Selenoprotein P

SelP, N terminus
Identifiers
SymbolSelP_N
PfamPF04592
Pfam clanCL0172
InterProIPR007671
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
SelP, C terminus
Identifiers
SymbolSelP_C
PfamPF04593
InterProIPR007672
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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.[1] This particular protein contains two domains: the C terminal and N terminal domain. The N-terminal domain is larger than the C terminal[2] and the N-terminal is thought to be glycosylated.[3]

  1. ^ Mostert V (April 2000). "Selenoprotein P: properties, functions, and regulation". Arch. Biochem. Biophys. 376 (2): 433–8. doi:10.1006/abbi.2000.1735. PMID 10775431.
  2. ^ Burk RF; Hill KE (2009). "Selenoprotein P-expression, functions, and roles in mammals". Biochim Biophys Acta. 1790 (11): 1441–7. doi:10.1016/j.bbagen.2009.03.026. PMC 2763998. PMID 19345254.
  3. ^ Kryukov GV; Gladyshev VN (December 2000). "Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues". Genes Cells. 5 (12): 1049–60. doi:10.1046/j.1365-2443.2000.00392.x. PMID 11168591. S2CID 31432708.