Selenoprotein P: Difference between revisions
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In [[molecular biology]] the [[protein domain]] ''' |
In [[molecular biology]], the [[protein domain]] '''selenoprotein P''' ('''SelP''') is the only known [[eukaryotic]] [[selenoprotein]] that contains multiple [[selenocysteine]] (Sec) residues. It is a [[secretion|secreted]] [[glycoprotein]], often found in the [[blood plasma|plasma]]. Its precise function remains to be elucidated; however, it is thought to have [[antioxidant]] properties.<ref name="pmid10775431">{{cite journal | author = Mostert V | title = Selenoprotein P: properties, functions, and regulation | journal = Arch. Biochem. Biophys. | volume = 376 | issue = 2 | pages = 433–8 |date=April 2000 | pmid = 10775431 | doi = 10.1006/abbi.2000.1735 }}</ref> This particular protein contains two domains: the [[C terminal]] and [[N terminal]] domain. The N-terminal domain is larger than the C terminal<ref name="pmid19345254">{{cite journal|author1=Burk RF |author2=Hill KE | title=Selenoprotein P-expression, functions, and roles in mammals. | journal=Biochim Biophys Acta | year= 2009 | volume= 1790 | issue= 11 | pages= 1441–7 | pmid=19345254 | doi=10.1016/j.bbagen.2009.03.026 | pmc=2763998 }}</ref> and the N-terminal is thought to be [[glycosylated]].<ref name="pmid11168591">{{cite journal |author1=Kryukov GV |author2=Gladyshev VN | title = Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues | journal = Genes Cells | volume = 5 | issue = 12 | pages = 1049–60 |date=December 2000 | pmid = 11168591 | doi = 10.1046/j.1365-2443.2000.00392.x|s2cid=31432708 | doi-access = free }}</ref> |
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==Function== |
==Function== |
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SelP may have [[antioxidant]] properties. It can attach to [[epithelial]] cells, and may protect vascular [[endothelial cell]]s against [[peroxynitrite]] [[toxic]]ity.<ref name="pmid10775431"/> The high selenium content of SelP suggests that it may be involved in selenium intercellular [[transport]] or storage.<ref name="pmid11168591"/> The [[promotor (biology)|promoter]] [[secondary structure|structure]] of [[cattle|bovine]] SelP suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function.<ref name="pmid9358058">{{cite journal |author1=Fujii M |author2=Saijoh K |author3=Kobayashi T |author4=Fujii S |author5=Lee MJ |author6=Sumino K | title = Analysis of bovine selenoprotein P-like protein gene and availability of metal responsive element (MRE) located in its promoter | journal = Gene | volume = 199 | issue = |
SelP may have [[antioxidant]] properties. It can attach to [[epithelial]] cells, and may protect vascular [[endothelial cell]]s against [[peroxynitrite]] [[toxic]]ity.<ref name="pmid10775431"/> The high selenium content of SelP suggests that it may be involved in selenium intercellular [[transport]] or storage.<ref name="pmid11168591"/> The [[promotor (biology)|promoter]] [[secondary structure|structure]] of [[cattle|bovine]] SelP suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function.<ref name="pmid9358058">{{cite journal |author1=Fujii M |author2=Saijoh K |author3=Kobayashi T |author4=Fujii S |author5=Lee MJ |author6=Sumino K | title = Analysis of bovine selenoprotein P-like protein gene and availability of metal responsive element (MRE) located in its promoter | journal = Gene | volume = 199 | issue = 1–2 | pages = 211–7 |date=October 1997 | pmid = 9358058 | doi = 10.1016/S0378-1119(97)00369-7}}</ref> |
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==Structure== |
==Structure== |
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===Function=== |
===Function=== |
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N-terminal domain allows conservation of whole body selenium |
N-terminal domain allows conservation of whole body selenium |
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and appears to supply selenium to the kidney<ref name="pmid17311913">{{cite journal |vauthors=Hill KE, Zhou J, Austin LM, Motley AK, Ham AJ, Olson GE, etal | title=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. | journal=J Biol Chem | year= 2007 | volume= 282 | issue= 15 | pages= 10972–80 | pmid=17311913 | doi=10.1074/jbc.M700436200 | |
and appears to supply selenium to the kidney<ref name="pmid17311913">{{cite journal |vauthors=Hill KE, Zhou J, Austin LM, Motley AK, Ham AJ, Olson GE, etal | title=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. | journal=J Biol Chem | year= 2007 | volume= 282 | issue= 15 | pages= 10972–80 | pmid=17311913 | doi=10.1074/jbc.M700436200 | doi-access=free }}</ref> |
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===Structure=== |
===Structure=== |
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===Function=== |
===Function=== |
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The function of the C-terminal domain is known to be vital for maintaining levels of selenium in brain and testis but not for the maintenance |
The function of the C-terminal domain is known to be vital for maintaining levels of selenium in brain and testis [[tissue (biology)|tissue]] but not for the maintenance |
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of whole |
of whole-body selenium.<ref name="pmid17311913"/> |
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===Structure=== |
===Structure=== |
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==Protein interactions== |
==Protein interactions== |
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Binds to |
Binds to heparin in a pH-dependent manner<ref name="pmid19345254"/> |
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==References== |
==References== |
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Latest revision as of 12:41, 14 July 2023
| 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.[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]
Function[edit]
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.[4]
Structure[edit]
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]
N terminal domain[edit]
Function[edit]
N-terminal domain allows conservation of whole body selenium and appears to supply selenium to the kidney[5]
Structure[edit]
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[edit]
Function[edit]
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[edit]
The C-terminal domain is smaller in size but far more rich in selenium.[5]
Protein interactions[edit]
Binds to heparin in a pH-dependent manner[2]
References[edit]
- ^ a b 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.
- ^ 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.
- ^ a b c d 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.
- ^ Fujii M; Saijoh K; Kobayashi T; Fujii S; Lee MJ; Sumino K (October 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. doi:10.1016/S0378-1119(97)00369-7. PMID 9358058.
- ^ a b c d 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.