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Literature summary for 7.2.2.10 extracted from

  • Champeil, P.; Menguy, T.; Soulie, S.; Juul, B.; Gomez de Garcia, A.; Rusconi, F.; Falson, P.; Denoroy, L.; Henao, F.; le Maire, M.; Moeller, J.V.
    Characterization of a protease-resistant domain of the cytosolic portion of sarcoplasmic reticulum Ca2+-ATPase (1998), J. Biol. Chem., 273, 6619-6631.
    View publication on PubMed
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General Stability

General Stability Organism
treatment with a variety of proteases, including elastase, proteinase K, and endoproteinase Asp-N and Hlu-C, results in accumulation of soluble fragments starting close to the ATPase phosphorylation site Asp351 and ending in the Lys605-Arg615 region. These fragments retain the ability to bind nucleoties, although with reduced affinity compared with the intact enzyme Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining
sarcoplasmic reticulum
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 Oryctolagus cuniculus 16529
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Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Ca2+/out
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 Oryctolagus cuniculus ADP + phosphate + Ca2+/in
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 ?
additional information the ATP-binding cleft is mainly located within the p29/30 domain with the phosphorylation site strategically located at the N-terminal border of this domain Oryctolagus cuniculus ?
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