Literature summary for 7.2.2.10 extracted from

Meneghelli, S.; Fusca, T.; Luoni, L.; De Michelis, M.I.
Dual mechanism of activation of plant plasma membrane Ca2+-ATPase by acidic phospholipids: evidence for a phospholipid binding site which overlaps the calmodulin-binding site (2008), Mol. Membr. Biol., 25, 539-546.

Search for more literature for 7.2.2.10

Activating Compound

Activating Compound	Comment	Organism	Structure
Calmodulin	strongly activated by calmodulin	Arabidopsis thaliana
additional information	PMCA isoform ACA8 activity is hardly affected by phosphatidylcholine or phosphatidylethanolamine	Arabidopsis thaliana
phosphatidylinositol 4-monophosphate	433% stimulation of activity at 1 mM	Arabidopsis thaliana
phosphatidylserine	465% stimulation of activity at 1 mM	Arabidopsis thaliana

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Saccharomyces cerevisiae strain K616	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
A56S	the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold	Arabidopsis thaliana
additional information	the N-deleted mutant DELTA74-ACA8 is also activated by acidic phospholipids	Arabidopsis thaliana
R59A	the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold	Arabidopsis thaliana
Y62A	the mutation leads to lowered apparent affinity of the PMCA isoform ACA8 for phosphatidylinositol 4-monophosphate by 2-3fold	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	dependent on	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Synonyms

Synonyms	Comment	Organism
ACA8	-	Arabidopsis thaliana
plasma membrane Ca2+-ATPase isoform ACA8	-	Arabidopsis thaliana
PM Ca2+-ATPase	-	Arabidopsis thaliana
PMCA	-	Arabidopsis thaliana

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Release 2023.1 (January 2023)