Identification and characterization of Fep15, a new selenocysteine-containing member of the Sep15 protein family

• DOI: 10.1042/bj20051569
• Publication Date: 2006-03-02T09:11:08Z
• Authors: Sergey V. Novoselov; Deame Hua; Alexey V. Lobanov; Vadim N. Gladyshev
• Keywords: Selenocysteine; Selenoprotein; Protein family; Stop codon

Sec (selenocysteine) is a rare amino acid in proteins. It co-translationally inserted into proteins at UGA codons with the help of SECIS (Sec insertion sequence) elements. A full set selenoproteins within genome, known as selenoproteome, highly variable different organisms. However, most eukaryotic are represented mammalian selenoproteome. In addition, many these have cysteine orthologues. Here, we describe new selenoprotein, designated Fep15, which distantly related to members 15 kDa selenoprotein (Sep15) family. Fep15 absent mammals, can be detected only fish and present organisms form. contrast other Sep15 family, contain putative active site composed cysteine, has Sec. When transiently expressed cells, incorporated an SECIS- SBP2 (SECIS-binding protein 2)-dependent manner was targeted endoplasmic reticulum by its N-terminal signal peptide. Phylogenetic analyses family suggest that evolved gene duplication.