GPX3_MACFU
ID GPX3_MACFU Reviewed; 226 AA.
AC Q4AEH4;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 23-FEB-2022, entry version 54.
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 Macaca fuscata fuscata (Japanese macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9543;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15967696; DOI=10.1016/j.cbpc.2005.05.002;
RA Fukuhara R., Kageyama T.;
RT "Structure, gene expression, and evolution of primate glutathione
RT peroxidases.";
RL Comp. Biochem. Physiol. 141B:428-436(2005).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed intensively in the kidney and adrenal
CC gland, and weakly in the cerebellum, heart, and lung. Secreted in
CC plasma. {ECO:0000269|PubMed:15967696}.
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; AB121008; BAE17016.1; -; mRNA.
DR PeroxiBase; 3706; MfGPx03.
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:0008430; F:selenium binding; ISS:UniProtKB.
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; Secreted; Selenocysteine; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..226
FT /note="Glutathione peroxidase 3"
FT /id="PRO_0000042606"
FT ACT_SITE 73
FT /evidence="ECO:0000250"
FT NON_STD 73
FT /note="Selenocysteine"
SQ SEQUENCE 226 AA; 25576 MW; CD13D80423FEB17E CRC64;
MARLLQASCL LSLLLAGFLP QSRGQDKSKM DCHGGVSGTI YEYGALTIDG EEYIPFKQYI
GKYVLFVNVA SYUGLTGQYI ELNALQEELA PFGLVLLGFP CNQFGKQEPG ENSEILPSLK
YVRPGGGFVP NFQLFEKGDV NGEKEQKFYT FLKNSCPPTS ELLGTSDRLF WEPMKVHDIR
WNFEKFLVGP DGIPVMRWHH RTTISNVKMD ILSYMRRQAA LGVKRK
