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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
 
 
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