Sarcolipin

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

SLN
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesSLN, sarcolipin
External IDsOMIM: 602203; GeneCards: SLN; OMA:SLN - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003063

n/a

RefSeq (protein)

NP_003054

n/a

Location (UCSC)Chr 11: 107.71 – 107.72 Mbn/a
PubMed search[2]n/a
Wikidata
View/Edit Human

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

Further reading

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