Literature summary for 7.2.2.10 extracted from

Clausen, J.D.; Holdensen, A.N.; Andersen, J.P.
Critical roles of interdomain interactions for modulatory ATP binding to sarcoplasmic reticulum Ca2+-ATPase (2014), J. Biol. Chem., 289, 29123-29134.

Search for more literature for 7.2.2.10

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
D203R	the mutant shows an about 5fold reduced basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
D203R/R678D	the mutant shows an about 3.5fold reduced basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
E439A	the mutant shows an about 15fold basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
E439S	the mutant shows an about 10fold basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
Q202A	th mutation causes reduced Ca2+ transport and ATPase activity	Oryctolagus cuniculus
Q202A/D203A	the mutant shows an about 4fold reduced basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
R678A	the mutant shows a reduced basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
R678D	the mutant shows an about 6fold reduced basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
R678Q	the mutant shows an about 1.4fold reduced basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
S186A	the mutant shows an about 6fold increased basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
S186E	the mutant shows an about 1,2fold reduced basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus
S186E/E439S	the mutant restores the basal dephosphorylation rate to a level about 2fold faster than that of the wild type. Little stimulation of the dephosphorylation by ATPis seen in this mutant	Oryctolagus cuniculus
S186P	the mutant shows an about 18fold increased basal dephosphorylation rate constant compared to the wild type enzyme	Oryctolagus cuniculus

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + 2 Ca2+[side 1]	Oryctolagus cuniculus	-	ADP + phosphate + 2 Ca2+[side 2]	-	?

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	P04191	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	upon binding to the Ca2E1 state, ATP phosphorylates the enzyme, and by binding to other conformational states in a non-phosphorylating modulatory mode ATP stimulates the dephosphorylation and other partial reaction steps of the cycle, thereby ensuring a high rate of Ca2+ transport under physiological conditions	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 + 2 Ca2+[side 1]	-	Oryctolagus cuniculus	ADP + phosphate + 2 Ca2+[side 2]	-	?

Synonyms

Synonyms	Comment	Organism
sarcoplasmic reticulum Ca2+-ATPase	-	Oryctolagus cuniculus
SERCA1a	-	Oryctolagus cuniculus

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Release 2023.1 (January 2023)