P00435 · GPX1_BOVIN
- ProteinGlutathione peroxidase 1
- GeneGPX1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids205 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 H2OThis reaction proceeds in the forward direction.
- 2 glutathione + tert-butyl hydroperoxide = glutathione disulfide + H2O + tert-butanolThis reaction proceeds in the forward direction.
- cumene hydroperoxide + 2 glutathione = 2-phenylpropan-2-ol + glutathione disulfide + H2OThis reaction proceeds in the forward direction.
- (13S)-hydroperoxy-(9Z,11E)-octadecadienoate + 2 glutathione = (13S)-hydroxy-(9Z,11E)-octadecadienoate + glutathione disulfide + H2OThis reaction proceeds in the forward direction.
- (9S)-hydroperoxy-(10E,12Z)-octadecadienoate + 2 glutathione = (9S)-hydroxy-(10E,12Z)-octadecadienoate + glutathione disulfide + H2OThis reaction proceeds in the forward direction.
- (5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2OThis reaction proceeds in the forward direction.
- (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12S)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2OThis reaction proceeds in the forward direction.
- (12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + 2 glutathione = (12R)-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + glutathione disulfide + H2OThis reaction proceeds in the forward direction.
- (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + 2 glutathione = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + glutathione disulfide + H2OThis 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 + H2OThis 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 + H2OThis reaction proceeds in the forward direction.
- (15S)-hydroperoxy-(11Z,13E)-eicosadienoate + 2 glutathione = (15S)-hydroxy-(11Z,13E)-eicosadienoate + glutathione disulfide + H2OThis 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 + H2OThis reaction proceeds in the forward direction.
Features
Showing features for site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 41 | Not glycated | ||||
Sequence: K | ||||||
Active site | 52 | |||||
Sequence: U | ||||||
Site | 52 | Subject to oxidation and hydroselenide loss to dehydroalanine | ||||
Sequence: U | ||||||
Site | 91 | Not glycated | ||||
Sequence: K | ||||||
Site | 100 | Not glycated | ||||
Sequence: K | ||||||
Site | 124 | Not glycated | ||||
Sequence: K | ||||||
Site | 151 | Not glycated | ||||
Sequence: K | ||||||
Site | 169 | Not glycated | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | mitochondrion | |
Molecular Function | glutathione peroxidase activity | |
Molecular Function | phospholipid-hydroperoxide glutathione peroxidase activity | |
Biological Process | arachidonic acid metabolic process | |
Biological Process | glutathione metabolic process | |
Biological Process | hydrogen peroxide catabolic process | |
Biological Process | lipoxygenase pathway | |
Biological Process | positive regulation of supramolecular fiber organization | |
Biological Process | response to hydrogen peroxide | |
Biological Process | response to selenium ion |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlutathione peroxidase 1
- EC number
- Short namesGPx-1; GSHPx-1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP00435
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000066608 | 1-205 | Glutathione peroxidase 1 | |||
Sequence: MCAAQRSAAALAAAAPRTVYAFSARPLAGGEPFNLSSLRGKVLLIENVASLUGTTVRDYTQMNDLQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNCLKYVRPGGGFEPNFMLFEKCEVNGEKAHPLFAFLREVLPTPSDDATALMTDPKFITWSPVCRNDVSWNFEKFLVGPDGVPVRRYSRRFLTIDIEPDIETLLSQGASA | ||||||
Modified residue | 37 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 91 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 91 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 117 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 117 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Glycosylation | 117 | N-linked (Glc) (glycation) lysine; in vitro | ||||
Sequence: K | ||||||
Modified residue | 124 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 151 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 151 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 200 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 204 | Phosphoserine | ||||
Sequence: S |
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
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length205
- Mass (Da)22,659
- Last updated2008-02-26 v3
- Checksum7CBDF736CAAA92F6
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0AAA9THK7 | A0AAA9THK7_BOVIN | GPX1 | 192 |
Features
Showing features for non-standard residue, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-standard residue | 52 | Selenocysteine | ||||
Sequence: U | ||||||
Sequence conflict | 96 | in Ref. 2; AAI49309 | ||||
Sequence: L → P |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X13684 EMBL· GenBank· DDBJ | CAB40806.1 EMBL· GenBank· DDBJ | mRNA | ||
BC149308 EMBL· GenBank· DDBJ | AAI49309.1 EMBL· GenBank· DDBJ | mRNA |