| 词条 | Selenoprotein P |
| 释义 |
| Symbol = SelP_N | Name = SelP, N terminus | image = | width = | caption = | Pfam = PF04592 | Pfam_clan = CL0172 | InterPro = IPR007671 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }}{{Infobox protein family | Symbol = SelP_C | Name = SelP, C terminus | image = | width = | caption = | Pfam = PF04593 | Pfam_clan = | InterPro = IPR007672 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} 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] FunctionSelP 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] StructureThe 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 domainFunctionN-terminal domain allows conservation of whole body selenium and appears to supply selenium to the kidney[5] StructureThe structure of the N-terminal domain is larger and contains less Selenium. However it is thought to be heavily glycosylated[5] C terminal domainFunctionThe 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 of whole body selenium. Brain and testis tissue.[5] StructureThe C-terminal domain is smaller in size but far more rich in selenium.[5] Protein interactionsBinds to herapin in a pH-dependent manner[2] References1. ^1 {{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 | url = }} {{InterPro content|IPR007672}}2. ^1 {{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 }} 3. ^1 2 3 {{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| url = }} 4. ^{{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| url = }} 5. ^1 2 3 {{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 | pmc= | url=https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=17311913 }} 1 : Protein families |
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