Aliases for SEPN1 Gene
External Ids for SEPN1 Gene
Previous HGNC Symbols for SEPN1 Gene
Previous GeneCards Identifiers for SEPN1 Gene
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. Mutations in this gene cause the classical phenotype of multiminicore disease and congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
GeneCards Summary for SEPN1 Gene
SEPN1 (Selenoprotein N, 1) is a Protein Coding gene. Diseases associated with SEPN1 include muscular dystrophy, rigid spine, 1 and myopathy, congenital, with fiber-type disproportion. Among its related pathways are Selenium Pathway and Selenium Metabolism and Selenoproteins. GO annotations related to this gene include calcium ion binding. An important paralog of this gene is ENSG00000255054.
UniProtKB/Swiss-Prot for SEPN1 Gene
Isoform 2: Plays an important role in cell protection against oxidative stress and in the regulation of redox-related calcium homeostasis. Regulates the calcium level of the ER by protecting the calcium pump ATP2A2 against the oxidoreductase ERO1A-mediated oxidative damage. Within the ER, ERO1A activity increases the concentration of H(2)O(2), which attacks the luminal thiols in ATP2A2 and thus leads to cysteinyl sulfenic acid formation (-SOH) and SEPN1 reduces the SOH back to free thiol (-SH), thus restoring ATP2A2 activity (PubMed:25452428). Acts as a modulator of ryanodine receptor (RyR) activity: protects RyR from oxidation due to increased oxidative stress, or directly controls the RyR redox state, regulating the RyR-mediated calcium mobilization required for normal muscle development and differentiation (PubMed:19557870, PubMed:18713863).
Essential for muscle regeneration and satellite cell maintenance in skeletal muscle (PubMed:21131290).