Selenoprotein F (SELENOF)

Selenoprotein F (SELENOF, also known as SEP15) is a 15 kDa selenoprotein found in most eukaryotes, localized within the endoplasmic reticulum. It contains the rare amino acid selenocysteine (encoded by UGA via a SECIS element) and is a member of the SEP15/Selenoprotein M protein family. SELENOF is thought to function primarily in the quality control of protein folding, partnering with the enzyme UDP-glucose:glycoprotein glucosyltransferase (UGGT1/UGGT2) and may act as a thiol-disulfide isomerase, facilitating proper disulfide bond formation. It contains a thioredoxin-like domain and a surface-accessible redox motif. SELENOF and its genetic locus are implicated in various cancers, including prostate and breast, with reduced expression associated with malignancy and certain cancer outcomes. Despite clear evidence for involvement in ER protein homeostasis and pathophysiological relevance, the precise molecular function and regulatory mechanisms of SELENOF are still being elucidated[2][3][1][5][7].

Other names

SEP1515 kDa selenoproteinSelenoprotein F (15 kDa)SELENOF