ID   GPX8B_XENLA             Reviewed;         209 AA.
AC   Q5U583;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable glutathione peroxidase 8-B;
DE            Short=GPx-8-B;
DE            Short=GSHPx-8-B;
DE            EC=1.11.1.9;
GN   Name=gpx8-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000305}.
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DR   EMBL; BC084801; AAH84801.1; -; mRNA.
DR   RefSeq; NP_001088474.1; NM_001095005.1.
DR   AlphaFoldDB; Q5U583; -.
DR   SMR; Q5U583; -.
DR   MaxQB; Q5U583; -.
DR   DNASU; 495339; -.
DR   GeneID; 495339; -.
DR   KEGG; xla:495339; -.
DR   CTD; 495339; -.
DR   Xenbase; XB-GENE-6253966; gpx8.L.
DR   OMA; KVVRFWR; -.
DR   OrthoDB; 1483113at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 495339; Expressed in internal ear and 20 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IPR013376; Glut_perox_Gpx7.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
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   TIGRFAMs; TIGR02540; gpx7; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Oxidoreductase; Peroxidase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..209
FT                   /note="Probable glutathione peroxidase 8-B"
FT                   /id="PRO_0000317760"
FT   TRANSMEM        18..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        79
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   209 AA;  23730 MW;  B4D575C7F5888041 CRC64;
     MEPLSPYPLK CSSPKAKVFL VFFSMVLCTG ILCVLQLKFL RAKGGDFYSY EVTDAKGRTV
     ALSKYRGKAS LVVNVASGCP HTEANYRSLQ ELHREFGPSH FTVLAFPCNQ FGESEPGTNK
     EIEAMAKRNY GVTFPVFSKI KILGSEAEPA YRFLVDSTKK EPRWNFWKYL VDPQGQVVKY
     WRPDETAESI RPEVASLVRQ IIMKKKEDL