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Sarcolipin

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(Redirected from SLN (gene)) Protein-coding gene in the species Homo sapiens
SLN
Available structures
PDBHuman UniProt search: PDBe RCSB
List of PDB id codes

1JDM

Identifiers
AliasesSLN, sarcolipin
External IDsOMIM: 602203; GeneCards: SLN; OMA:SLN - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)
Chromosome 11 (human)Genomic location for SLNGenomic location for SLN
Band11q22.3Start107,707,378 bp
End107,719,693 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
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
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6588

n/a

Ensembl

ENSG00000170290

n/a

UniProt

O00631

n/a

RefSeq (mRNA)

NM_003063

n/a

RefSeq (protein)

NP_003054

n/a

Location (UCSC)Chr 11: 107.71 – 107.72 Mbn/a
PubMed searchn/a
Wikidata
View/Edit Human

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

Function

Sarcoplasmic reticulum Ca-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca 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 Ca-ATPases by reducing the accumulation of Ca in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis.

Ablation of sarcolipin increases atrial Ca 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.


Sarcolipin is an important mediator of muscle based non shivering thermogenesis (NST). It causes the sarcoplasmic reticulum Ca-ATPases to stop pumping Ca ions but continue futilely hydrolysing ATP, thus releasing the energy as heat. 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. 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 and ATP2A1.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000170290Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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.
  4. ^ "Entrez Gene: SLN sarcolipin".
  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.
  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.
  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.
  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.
  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.
  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.

Further reading

PDB gallery
  • 1jdm: NMR Structure of Sarcolipin 1jdm: NMR Structure of Sarcolipin
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