SLN (gene)

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Sarcolipin
PDB rendering based on 1jdm.
Available structures: 1jdm
Identifiers
Symbol(s) SLN; MGC12301; MGC125854; MGC125855
External IDs OMIM: 602203
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 6588 n/a
Ensembl ENSG00000170290 n/a
Uniprot O00631 n/a
Refseq NM_003063 (mRNA)
NP_003054 (protein)		 n/a (mRNA)
n/a (protein)
Location Chr 11: 107.08 - 107.09 Mb n/a
Pubmed search [1] n/a

Sarcolipin, also known as SLN, is a human gene.[1]

Sarcoplasmic reticulum Ca(2+)-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca(2+) from the cytosol into the lumen of the sarcoplasmic reticulum in muscle cells. This gene encodes a small proteolipid that regulates several sarcoplasmic reticulum Ca(2+)-ATPases. The transmembrane protein interacts with Ca(2+)-ATPases and reduces the accumulation of Ca(2+) in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis.[1]

[edit] References

  1. ^ a b Entrez Gene: SLN sarcolipin.

[edit] Further reading

  • Lanfranchi G, Muraro T, Caldara F, et al. (1996). "Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization.". Genome Res. 6 (1): 35–42. PMID 8681137. 
  • Odermatt A, Taschner PE, Scherer SW, et al. (1998). "Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease.". Genomics 45 (3): 541–53. doi:10.1006/geno.1997.4967. PMID 9367679. 
  • Odermatt A, Becker S, Khanna VK, et al. (1998). "Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase.". J. Biol. Chem. 273 (20): 12360–9. PMID 9575189. 
  • Smith WS, Broadbridge R, East JM, Lee AG (2002). "Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulum.". Biochem. J. 361 (Pt 2): 277–86. PMID 11772399. 
  • Mascioni A, Karim C, Barany G, et al. (2002). "Structure and orientation of sarcolipin in lipid environments.". Biochemistry 41 (2): 475–82. PMID 11781085. 
  • Asahi M, Kurzydlowski K, Tada M, MacLennan DH (2002). "Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs).". J. Biol. Chem. 277 (30): 26725–8. doi:10.1074/jbc.C200269200. PMID 12032137. 
  • 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. PMID 12477932. 
  • Minamisawa S, Wang Y, Chen J, et al. (2003). "Atrial chamber-specific expression of sarcolipin is regulated during development and hypertrophic remodeling.". J. Biol. Chem. 278 (11): 9570–5. PMID 12645548. 
  • Asahi M, Sugita Y, Kurzydlowski K, et al. (2003). "Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban.". Proc. Natl. Acad. Sci. U.S.A. 100 (9): 5040–5. doi:10.1073/pnas.0330962100. PMID 12692302. 
  • Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions.". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMID 15342556. 
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  • Vittorini S, Storti S, Parri MS, et al. (2007). "SERCA2a, phospholamban, sarcolipin, and ryanodine receptors gene expression in children with congenital heart defects.". Mol. Med. 13 (1-2): 105–11. doi:10.2119/2006-00054.Vittorini. PMID 17515962. 
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