ID   GPX3_BOVIN              Reviewed;         226 AA.
AC   P37141; A6QPD6;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 127.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   PubMed=8262911; DOI=10.1093/oxfordjournals.jbchem.a124168;
RA   Martin-Alonso J.M., Ghosh S., Coca-Prados M.;
RT   "Cloning of the bovine plasma selenium-dependent glutathione peroxidase
RT   (GP) cDNA from the ocular ciliary epithelium: expression of the plasma and
RT   cellular forms within the mammalian eye.";
RL   J. Biochem. 114:284-291(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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|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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L10325; AAA16579.2; -; mRNA.
DR   EMBL; BC149266; AAI49267.1; -; mRNA.
DR   PIR; JX0280; JX0280.
DR   RefSeq; NP_776502.1; NM_174077.4.
DR   STRING; 9913.ENSBTAP00000053146; -.
DR   PeroxiBase; 3636; BtGPx03.
DR   PaxDb; P37141; -.
DR   PRIDE; P37141; -.
DR   Ensembl; ENSBTAT00000060554; ENSBTAP00000053146; ENSBTAG00000043553.
DR   GeneID; 281210; -.
DR   KEGG; bta:281210; -.
DR   CTD; 2878; -.
DR   VEuPathDB; HostDB:ENSBTAG00000043553; -.
DR   VGNC; VGNC:29619; GPX3.
DR   eggNOG; KOG1651; Eukaryota.
DR   GeneTree; ENSGT00940000161754; -.
DR   InParanoid; P37141; -.
DR   OMA; KTDCHAG; -.
DR   OrthoDB; 1483113at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000043553; Expressed in metanephros cortex and 103 other tissues.
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:0004601; F:peroxidase activity; IBA:GO_Central.
DR   GO; GO:0008430; F:selenium binding; ISS:UniProtKB.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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; 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_0000013061"
FT   ACT_SITE        73
FT   NON_STD         73
FT                   /note="Selenocysteine"
FT   CONFLICT        169
FT                   /note="L -> H (in Ref. 2; AAI49267)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   226 AA;  25663 MW;  6357FCED08507923 CRC64;
     MARLFRASCL LSLLLAGFIP PSQGQEKSKT DCHAGVGGTI YEYGALTIDG EEYIPFKQYA
     GKYILFVNVA SYUGLTGQYV ELNALQEELE PFGLVILGFP CNQFGKQEPG ENSEILATLK
     YVRPGGGFTP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGSPDRLF WEPMKVHDIR
     WNFEKFLVGP DGIPIMRWYH RTTVNSVKMD ILTYMRRRAV WEAKGK