GPX1_PIG
ID GPX1_PIG Reviewed; 206 AA.
AC Q8MJ14;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 29-SEP-2021, entry version 93.
DE RecName: Full=Glutathione peroxidase 1 {ECO:0000305};
DE Short=GPx-1;
DE Short=GSHPx-1;
DE EC=1.11.1.9 {ECO:0000250|UniProtKB:P07203};
DE AltName: Full=Cellular glutathione peroxidase;
GN Name=GPX1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hostetler C.E., Robison M.R., Kincaid R.L., Ott T.L.;
RT "Sus scrofa selenium-containing enzyme cytosolic glutathione peroxidase 1
RT (cGPX1) from the day 13 embryo.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protects the hemoglobin in erythrocytes from oxidative
CC breakdown. In platelets, plays a crucial role of glutathione peroxidase
CC in the arachidonic acid metabolism. {ECO:0000250|UniProtKB:P11352}.
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:P11352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834;
CC Evidence={ECO:0000250|UniProtKB:P11352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2
CC glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate +
CC glutathione disulfide + H2O; Xref=Rhea:RHEA:50708, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57444, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297,
CC ChEBI:CHEBI:90680; Evidence={ECO:0000250|UniProtKB:P11352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50709;
CC Evidence={ECO:0000250|UniProtKB:P11352};
CC -!- SUBUNIT: Homotetramer. Interacts with MIEN1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: During periods of oxidative stress, Sec-52 may react with a
CC superoxide radical, irreversibly lose hydroselenide and be converted to
CC dehydroalanine. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000305}.
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DR EMBL; AF532927; AAM94630.1; -; mRNA.
DR RefSeq; NP_999366.1; NM_214201.1.
DR IntAct; Q8MJ14; 1.
DR PeroxiBase; 3722; SscGPx01.
DR PeptideAtlas; Q8MJ14; -.
DR PRIDE; Q8MJ14; -.
DR GeneID; 397403; -.
DR KEGG; ssc:397403; -.
DR CTD; 2876; -.
DR InParanoid; Q8MJ14; -.
DR OrthoDB; 1483113at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IBA:GO_Central.
DR GO; GO:0047066; F:phospholipid-hydroperoxide glutathione peroxidase activity; ISS:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0019372; P:lipoxygenase pathway; ISS:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0010269; P:response to selenium ion; IBA:GO_Central.
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 Acetylation; Cytoplasm; Lipid metabolism; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Reference proteome; Selenocysteine.
FT CHAIN 1..206
FT /note="Glutathione peroxidase 1"
FT /id="PRO_0000066614"
FT ACT_SITE 52
FT /evidence="ECO:0000250"
FT SITE 52
FT /note="Subject to oxidation and hydroselenide loss to
FT dehydroalanine"
FT /evidence="ECO:0000250"
FT NON_STD 52
FT /note="Selenocysteine"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
FT MOD_RES 91
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 91
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 117
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 151
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 151
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07203"
SQ SEQUENCE 206 AA; 22591 MW; 4431BECD35A797A0 CRC64;
MCAAQRSAAA LAAVAPRSVY AFSARPLAGG EPISLGSLRG KVLLIENVAS LUGTTVRDYT
QMNELQRRLG PRGLVVLGFP CNQFGHQENA KNGEILNCLK YVRPGGGFEP NFMLFEKCEV
NGANAHPLFA FLREALPTPS DDATALMTDP KFITWSPVCR NDIAWNFEKF LVGPDGVPLR
RYSRRFLTID IEPDIEALLS QEPSSA
