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Literature summary for 7.2.2.10 extracted from

  • Holdensen, A.N.; Andersen, J.P.
    The length of the A-M3 linker is a crucial determinant of the rate of the Ca2+ transport cycle of sarcoplasmic reticulum Ca2+-ATPase (2009), J. Biol. Chem., 284, 12258-12265.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.2.2.10

Cloned(Commentary)

Cloned (Comment) Organism
mutants are expressed in COS-1 cells Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
E243G/Q244G the mutant shows wild type-like Ca2+-ATPase activity Oryctolagus cuniculus
K234A the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme Oryctolagus cuniculus
K234G the mutant shows reduced relative Ca2+ ATPase activiy compared to the wild type enzyme Oryctolagus cuniculus
additional information the deletion of either Glu243 or Gln244 results in a decrease in the relative Ca2+-ATPase activity, 1G and 3G inserts at site 2 have severe consequences consistent with the lack of measurable Ca2+ transport Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Oryctolagus cuniculus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Ca2+/cis
-
 Oryctolagus cuniculus ADP + phosphate + Ca2+/trans
-
 ?

Synonyms

Synonyms Comment Organism
sarco(endo)plasmic reticulum Ca2+-ATPase
-
 Oryctolagus cuniculus
sarcoplasmic reticulum Ca2+-ATPase
-
 Oryctolagus cuniculus
SERCA1a isoform Oryctolagus cuniculus