Literature summary for 7.1.2.1 extracted from

Mason, A. B.; Allen, K.; Slaymana, C.
C-Terminal truncations of the Saccharomyces cerevisiae PMA1 H+-ATPase have major impacts on protein conformation, trafficking, quality control, and function (2014), Eukaryot. Cell, 13, 43-52.

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Protein Variants

Protein Variants	Comment	Organism
additional information	generation of stepwise truncation mutants. Truncations upstream of Lys889, removing more than 30 amino acid residues, yield no viable mutants, and the stretch from Ala881 (at the end of TM10) to Gly888 is required for stable folding and plasma membrane targeting. The stretch between Lys889 and Lys916 is ubiquitinated in carbon-starved cells as part of cellular quality control and is essential for normal ATPase folding and stability, as well as for autoinhibition of ATPase activity during glucose starvation. Removal of even one or two residues (Glu917 and Thr918) from the extreme C-terminus leads to visibly reduced expression of the ATPase at the plasma membrane	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P05030	-	-

Synonyms

Synonyms	Comment	Organism
PMA1	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)