Sarcolipin

SLN
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	1JDM
Identifiers
Aliases	SLN, sarcolipin
External IDs	OMIM: 602203; GeneCards: SLN; OMA:SLN - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	107,719,693 bp
RNA expression pattern
	Top expressed in
	thoracic diaphragm; ; triceps brachii muscle; ; glutes; ; biceps brachii; ; Skeletal muscle tissue of biceps brachii; ; Skeletal muscle tissue of rectus abdominis; ; muscle of thigh; ; quadriceps femoris muscle; ; vastus lateralis muscle; ; body of tongue;
	n/a
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	ATPase binding; enzyme inhibitor activity; enzyme regulator activity; protein binding;
Cellular component	integral component of membrane; endoplasmic reticulum membrane; membrane; endoplasmic reticulum; sarcoplasmic reticulum membrane; sarcoplasmic reticulum;
Biological process	positive regulation of protein depolymerization; negative regulation of protein-containing complex disassembly; negative regulation of calcium ion binding; regulation of calcium ion transport; negative regulation of catalytic activity; negative regulation of calcium ion transmembrane transporter activity; calcium ion transport; negative regulation of calcium ion import; sarcoplasmic reticulum calcium ion transport; regulation of relaxation of muscle; regulation of ATPase-coupled calcium transmembrane transporter activity; positive regulation of cold-induced thermogenesis;
	Sources:Amigo / QuickGO
Orthologs
	6588
	n/a
	ENSG00000170290
	n/a
	O00631
	n/a
	NM_003063
	n/a
	NP_003054
	n/a
	Wikidata
View/Edit Human

Sarcolipin is a micropeptide protein that in humans is encoded by the SLN gene.^[3]^[4]

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. The SLN gene encodes a small transmembrane proteolipid that regulates several sarcoplasmic reticulum Ca²-ATPases by reducing the accumulation of Ca² in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis.^[4]

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.^[5]

Sarcolipin is an important mediator of muscle based non shivering thermogenesis (NST). It causes the sarcoplasmic reticulum Ca²-ATPases to stop pumping Ca² ions but continue futilely hydrolysing ATP, thus releasing the energy as heat.^[6]^[7] Sarcolipin mediated heat production is very important for many organisms to maintain a warm body. In mammals thermogenesis by skeletal muscles is complemented by thermogenesis in the brown adipose tissue and beige adipose tissue. ^[8] Sarcolipin mediated heat production in contractile muscles helps endothermic fish like the opah heat its body. Some fishes like the billfishes have a specialised brain heater tissue that is derived from muscles that cannot contract but specialise in producing heat using sarcolipin.

Interactions

SLN (gene) has been shown to interact with PLN^[9]^[10] and ATP2A1.^[9]^[10]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000170290 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Odermatt A, Taschner PE, Scherer SW, Beatty B, Khanna VK, Cornblath DR, et al. (November 1997). "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. hdl:2066/25426. PMID 9367679. S2CID 41989102.
^ ^a ^b "Entrez Gene: SLN sarcolipin".
^ Babu GJ, Bhupathy P, Timofeyev V, Petrashevskaya NN, Reiser PJ, Chiamvimonvat N, Periasamy M (November 2007). "Ablation of sarcolipin enhances sarcoplasmic reticulum calcium transport and atrial contractility". Proceedings of the National Academy of Sciences of the United States of America. 104 (45): 17867–72. Bibcode:2007PNAS..10417867B. doi:10.1073/pnas.0707722104. PMC 2077025. PMID 17971438.
^ Bal NC, Periasamy M (March 2020). "Uncoupling of sarcoendoplasmic reticulum calcium ATPase pump activity by sarcolipin as the basis for muscle non-shivering thermogenesis". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 375 (1793): 20190135. doi:10.1098/rstb.2019.0135. PMC 7017432. PMID 31928193.
^ Legendre LJ, Davesne D (March 2020). "The evolution of mechanisms involved in vertebrate endothermy". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 375 (1793): 20190136. doi:10.1098/rstb.2019.0136. PMC 7017440. PMID 31928191.
^ Reilly SM, Saltiel RA (22 October 2015). "A Futile Approach to Fighting Obesity?". Cell. 163 (3): 539–540. doi:10.1016/j.cell.2015.10.006. PMID 26496598. S2CID 10336243.
^ ^a ^b Asahi M, Sugita Y, Kurzydlowski K, De Leon S, Tada M, Toyoshima C, MacLennan DH (April 2003). "Sarcolipin regulates sarco(endo)plasmic reticulum Ca2 -ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban". Proceedings of the National Academy of Sciences of the United States of America. 100 (9): 5040–5. Bibcode:2003PNAS..100.5040A. doi:10.1073/pnas.0330962100. PMC 154294. PMID 12692302.
^ ^a ^b Asahi M, Kurzydlowski K, Tada M, MacLennan DH (July 2002). "Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2 -ATPases (SERCAs)". The Journal of Biological Chemistry. 277 (30): 26725–8. doi:10.1074/jbc.C200269200. PMID 12032137.

