Aliases for GPX4 Gene
External Ids for GPX4 Gene
Previous GeneCards Identifiers for GPX4 Gene
This gene encodes a member of the glutathione peroxidase protein family. Glutathione peroxidase catalyzes the reduction of hydrogen peroxide, organic hydroperoxide, and lipid peroxides by reduced glutathione and functions in the protection of cells against oxidative damage. Human plasma glutathione peroxidase has been shown to be a selenium-containing enzyme and the UGA codon is translated into a selenocysteine. The encoded protein has been identified as a moonlighting protein based on its ability to serve dual functions as a peroxidase as well as a structural protein in mature spermatozoa. Through alternative splicing and transcription initiation, rat produces proteins that localize to the nucleus, mitochondrion, and cytoplasm. In humans, alternative transcription initiation and the cleavage sites of the mitochondrial and nuclear transit peptides need to be experimentally verified. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
GeneCards Summary for GPX4 Gene
GPX4 (Glutathione Peroxidase 4) is a Protein Coding gene. Diseases associated with GPX4 include Spondylometaphyseal Dysplasia, Sedaghatian Type and Neurotic Disorder. Among its related pathways are Arachidonic acid metabolism and Glutathione metabolism. GO annotations related to this gene include glutathione peroxidase activity and glutathione binding. An important paralog of this gene is GPX8.
UniProtKB/Swiss-Prot for GPX4 Gene
Protects cells against membrane lipid peroxidation and cell death. Required for normal sperm development and male fertility. Could play a major role in protecting mammals from the toxicity of ingested lipid hydroperoxides. Essential for embryonic development. Protects from radiation and oxidative damage. Essential for maturation and survival of photoreceptor cells. Plays a role in a primary T cell response to viral and parasitic infection by protecting T cells from ferroptosis, a cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species, and by supporting T cell expansion.