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Sarcolipin

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
SLN
Available structures
PDBHuman UniProt search:PDBeRCSB
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)[1]
Chromosome 11 (human)
Genomic location for SLN
Genomic location for SLN
Band11q22.3Start107,707,378bp[1]
End107,719,693bp[1]
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 search[2]n/a
Wikidata
View/Edit Human

Sarcolipin is amicropeptideprotein that in humans is encoded by theSLNgene.[3][4]

Function

[edit]

Sarcoplasmic reticulum Ca2+-ATPases are transmembrane proteins that catalyze theATP-dependent transport ofCa2+ from the cytosol into the lumen of thesarcoplasmic 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 enhancedatrialcontractility. Furthermore, atria from sarcolipin-null mice have blunted response toisoproterenol stimulation, implicating sarcolipin as a mediator ofbeta-adrenergic responses in atria.[5]


Sarcolipin is an important mediator of muscle based non shivering thermogenesis (NST). It causes thesarcoplasmic 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 thebrown adipose tissue and beige adipose tissue.[8] Sarcolipin mediated heat production in contractile muscles helps endothermic fish like theopah heat its body. Some fishes like thebillfishes have a specialised brain heater tissue that is derived from muscles that cannot contract but specialise in producing heat using sarcolipin.

Interactions

[edit]

SLN (gene) has been shown tointeract withPLN[9][10] andATP2A1.[9][10]

References

[edit]
  1. ^abcGRCh38: 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. ^ab"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. ^abAsahi 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. ^abAsahi 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]
PDB gallery
  • 1jdm: NMR Structure of Sarcolipin
    1jdm: NMR Structure of Sarcolipin
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