GPX1_RABIT
ID GPX1_RABIT Reviewed; 200 AA.
AC P11909;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 123.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=2928123; DOI=10.1093/nar/17.5.2136;
RA Akasaka M., Mizoguchi J., Yoshimura S., Watanabe K.;
RT "Nucleotide sequence of cDNA for rabbit glutathione peroxidase.";
RL Nucleic Acids Res. 17:2136-2136(1989).
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.
CC -!- PTM: During periods of oxidative stress, Sec-46 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; X13837; CAB43546.1; -; mRNA.
DR PIR; S03723; S03723.
DR RefSeq; NP_001078913.1; NM_001085444.1.
DR STRING; 9986.ENSOCUP00000005141; -.
DR PeroxiBase; 3729; OcuGPx01.
DR GeneID; 100009258; -.
DR KEGG; ocu:100009258; -.
DR CTD; 2876; -.
DR eggNOG; KOG1651; Eukaryota.
DR InParanoid; P11909; -.
DR OrthoDB; 1483113at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISS:UniProtKB.
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:0019372; P:lipoxygenase pathway; 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 Acetylation; Cytoplasm; Lipid metabolism; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Reference proteome; Selenocysteine.
FT CHAIN 1..200
FT /note="Glutathione peroxidase 1"
FT /id="PRO_0000066616"
FT ACT_SITE 46
FT SITE 46
FT /note="Subject to oxidation and hydroselenide loss to
FT dehydroalanine"
FT /evidence="ECO:0000250"
FT NON_STD 46
FT /note="Selenocysteine"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
FT MOD_RES 85
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 85
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 111
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 111
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 145
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 145
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11352"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04041"
SQ SEQUENCE 200 AA; 21883 MW; D61951FEC2805814 CRC64;
MCAARMAAAA QSVYSFSAHP LAGGEPVNLG SLRGKVLLIE NVASLUGTTV RDYTQMNELQ
ERLGPRALVV LGFPCNQFGH QENAKNEEIL NSLKYVRPGG GFEPNFMLFQ KCEVNGAKAS
PLFAFLREAL PPPSDDPTAL MTDPKFITWC PVCRNDVSWS FEKFLVGPDG VPVRRYSRRF
PTIDIEPDIQ ALLSKGSGGA
