ID   GPX3_RAT                Reviewed;         226 AA.
AC   P23764; Q6P6H2;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   23-FEB-2022, entry version 139.
DE   RecName: Full=Glutathione peroxidase 3 {ECO:0000305};
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:0000312|RGD:69224};
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].
RC   TISSUE=Kidney;
RX   PubMed=1939013; DOI=10.1093/oxfordjournals.jbchem.a123480;
RA   Yoshimura S., Watanabe K., Suemizu H., Onozawa T., Mizoguchi J., Tsuda K.,
RA   Hatta H., Moriuchi T.;
RT   "Tissue specific expression of the plasma glutathione peroxidase gene in
RT   rat kidney.";
RL   J. Biochem. 109:918-923(1991).
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).
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.
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; D00680; BAA00587.2; -; mRNA.
DR   EMBL; BC062227; AAH62227.1; -; mRNA.
DR   PIR; JX0176; JX0176.
DR   RefSeq; NP_071970.2; NM_022525.4.
DR   PeroxiBase; 3732; RnoGPx03.
DR   iPTMnet; P23764; -.
DR   PhosphoSitePlus; P23764; -.
DR   PRIDE; P23764; -.
DR   GeneID; 64317; -.
DR   KEGG; rno:64317; -.
DR   UCSC; RGD:69224; rat.
DR   CTD; 2878; -.
DR   RGD; 69224; Gpx3.
DR   InParanoid; P23764; -.
DR   OrthoDB; 1483113at2759; -.
DR   PhylomeDB; P23764; -.
DR   Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:P23764; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0008430; F:selenium binding; IDA:RGD.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:RGD.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:RGD.
DR   GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
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; Reference proteome; Secreted; Selenocysteine;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..226
FT                   /note="Glutathione peroxidase 3"
FT                   /id="PRO_0000013064"
FT   ACT_SITE        73
FT   NON_STD         73
FT                   /note="Selenocysteine"
FT   CONFLICT        2
FT                   /note="A -> S (in Ref. 1; BAA00587)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  25424 MW;  414BF56F8F553F88 CRC64;
     MARILRASCL LSLLLAGFVP PGRGQEKSKT DCHGGMSGTI YEYGALTIDG EEYIPFKQYA
     GKYILFVNVA SYUGLTDQYL ELNALQEELG PFGLVILGFP CNQFGKQEPG ENSEILPSLK
     YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTA ELLGSPGRLF WEPMKIHDIR
     WNFEKFLVGP DGIPIMRWYH RTTVSNVKMD ILSYMRRQAA LGARGK