Selenoprotein P
| SelP, N terminus | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | SelP_N | ||||||||
| Pfam | PF04592 | ||||||||
| Pfam clan | CL0172 | ||||||||
| InterPro | IPR007671 | ||||||||
| |||||||||
| SelP, C terminus | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | SelP_C | ||||||||
| Pfam | PF04593 | ||||||||
| InterPro | IPR007672 | ||||||||
| |||||||||
In molecular biology, the protein domain selenoprotein P (SelP) is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues. It is a secreted glycoprotein, often found in the plasma. Its precise function remains to be elucidated; however, it is thought to have antioxidant properties. This particular protein contains two domains: the C terminal and N terminal domain. The N-terminal domain is larger than the C terminal and the N-terminal is thought to be glycosylated. The human version is SEPP1.