Selenoprotein P
| SelP_C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | SelP_C | ||||||||
| Pfam | PF04593 | ||||||||
| InterPro | IPR007672 | ||||||||
| |||||||||
| SelP_N | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | SelP_N | ||||||||
| Pfam | PF04592 | ||||||||
| Pfam clan | CL0172 | ||||||||
| InterPro | IPR007671 | ||||||||
| |||||||||
In molecular biology the protein domain SelP stands for selenoprotein P which is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec) residues. It is a secreted glycoprotein, often found in the plasma. It's 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].
It is thought to be glycosylated.[3]
N terminal domain
Function
Structure
Larger Selenium poor[4]
C terminal domain
Function
critical for the maintenance of selenium in brain and testis but not for the maintenance of whole body selenium[4]
Structure
Smaller selenium rich [4]
Protein interactions
Binds to herapin in a pH-dependent manner[2]
Function
SelP may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity.[1] The high selenium content of SelP suggests that it may be involved in selenium intercellular transport or storage.[3] The promoter structure of bovine SelP suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function.[5]
Structure
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.[3] 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.[3]
References
- ^ a b Mostert V (2000). "Selenoprotein P: properties, functions, and regulation". Arch. Biochem. Biophys. 376 (2): 433–8. doi:10.1006/abbi.2000.1735. PMID 10775431.
{{cite journal}}: Unknown parameter|month=ignored (help) - ^ a b 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.
{{cite journal}}: CS1 maint: PMC format (link) - ^ a b c d Kryukov GV, Gladyshev VN (2000). "Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues". Genes Cells. 5 (12): 1049–60. PMID 11168591.
{{cite journal}}: Unknown parameter|month=ignored (help) - ^ a b c Hill KE, Zhou J, Austin LM, Motley AK, Ham AJ, Olson GE; et al. (2007). "The selenium-rich C-terminal domain of mouse selenoprotein P is necessary for the supply of selenium to brain and testis but not for the maintenance of whole body selenium". J Biol Chem. 282 (15): 10972–80. doi:10.1074/jbc.M700436200. PMID 17311913.
{{cite journal}}: Explicit use of et al. in:|author=(help)CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ Fujii M, Saijoh K, Kobayashi T, Fujii S, Lee MJ, Sumino K (1997). "Analysis of bovine selenoprotein P-like protein gene and availability of metal responsive element (MRE) located in its promoter". Gene. 199 (1–2): 211–7. PMID 9358058.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link)