Protein ATP2A1 PDB 1iwo.png
AliasesATP2A1, ATP2A, SERCA1, ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1
External IDsOMIM: 108730 MGI: 105058 HomoloGene: 7635 GeneCards: ATP2A1
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 16: 28.88 – 28.9 MbChr 7: 126.05 – 126.06 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (SERCA1) is an enzyme that in humans is encoded by the ATP2A1 gene.[5]


This gene encodes one of the SERCA Ca2+-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in muscular excitation and contraction.[5]

Clinical significance

Mutations in this gene cause some autosomal recessive forms of Brody disease, characterized by increasing impairment of muscular relaxation during exercise. Alternative splicing results in two transcript variants encoding different isoforms.[5] Alternative splicing of ATP2A1 is also implicated in myotonic dystrophy type 1.

ATP2A1 SERCA pumps were very strongly down regulated in amyotrophic lateral sclerosis.[6]


ATP2A1 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000196296 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030730 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c "Entrez Gene: ATP2A1 ATPase, Ca++ transporting, cardiac muscle, fast twitch 1".
  6. ^ Mukund, Kavitha; Subramaniam, Shankar (2017). "Co-expression Network Approach Reveals Functional Similarities among Diseases Affecting Human Skeletal Muscle". Frontiers in Physiology. 8: 980. doi:10.3389/fphys.2017.00980. PMC 5717538. PMID 29249983.
  7. ^ 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)". J. Biol. Chem. 277 (30): 26725–8. doi:10.1074/jbc.C200269200. PMID 12032137.
  8. ^ 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". Proc. Natl. Acad. Sci. U.S.A. 100 (9): 5040–5. Bibcode:2003PNAS..100.5040A. doi:10.1073/pnas.0330962100. PMC 154294. PMID 12692302.
  9. ^ Asahi M, Kimura Y, Kurzydlowski K, Tada M, MacLennan DH (November 1999). "Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites". J. Biol. Chem. 274 (46): 32855–62. doi:10.1074/jbc.274.46.32855. PMID 10551848.
  10. ^ Asahi M, Green NM, Kurzydlowski K, Tada M, MacLennan DH (August 2001). "Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPases". Proc. Natl. Acad. Sci. U.S.A. 98 (18): 10061–6. Bibcode:2001PNAS...9810061A. doi:10.1073/pnas.181348298. PMC 56915. PMID 11526231.

Further reading