SEPP1

SEPP1
Identifiers
Aliases SEPP1, SELP, SeP, SEPP, selenoprotein P, plasma, 1
External IDs MGI: 894288 HomoloGene: 3945 GeneCards: SEPP1
Orthologs
Species Human Mouse
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_001078955.1
NP_005401.3

NP_001036078.1
NP_001036079.1
NP_033181.3

Location (UCSC) Chr 5: 42.8 – 42.89 Mb Chr 15: 3.27 – 3.28 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Selenoprotein P is a protein that in humans is encoded by the SEPP1 gene.[3][4]

This gene encodes a selenoprotein containing multiple selenocysteine (Sec) residues, which are encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), which is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This selenoprotein is an extracellular glycoprotein, and is unusual in that it contains 9 Sec residues (human, rat, mouse - see Burk and Hill 2009) per polypeptide. 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.[4]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ Hill KE, Lloyd RS, Burk RF (Feb 1993). "Conserved nucleotide sequences in the open reading frame and 3' untranslated region of selenoprotein P mRNA". Proc Natl Acad Sci U S A. 90 (2): 537–41. doi:10.1073/pnas.90.2.537. PMC 45698Freely accessible. PMID 8421687.
  4. 1 2 "Entrez Gene: SEPP1 selenoprotein P, plasma, 1".

Further reading

  • Burk RF, Hill KE (1994). "Selenoprotein P. A selenium-rich extracellular glycoprotein". J. Nutr. 124 (10): 1891–7. PMID 7931697. 
  • Mostert V (2000). "Selenoprotein P: properties, functions, and regulation". Arch. Biochem. Biophys. 376 (2): 433–8. doi:10.1006/abbi.2000.1735. PMID 10775431. 
  • Hill KE, Lloyd RS, Yang JG, et al. (1991). "The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame". J. Biol. Chem. 266 (16): 10050–3. PMID 2037562. 
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
  • Akesson B, Bellew T, Burk RF (1994). "Purification of selenoprotein P from human plasma". Biochim. Biophys. Acta. 1204 (2): 243–9. doi:10.1016/0167-4838(94)90014-0. PMID 8142465. 
  • Hill KE, Dasouki M, Phillips JA, Burk RF (1997). "Human selenoprotein P gene maps to 5q31". Genomics. 36 (3): 550–1. doi:10.1006/geno.1996.0505. PMID 8884283. 
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
  • Mostert V, Lombeck I, Abel J (1998). "A novel method for the purification of selenoprotein P from human plasma". Arch. Biochem. Biophys. 357 (2): 326–30. doi:10.1006/abbi.1998.0809. PMID 9735174. 
  • Saito Y, Hayashi T, Tanaka A, et al. (1999). "Selenoprotein P in human plasma as an extracellular phospholipid hydroperoxide glutathione peroxidase. Isolation and enzymatic characterization of human selenoprotein p". J. Biol. Chem. 274 (5): 2866–71. doi:10.1074/jbc.274.5.2866. PMID 9915822. 
  • Koyama H, Omura K, Ejima A, et al. (1999). "Separation of selenium-containing proteins in human and mouse plasma using tandem high-performance liquid chromatography columns coupled with inductively coupled plasma-mass spectrometry". Anal. Biochem. 267 (1): 84–91. doi:10.1006/abio.1998.2949. PMID 9918658. 
  • Arteel GE, Franken S, Kappler J, Sies H (2000). "Binding of selenoprotein P to heparin: characterization with surface plasmon resonance". Biol. Chem. 381 (3): 265–8. doi:10.1515/BC.2000.034. PMID 10782998. 
  • Hondal RJ, Ma S, Caprioli RM, et al. (2001). "Heparin-binding histidine and lysine residues of rat selenoprotein P". J. Biol. Chem. 276 (19): 15823–31. doi:10.1074/jbc.M010405200. PMID 11278668. 
  • Nishimura K, Matsumiya K, Tsujimura A, et al. (2001). "Association of selenoprotein P with testosterone production in cultured Leydig cells". Arch. Androl. 47 (1): 67–76. doi:10.1080/01485010152104026. PMID 11442337. 
  • Al-Taie OH, Seufert J, Mörk H, et al. (2003). "A complex DNA-repeat structure within the Selenoprotein P promoter contains a functionally relevant polymorphism and is genetically unstable under conditions of mismatch repair deficiency". Eur. J. Hum. Genet. 10 (9): 499–504. doi:10.1038/sj.ejhg.5200811. PMID 12173025. 
  • Saito Y, Takahashi K (2003). "Characterization of selenoprotein P as a selenium supply protein". Eur. J. Biochem. 269 (22): 5746–51. doi:10.1046/j.1432-1033.2002.03298.x. PMID 12423375. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241Freely accessible. PMID 12477932. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 


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