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
glycosylated.[3]
Function
SelP may have
structure of bovine SelP suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function.[4]
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
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]
N terminal domain
Function
N-terminal domain allows conservation of whole body selenium and appears to supply selenium to the kidney[5]
Structure
The structure of the N-terminal domain is larger and contains less Selenium. However it is thought to be heavily glycosylated[5]
C terminal domain
Function
The function of the C-terminal domain is known to be vital for maintaining levels of selenium in brain and testis tissue but not for the maintenance of whole-body selenium.[5]
Structure
The C-terminal domain is smaller in size but far more rich in selenium.[5]
Protein interactions
Binds to heparin in a pH-dependent manner[2]