SELENOS Antibody – Rabbit Polyclonal

This gene encodes a transmembrane protein that is localized in the endoplasmic reticulum (ER). It is involved in the degradation process of misfolded proteins in the ER, and may also have a role in inflammation control. This protein is a selenoprotein, containing the rare amino acid selenocysteine (Sec). Sec is encoded by the UGA codon, which normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, designated the Sec insertion sequence (SECIS) element, that is necessary for the recognition of UGA as a Sec codon, rather than as a stop signal. Two additional phylogenetically conserved stem-loop structures (Stem-loop 1 and Stem-loop 2) in the 3' UTR of this mRNA have been shown to function as modulators of Sec insertion. An alternatively spliced transcript variant, lacking the SECIS element and encoding a non-Sec containing shorter isoform, has been described for this gene (PMID:23614019). [provided by RefSeq, Jul 2017]

SELS: Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination. Belongs to the selenoprotein S family.

Protein type: Membrane protein, integral; Endoplasmic reticulum

Chromosomal Location of Human Ortholog: 15q26.3

Cellular Component: cytoplasmic microtubule; endoplasmic reticulum; integral to endoplasmic reticulum membrane; plasma membrane

Molecular Function: antioxidant activity; ATPase binding; enzyme binding; protein binding; receptor activity

Biological Process: cell redox homeostasis; cellular response to insulin stimulus; ER overload response; ER-associated protein catabolic process; establishment of protein localization; negative regulation of acute inflammatory response to antigenic stimulus; negative regulation of glucose import; negative regulation of glycogen biosynthetic process; negative regulation of inflammatory response; negative regulation of interleukin-6 production; negative regulation of nitric-oxide synthase biosynthetic process; negative regulation of tumor necrosis factor production; regulation of gluconeogenesis; response to glucose stimulus; response to redox state; retrograde protein transport, ER to cytosol; unfolded protein response