Sarcolipin

Sarcolipin
PDB rendering based on 1jdm.
Available structures PDB 1jdm
Identifiers
Symbols	SLN; MGC12301; MGC125854; MGC125855
External IDs	OMIM: 602203 MGI: 1913652 GeneCards: SLN Gene
Gene Ontology Molecular function • enzyme regulator activity Cellular component • membrane • integral to membrane • sarcoplasmic reticulum • sarcoplasmic reticulum membrane Biological process • calcium ion transport • regulation of calcium ion transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6588	66402
Ensembl	ENSG00000170290	ENSMUSG00000042045
UniProt	O00631	Q9CQD6
RefSeq (mRNA)	NM_003063	NM_025540
RefSeq (protein)	NP_003054	NP_079816
Location (UCSC)	Chr 11: 107.58 – 107.59 Mb	Chr 9: 53.7 – 53.7 Mb
PubMed search	[1]	[2]

Sarcolipin is a protein that in humans is encoded by the SLN gene.

Function

Sarcoplasmic reticulum Ca²⁺-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca²⁺ from the cytosol into the lumen of the sarcoplasmic reticulum in muscle cells. This gene encodes a small proteolipid that regulates several sarcoplasmic reticulum Ca²⁺-ATPases. The transmembrane protein interacts with Ca²⁺-ATPases and reduces the accumulation of Ca²⁺ in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis.

Ablation of sarcolipin increases atrial Ca²⁺ transient amplitudes and enhanced atrial contractility. Furthermore, atria from sarcolipin-null mice have blunted response to isoproterenol stimulation, implicating sarcolipin as a mediator of beta-adrenergic responses in atria.

Interactions

SLN (gene) has been shown to interact with PLNand ATP2A1.

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. doi:10.1101/gr.6.1.35. PMID 8681137. 
• 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. doi:10.1074/jbc.273.20.12360. 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. doi:10.1042/0264-6021:3610277. PMC 1222307. PMID 11772399. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222307. 
• Mascioni A, Karim C, Barany G, et al. (2002). "Structure and orientation of sarcolipin in lipid environments.". Biochemistry 41 (2): 475–82. doi:10.1021/bi011243m. 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. doi:10.1074/jbc.M213132200. 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. PMC 154294. PMID 12692302. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=154294. 
• 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. PMC 515316. PMID 15342556. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=515316. 
• 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. PMC 1869624. PMID 17515962. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1869624.