ID   GPX3_PONPY              Reviewed;         226 AA.
AC   Q5RFG3;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   29-OCT-2014, entry version 56.
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   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9600;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CATALYTIC ACTIVITY: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Secreted in plasma.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AB121006; BAE17014.1; -; mRNA.
DR   EMBL; CR857195; CAH89494.2; -; mRNA.
DR   ProteinModelPortal; Q5RFG3; -.
DR   STRING; 9600.ENSPPYP00000017858; -.
DR   PeroxiBase; 3727; PpyGPx03.
DR   eggNOG; COG0386; -.
DR   HOGENOM; HOG000277055; -.
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; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
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; 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       {ECO:0000255}.
FT   CHAIN        25    226       Glutathione peroxidase 3.
FT                                /FTId=PRO_0000042615.
FT   ACT_SITE     73     73       {ECO:0000250}.
FT   NON_STD      73     73       Selenocysteine.
SQ   SEQUENCE   226 AA;  25562 MW;  D7F77A1692493D98 CRC64;
     MARLLQASCL LSLLLAGFVP QSRGQEKSKM DCHGGISGTI YEYGALTIDG EEYIPFKQYA
     GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVILGFP CNQFGKQEPG ENSEILPTLK
     YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR
     WNFEKFLVGP DGIPIMRWHH RTTVSNVKMD ILSYMRRQAA LGVKRK
//