P00435 · GPX1_BOVIN

  • Protein
    Glutathione peroxidase 1
  • Gene
    GPX1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis. Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides. In platelets catalyzes the reduction of 12-hydroperoxyeicosatetraenoic acid, the primary product of the arachidonate 12-lipoxygenase pathway.

Catalytic activity

  • 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
    This reaction proceeds in the forward direction.
    EC:1.11.1.9 (UniProtKB | ENZYME | Rhea)
  • a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
    EC:1.11.1.12 (UniProtKB | ENZYME | Rhea)
  • 2 glutathione + tert-butyl hydroperoxide = glutathione disulfide + H2O + tert-butanol
    This reaction proceeds in the forward direction.
  • cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (9S)-hydroperoxy-(10E,12Z)-octadecadienoate + 2 glutathione = (9S)-hydroxy-(10E,12Z)-octadecadienoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12R)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (5S)-hydroperoxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z,17Z)-eicosapentaenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (15S)-hydroperoxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (15S)-hydroperoxy-(11Z,13E)-eicosadienoate + 2 glutathione = (15S)-hydroxy-(11Z,13E)-eicosadienoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.
  • (17S)-hydroperoxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + 2 glutathione = (17S)-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + glutathione disulfide + H2O
    This reaction proceeds in the forward direction.

Features

Showing features for site, active site.

TypeIDPosition(s)Description
Site41Not glycated
Active site52
Site52Subject to oxidation and hydroselenide loss to dehydroalanine
Site91Not glycated
Site100Not glycated
Site124Not glycated
Site151Not glycated
Site169Not glycated

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentmitochondrion
Molecular Functionglutathione peroxidase activity
Molecular Functionphospholipid-hydroperoxide glutathione peroxidase activity
Biological Processarachidonic acid metabolic process
Biological Processglutathione metabolic process
Biological Processhydrogen peroxide catabolic process
Biological Processlipoxygenase pathway
Biological Processpositive regulation of supramolecular fiber organization
Biological Processresponse to hydrogen peroxide
Biological Processresponse to selenium ion

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutathione peroxidase 1
  • EC number
  • Short names
    GPx-1; GSHPx-1
  • Alternative names
    • Cellular glutathione peroxidase
    • Phospholipid-hydroperoxide glutathione peroxidase GPX1 (EC:1.11.1.12
      ) . EC:1.11.1.12 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      GPX1

Organism names

  • Taxonomic identifier
  • Strain
    • Crossbred X Angus
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P00435
  • Secondary accessions
    • A6QPG3

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000666081-205Glutathione peroxidase 1
Modified residue37Phosphoserine
Modified residue91N6-acetyllysine; alternate
Modified residue91N6-succinyllysine; alternate
Modified residue117N6-acetyllysine; alternate
Modified residue117N6-succinyllysine; alternate
Glycosylation117N-linked (Glc) (glycation) lysine; in vitro
Modified residue124N6-acetyllysine
Modified residue151N6-acetyllysine; alternate
Modified residue151N6-succinyllysine; alternate
Modified residue200Phosphoserine
Modified residue204Phosphoserine

Post-translational modification

During periods of oxidative stress, Sec-52 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homotetramer. Interacts with MIEN1.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the glutathione peroxidase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    205
  • Mass (Da)
    22,659
  • Last updated
    2008-02-26 v3
  • Checksum
    7CBDF736CAAA92F6
MCAAQRSAAALAAAAPRTVYAFSARPLAGGEPFNLSSLRGKVLLIENVASLUGTTVRDYTQMNDLQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNCLKYVRPGGGFEPNFMLFEKCEVNGEKAHPLFAFLREVLPTPSDDATALMTDPKFITWSPVCRNDVSWNFEKFLVGPDGVPVRRYSRRFLTIDIEPDIETLLSQGASA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0AAA9THK7A0AAA9THK7_BOVINGPX1192

Features

Showing features for non-standard residue, sequence conflict.

TypeIDPosition(s)Description
Non-standard residue52Selenocysteine
Sequence conflict96in Ref. 2; AAI49309

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X13684
EMBL· GenBank· DDBJ
CAB40806.1
EMBL· GenBank· DDBJ
mRNA
BC149308
EMBL· GenBank· DDBJ
AAI49309.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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