ID   GPX3_MACFU              Reviewed;         226 AA.
AC   Q4AEH4;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   06-MAR-2013, entry version 37.
DE   RecName: Full=Glutathione peroxidase 3;
DE            Short=GPx-3;
DE            Short=GSHPx-3;
DE            EC=1.11.1.9;
DE   AltName: Full=Plasma glutathione peroxidase;
DE            Short=GPx-P;
DE            Short=GSHPx-P;
DE   Flags: Precursor;
GN   Name=GPX3;
OS   Macaca fuscata fuscata (Japanese macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed intensively in the kidney and
CC       adrenal gland, and weakly in the cerebellum, heart, and lung.
CC       Secreted in plasma.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
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DR   EMBL; AB121008; BAE17016.1; -; mRNA.
DR   ProteinModelPortal; Q4AEH4; -.
DR   PeroxiBase; 3706; MfGPx03.
DR   HOVERGEN; HBG004333; -.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR   GO; GO:0008430; F:selenium binding; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   PANTHER; PTHR11592; PTHR11592; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 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       Potential.
FT   CHAIN        25    226       Glutathione peroxidase 3.
FT                                /FTId=PRO_0000042606.
FT   ACT_SITE     73     73       By similarity.
FT   NON_STD      73     73       Selenocysteine.
SQ   SEQUENCE   226 AA;  25576 MW;  CD13D80423FEB17E CRC64;
     MARLLQASCL LSLLLAGFLP QSRGQDKSKM DCHGGVSGTI YEYGALTIDG EEYIPFKQYI
     GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVLLGFP CNQFGKQEPG ENSEILPSLK
     YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR
     WNFEKFLVGP DGIPVMRWHH RTTISNVKMD ILSYMRRQAA LGVKRK
//