Selenoprotein M (SELENOM)

Selenoprotein M (SELENOM) is a member of the selenoprotein M/SEP15 family, characterized by the presence of the rare amino acid selenocysteine, which is inserted at a UGA codon through a specialized mechanism involving a SECIS element in the mRNA[1][2]. SELENOM is highly expressed in the brain and localized primarily to the endoplasmic reticulum, where it may function as a thiol-disulfide oxidoreductase, participating in the formation and reduction of disulfide bonds via a CXXU motif (U = selenocysteine)[1][2][3]. Structurally, it is close to thioredoxin but forms a distinct subfamily with SELENOF, with unique features in its redox-active domain[1]. SELENOM interacts with cytoplasmic actins and participates in regulating the actin cytoskeleton, potentially impacting cell adhesion, migration, and mitosis—processes relevant in cancer and metastasis[1][2]. SELENOM is implicated in cellular protection against oxidative stress, neuroprotection, regulation of energy metabolism, and is required for normal bone and cartilage development[1][2]. Its dysregulation has been associated with several diseases, including neurodegenerative disorders and cancers such as hepatocellular carcinoma and renal cell carcinoma, where its levels may serve as a biomarker for disease progression and prognosis[1][2]. Currently, there is no direct therapeutic targeting of SELENOM with small-molecule drugs, but selenium supplementation alters its expression and activity; caution is warranted due to potential selenium toxicity[1][2].

Other names

SELMSEPMSelMselenoprotein SelMselenoprotein M/SEP15 family

Not specifically defined for therapeutic drugs, but selenium compounds regulate expression and redox activity; potential modulation of PI3K/Akt/mTOR pathway in cancer