SLN (gene)

Sarcolipin
File:PBB Protein SLN image.jpg PDB rendering based on 1jdm.
Available structures PDB List of PDB id codes 1jdm​
Identifiers
Symbols	SLN ; MGC12301; MGC125854; MGC125855
External IDs	Template:OMIM5
Gene ontology Molecular function Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE SLN 205374 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Sarcolipin, also known as SLN, is a human gene.

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.

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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Mascioni A, Karim C, Barany G; et al. (2002). "Structure and orientation of sarcolipin in lipid environments". Biochemistry. 41 (2): 475–82. PMID 11781085.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)