| Primary Identifier | IPR007672 | Type | Domain |
| Short Name | SelP_C |
| description | SelP is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues, and accounts for more than 50% of the selenium content of rat and human plasma []. It is thought to be glycosylated []. SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity []. The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage []. The promoter structure of bovine SelP suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function []. The N-terminal region always contains one Sec residue, and this is separated from the C-terminal region (9-16 sec residues) by a histidine-rich sequence []. The large number of Sec residues in the C-terminal portion of SelP suggests that it may be involved in selenium transport or storage. However, it is also possible that this region has a redox function []. |
