ID   GPXC_DIRIM              Reviewed;         221 AA.
AC   P52033;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Glutathione peroxidase;
DE            EC=1.11.1.9;
DE   AltName: Full=Di29;
DE   Flags: Precursor;
OS   Dirofilaria immitis (Canine heartworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Dirofilaria.
OX   NCBI_TaxID=6287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Venkatakrishnaiah L., James E.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=9501847; DOI=10.1006/expr.1998.4217;
RA   Tripp C.A., Frank R.S., Selkirk M.E., Tang L., Mika-Grieve M., Frank G.R.,
RA   Grieve R.B.;
RT   "Dirofilaria immitis: molecular cloning and expression of a cDNA encoding a
RT   selenium-independent secreted glutathione peroxidase.";
RL   Exp. Parasitol. 88:43-50(1998).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; U04693; AAA16224.1; -; mRNA.
DR   EMBL; U87457; AAB58573.1; -; mRNA.
DR   EMBL; U87458; AAB58574.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52033; -.
DR   SMR; P52033; -.
DR   PeroxiBase; 3752; DiGPx01.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
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   Glycoprotein; Oxidoreductase; Peroxidase; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..221
FT                   /note="Glutathione peroxidase"
FT                   /id="PRO_0000013094"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   221 AA;  25453 MW;  88FFF848D567CF28 CRC64;
     MFIQLLILSY AILLQLIATQ VADKQLPNLT KQCEPTSQTI YDFHVPTLDG SEKSLAEYRG
     KVLLLVNVAT YCAYTFQYND FNPMLENNSN GTLKILAFPC NQFLLQEPAE NHELLNGLKY
     VRPGNGWEPH GNMHIFGKVE VNGDDHHPLY KFLKEHCPQT VPIIGDRHQL MYNPIGTNDI
     IWNFEKFLID KKGHPRYRFH PSAWVQGSVI APFIDELERE I