ILSYMRRQAA LGVKRK