GPX_PROCL
ID GPX_PROCL Reviewed; 172 AA.
AC G9JJU2;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 29-SEP-2021, entry version 21.
DE RecName: Full=Glutathione peroxidase {ECO:0000303|PubMed:23567855};
DE Short=PcGPx {ECO:0000303|PubMed:23567855};
DE Short=Se-PcGPx {ECO:0000303|PubMed:23567855};
DE EC=1.11.1.9 {ECO:0000250|UniProtKB:P22352};
GN Name=GPx {ECO:0000303|PubMed:23567855};
OS Procambarus clarkii (Red swamp crayfish).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Astacoidea; Cambaridae; Procambarus.
OX NCBI_TaxID=6728;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AEU08498.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PUTATIVE FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Ovary {ECO:0000269|PubMed:23567855};
RX PubMed=23567855; DOI=10.1016/j.fsi.2013.03.375;
RA Xia X.F., Zheng J.J., Shao G.M., Wang J.L., Liu X.S., Wang Y.F.;
RT "Cloning and functional analysis of glutathione peroxidase gene in red
RT swamp crayfish Procambarus clarkii.";
RL Fish Shellfish Immunol. 34:1587-1595(2013).
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 (By similarity). May defend
CC against reactive oxygen species that accumulate during the immune
CC response. {ECO:0000250|UniProtKB:P22352, ECO:0000269|PubMed:23567855}.
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 -!- TISSUE SPECIFICITY: Expressed at high levels in the ovary and at lower
CC levels in the gill and hepatopancreas. Not detected in heart, brain,
CC thoracic ganglia, gut, muscle, epidermis or testis.
CC {ECO:0000269|PubMed:23567855}.
CC -!- DEVELOPMENTAL STAGE: Expressed strongly in fertilized eggs; expression
CC decreases significantly during the cleavage stage and is barely
CC detectable in subsequent stages of embryogenesis.
CC {ECO:0000269|PubMed:23567855}.
CC -!- INDUCTION: Up-regulated in hepatopancreas following bacterial or viral
CC infection. {ECO:0000269|PubMed:23567855}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000255}.
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DR EMBL; JN835259; AEU08498.1; -; mRNA.
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 Oxidoreductase; Peroxidase; Selenocysteine.
FT CHAIN 1..172
FT /note="Glutathione peroxidase"
FT /id="PRO_0000423663"
FT ACT_SITE 28
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT NON_STD 28
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 172 AA; 19557 MW; 392C604D1843A00D CRC64;
MSLENGTDVS FEEFRGKVVL VINVATYUGL TVPSYTQMNA LAEFYVDQDF VILGFPCNQF
EMLEPAANAE IMNGIRYVRP GDGFEPLMTL FEKTEVNGAT EDPLFTFLKS ACESTYTEFY
SSLFYEPIRI GDIQWNFEKF LIGKDGKPYT RYHPDVVDPE ALKDDINTLL SA
