ID   GPX6_RAT                Reviewed;         221 AA.
AC   Q64625;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Glutathione peroxidase 6;
DE            Short=GPx-6;
DE            Short=GSHPx-6;
DE            EC=1.11.1.9;
DE   AltName: Full=Odorant-metabolizing protein RY2D1;
DE   Flags: Precursor;
GN   Name=Gpx6;
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=Olfactory epithelium;
RX   PubMed=1931961; DOI=10.1021/bi00107a003;
RA   Dear T.N., Campbell K., Rabbitts T.H.;
RT   "Molecular cloning of putative odorant-binding and odorant-metabolizing
RT   proteins.";
RL   Biochemistry 30:10376-10382(1991).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in the Bowman glands.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; M76733; AAA42094.1; -; mRNA.
DR   PIR; B40464; B40464.
DR   RefSeq; NP_671694.1; NM_147165.1.
DR   AlphaFoldDB; Q64625; -.
DR   SMR; Q64625; -.
DR   STRING; 10116.ENSRNOP00000055070; -.
DR   PeroxiBase; 3736; RnoGPx06.
DR   PaxDb; Q64625; -.
DR   PRIDE; Q64625; -.
DR   Ensembl; ENSRNOT00000082782; ENSRNOP00000070342; ENSRNOG00000060749.
DR   GeneID; 259233; -.
DR   KEGG; rno:259233; -.
DR   UCSC; RGD:628789; rat.
DR   CTD; 257202; -.
DR   RGD; 628789; Gpx6.
DR   eggNOG; KOG1651; Eukaryota.
DR   GeneTree; ENSGT00940000161098; -.
DR   InParanoid; Q64625; -.
DR   OrthoDB; 1483113at2759; -.
DR   PhylomeDB; Q64625; -.
DR   Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
DR   PRO; PR:Q64625; -.
DR   Proteomes; UP000002494; Chromosome 17.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; 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; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..221
FT                   /note="Glutathione peroxidase 6"
FT                   /id="PRO_0000013083"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   221 AA;  24961 MW;  92749EAF6A3EF48C CRC64;
     MTQQFWGPCL FSLFMAVLAQ ETLDPQKSKV DCNKGVAGTV YEYGANTLDG GEYVQFQQYA
     GKHILFVNVA SFCGLTATYP ELNTLQEELR PFNVSVLGFP CNQFGKQEPG KNSEILLGLK
     YVRPGGGFVP NFQLFEKGDV NGDNEQKVFS FLKSSCPPTS ELLGSPEHLF WDPMKVHDIR
     WNFEKFLVGP DGAPVMRWFH QTPVRVVQSD IMEYLNQTRT Q