Sarcolipin

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SLN
Protein SLN PDB 1jdm.png
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
AliasesSLN, sarcolipin
External IDsOMIM: 602203 GeneCards: SLN
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for SLN
Genomic location for SLN
Band11q22.3Start107,707,378 bp[1]
End107,719,693 bp[1]
RNA expression pattern
PBB GE SLN 205374 at fs.png
More reference expression data
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

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

Function[edit]

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] Recently it has been shown that SLN is an important mediator of muscle based thermogenesis and loss of sarcolipin predisposes mice to diet-induced obesity thus suggesting its role in energy metabolism and regulation of weight gain [6]

Interactions[edit]

SLN (gene) has been shown to interact with PLN[7][8] and ATP2A1.[7][8]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000170290 - Ensembl, 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, Chaudhry V, Yee WC, Schrank B, Karpati G, Breuning MH, Knoers N, MacLennan DH (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.
  4. ^ a b "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. doi:10.1073/pnas.0707722104. PMC 2077025. PMID 17971438.
  6. ^ Bal NC, Maurya SK, Sopariwala DH, Sahoo SK, Gupta SC, Shaikh SA, Pant M et al.: Sarcolipin is a newly identified regulator of muscle-based thermogenesis in mammals. Nat Med, 2012. http://www.nature.com/nm/journal/vaop/ncurrent/full/nm.2897.html
  7. ^ 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. doi:10.1073/pnas.0330962100. PMC 154294. PMID 12692302.
  8. ^ 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.

Further reading[edit]