Lanfranchi G, Muraro T, Caldara F, Pacchioni B, Pallavicini A, Pandolfo D, et al. (January 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 Research. 6 (1): 35–42. doi:10.1101/gr.6.1.35. PMID 8681137.
Odermatt A, Becker S, Khanna VK, Kurzydlowski K, Leisner E, Pette D, MacLennan DH (May 1998). "Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2 -ATPase". The Journal of Biological Chemistry. 273 (20): 12360–9. doi:10.1074/jbc.273.20.12360. PMID 9575189.
Smith WS, Broadbridge R, East JM, Lee AG (January 2002). "Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2 by the Ca2 -ATPase of skeletal-muscle sarcoplasmic reticulum". The Biochemical Journal. 361 (Pt 2): 277–86. doi:10.1042/0264-6021:3610277. PMC 1222307. PMID 11772399.
Mascioni A, Karim C, Barany G, Thomas DD, Veglia G (January 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 (July 2002). "Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2 -ATPases (SERCAs)". The Journal of Biological Chemistry. 277 (30): 26725–8. doi:10.1074/jbc.C200269200. PMID 12032137.
Minamisawa S, Wang Y, Chen J, Ishikawa Y, Chien KR, Matsuoka R (March 2003). "Atrial chamber-specific expression of sarcolipin is regulated during development and hypertrophic remodeling". The Journal of Biological Chemistry. 278 (11): 9570–5. doi:10.1074/jbc.M213132200. PMID 12645548.
Asahi M, Sugita Y, Kurzydlowski K, De Leon S, Tada M, Toyoshima C, MacLennan DH (April 2003). "Sarcolipin regulates sarco(endo)plasmic reticulum Ca2 -ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban". Proceedings of the National Academy of Sciences of the United States of America. 100 (9): 5040–5. Bibcode:2003PNAS..100.5040A. doi:10.1073/pnas.0330962100. PMC 154294. PMID 12692302.
Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, et al. (September 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Vittorini S, Storti S, Parri MS, Cerillo AG, Clerico A (2007). "SERCA2a, phospholamban, sarcolipin, and ryanodine receptors gene expression in children with congenital heart defects". Molecular Medicine. 13 (1–2): 105–11. doi:10.2119/2006-00054.Vittorini. PMC 1869624. PMID 17515962.

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000170290 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9367679-3] Odermatt A, Taschner PE, Scherer SW, Beatty B, Khanna VK, Cornblath DR, et al. (November 1997). "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. hdl:2066/25426. PMID 9367679. S2CID 41989102.

[entrez-4] "Entrez Gene: SLN sarcolipin".

[pmid17971438-5] Babu GJ, Bhupathy P, Timofeyev V, Petrashevskaya NN, Reiser PJ, Chiamvimonvat N, Periasamy M (November 2007). "Ablation of sarcolipin enhances sarcoplasmic reticulum calcium transport and atrial contractility". Proceedings of the National Academy of Sciences of the United States of America. 104 (45): 17867–72. Bibcode:2007PNAS..10417867B. doi:10.1073/pnas.0707722104. PMC 2077025. PMID 17971438.

[Bal2020-6] Bal NC, Periasamy M (March 2020). "Uncoupling of sarcoendoplasmic reticulum calcium ATPase pump activity by sarcolipin as the basis for muscle non-shivering thermogenesis". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 375 (1793): 20190135. doi:10.1098/rstb.2019.0135. PMC 7017432. PMID 31928193.

[Legendre2020-7] Legendre LJ, Davesne D (March 2020). "The evolution of mechanisms involved in vertebrate endothermy". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 375 (1793): 20190136. doi:10.1098/rstb.2019.0136. PMC 7017440. PMID 31928191.

[Reilly2020-8] Reilly SM, Saltiel RA (22 October 2015). "A Futile Approach to Fighting Obesity?". Cell. 163 (3): 539–540. doi:10.1016/j.cell.2015.10.006. PMID 26496598. S2CID 10336243.

[pmid12692302-9] Asahi M, Sugita Y, Kurzydlowski K, De Leon S, Tada M, Toyoshima C, MacLennan DH (April 2003). "Sarcolipin regulates sarco(endo)plasmic reticulum Ca2 -ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban". Proceedings of the National Academy of Sciences of the United States of America. 100 (9): 5040–5. Bibcode:2003PNAS..100.5040A. doi:10.1073/pnas.0330962100. PMC 154294. PMID 12692302.

[pmid12032137-10] Asahi M, Kurzydlowski K, Tada M, MacLennan DH (July 2002). "Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2 -ATPases (SERCAs)". The Journal of Biological Chemistry. 277 (30): 26725–8. doi:10.1074/jbc.C200269200. PMID 12032137.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

Function

Interactions

References

Further reading