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Selenoprotein P

From Wikipedia, the free encyclopedia
(Redirected from SEPP1)

SELENOP
Identifiers
AliasesSELENOP, SELP, SeP, SEPP, SEPP1, selenoprotein P, plasma, 1, selenoprotein P
External IDsOMIM: 601484; MGI: 894288; GeneCards: SELENOP
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

6414

20363

Ensembl

ENSG00000250722

ENSMUSG00000064373

UniProt

P49908

P70274

RefSeq (mRNA)

NM_005410
NM_001085486
NM_001093726

NM_001042613
NM_001042614
NM_009155

RefSeq (protein)

NP_001078955
NP_001087195
NP_005401

NP_001036078
NP_001036079
NP_033181

Location (UCSC)Chr 5: 42.8 – 42.89 MbChr 15: 3.3 – 3.31 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
SelP, N terminus
Identifiers
SymbolSelP_N
PfamPF04592
Pfam clanCL0172
InterProIPR007671
Available protein structures:
PDB  IPR007671 PF04592 (ECOD; PDBsum)  
AlphaFold
SelP, C terminus
Identifiers
SymbolSelP_C
PfamPF04593
InterProIPR007672
Available protein structures:
PDB  IPR007672 PF04593 (ECOD; PDBsum)  
AlphaFold

Selenoprotein P is a protein that in humans is encoded by the SELENOP gene.[5][6]

Selenoprotein P is the only known eukaryotic selenoprotein that contains multiple selenocysteine (Sec). These residues are encoded by the UGA codon that normally signals translation termination. In humans, rats, and mice, it contains 10 Sec residues,[7] one located at the C-terminal side of protein and others at the N-terminal side. It is a heparin-binding protein that appears to be associated with endothelial cells, and has been implicated to function as an antioxidant in the extracellular space. Several transcript variants, encoding either the same or different isoform, have been found for this gene.[6]

It is a secreted glycoprotein,[8] often found in the plasma. Its precise function remains to be elucidated; however, it is thought to have antioxidant properties.[9] This particular protein contains two domains: the C terminal and N terminal domain. The N-terminal domain is larger than the C terminal[10]

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.[8] The large number of Sec residues in the C-terminal portion of Selenoprotein P suggests that it may be involved in selenium transport or storage. However, it is also possible that this region has a redox function.[8]

N terminal domain

[edit]

N-terminal domain allows conservation of whole body selenium and appears to supply selenium to the kidney.[11]

The structure of the N-terminal domain is larger and contains less Selenium. However it is thought to be heavily glycosylated.[11]

C terminal domain

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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 tissue but not for the maintenance of whole-body selenium.[11]

The C-terminal domain is smaller in size but far more rich in selenium.[11]

Function

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Selenoprotein P may have antioxidant properties. It can attach to epithelial cells, and may protect vascular endothelial cells against peroxynitrite toxicity.[9] The high selenium content of Selenoprotein P suggests that it may be involved in selenium intercellular transport or storage.[8] The promoter structure of bovine Selenoprotein P suggests that it may be involved in countering heavy metal intoxication, and may also have a developmental function.[12]

Animal models

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Mice and dogs with knock-out variants in their SELENOP homologues (Selenop[13] and SELENOP[14] respectively) may develop cerebellar ataxia phenotypes.[15][16] SELENOP and neural precursor cell levels in mouse brains increase post-exercise. Mice engineered to lack SELENOP did not increase neural precursors.[17][18]

Protein interactions

[edit]

Binds to heparin in a pH-dependent manner[10]

References

[edit]
  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000250722 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000064373 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Hill KE, Lloyd RS, Burk RF (January 1993). "Conserved nucleotide sequences in the open reading frame and 3' untranslated region of selenoprotein P mRNA". Proceedings of the National Academy of Sciences of the United States of America. 90 (2): 537–541. Bibcode:1993PNAS...90..537H. doi:10.1073/pnas.90.2.537. PMC 45698. PMID 8421687.
  6. 1 2 "Entrez Gene: SELENOP selenoprotein P". Retrieved 2026-08-27.
  7. ↑ Burk and Hill 2009
  8. 1 2 3 4 Kryukov GV, Gladyshev VN (December 2000). "Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and expression of a protein containing 17 selenocysteine residues". Genes to Cells. 5 (12): 1049–1060. doi:10.1046/j.1365-2443.2000.00392.x. PMID 11168591. S2CID 31432708.
  9. 1 2 Mostert V (April 2000). "Selenoprotein P: properties, functions, and regulation". Archives of Biochemistry and Biophysics. 376 (2): 433–438. doi:10.1006/abbi.2000.1735. PMID 10775431.
  10. 1 2 Burk RF, Hill KE (November 2009). "Selenoprotein P-expression, functions, and roles in mammals". Biochimica et Biophysica Acta. 1790 (11): 1441–1447. doi:10.1016/j.bbagen.2009.03.026. PMC 2763998. PMID 19345254.
  11. 1 2 3 4 Hill KE, Zhou J, Austin LM, Motley AK, Ham AJ, Olson GE, et al. (April 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". The Journal of Biological Chemistry. 282 (15): 10972–10980. doi:10.1074/jbc.M700436200. PMID 17311913.
  12. ↑ 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): 211–217. doi:10.1016/S0378-1119(97)00369-7. PMID 9358058.
  13. ↑ "Selenop selenoprotein P [Mus musculus (house mouse)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-01-24.
  14. ↑ "SELENOP selenoprotein P [Canis lupus familiaris (dog)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-01-24.
  15. ↑ Christen M, Högler S, Kleiter M, Leschnik M, Weber C, Thaller D, et al. (August 2021). "Deletion of the SELENOP gene leads to CNS atrophy with cerebellar ataxia in dogs". PLoS Genetics. 17 (8) e1009716. doi:10.1371/journal.pgen.1009716. PMC 8360551. PMID 34339417.
  16. ↑ Schomburg L, Schweizer U, Holtmann B, Flohé L, Sendtner M, Köhrle J (March 2003). "Gene disruption discloses role of selenoprotein P in selenium delivery to target tissues". The Biochemical Journal. 370 (Pt 2): 397–402. doi:10.1042/bj20021853. PMC 1223208. PMID 12521380.
  17. ↑ PÉREZ ORTEGA RO (February 3, 2022). "Widely available supplement may explain brain boost from exercise". www.science.org. Retrieved 2022-02-07.
  18. ↑ Leiter O, Zhuo Z, Rust R, Wasielewska JM, Grönnert L, Kowal S, et al. (March 2022). "Selenium mediates exercise-induced adult neurogenesis and reverses learning deficits induced by hippocampal injury and aging". Cell Metabolism. 34 (3): 408–423.e8. doi:10.1016/j.cmet.2022.01.005. hdl:10072/418192. PMID 35120590. S2CID 246556829.
This article incorporates text from the public domain Pfam and InterPro: IPR007672

Further reading

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Retrieved from "https://en.wikipedia.org/w/index.php?title=Selenoprotein_P&oldid=1376449496"