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Literature summary for 7.2.2.2 extracted from

  • Adle, D.J.; Lee, J.
    Expressional control of a cadmium-transporting P1B-type ATPase by a metal sensing degradation signal (2008), J. Biol. Chem., 283, 31460-31468.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information in response to cadmium, yeast cells rapidly enhance expression of Pca1 by a post-transcriptional mechanism Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
Pca1 expression analysis Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information construction of the BY4741 haploid strain and null mutants. Fusion of the metal-responding degradation signal encompassing amino acids 250-350 to a stable protein demonstrates that it functions autonomously in a metal-responsive manner. Pca1 is not stabilized in a strain defective in endocytosis. Mutation of all seven cysteine residues to alanine alters the regulation of the enzyme expression, overview Saccharomyces cerevisiae

General Stability

General Stability Organism
Pca1 is a short-lived proteinwith t1?2 below 5 min and is subject to ubiquitination when cells are growing in media lacking cadmium Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
additional information Pca1 degradation is dependent on the proteasome but not vacuolar proteases Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information Pca1 contains a cytosolic cysteine-rich N-terminal extension of nearly 400 residues Saccharomyces cerevisiae
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plasma membrane in the absence of cadmium, Pca1 is targeted for degradation before reaching the plasma membrane Saccharomyces cerevisiae 5886
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharomyces cerevisiae Pca1, a P1B-type ATPase, plays a critical role in cadmium resistance in Saccharomyces cerevisiae by extruding intracellular cadmium as a cadmium-specific efflux pump, regulation requires cysteine residues within the cytosolic domain. Mechanistic insights into the cadmium-dependent control of Pca1 expression, pathway for Pca1 turnover and the mechanism of cadmium sensing that leads to up-regulation of Pca1, overview. Pca1 degradation is dependent on the proteasome but not vacuolar proteases ?
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?
additional information Saccharomyces cerevisiae BY4741 Pca1, a P1B-type ATPase, plays a critical role in cadmium resistance in Saccharomyces cerevisiae by extruding intracellular cadmium as a cadmium-specific efflux pump, regulation requires cysteine residues within the cytosolic domain. Mechanistic insights into the cadmium-dependent control of Pca1 expression, pathway for Pca1 turnover and the mechanism of cadmium sensing that leads to up-regulation of Pca1, overview. Pca1 degradation is dependent on the proteasome but not vacuolar proteases ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Posttranslational Modification

Posttranslational Modification Comment Organism
additional information cadmium sensing by cysteine residues within the domain, the N-terminal metal-responding degradation signal encompassing amino acids 250-350, circumvents ubiquitination and degradation of Pca1 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Cd2+/in Pca1 is a cadmium transporter, the N-terminal metal-responding degradation signal encompassing amino acids 250-350 functions autonomously in a metal-responsive manner, overview Saccharomyces cerevisiae ADP + phosphate + Cd2+/out
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?
ATP + H2O + Cd2+/in Pca1 is a cadmium transporter, the N-terminal metal-responding degradation signal encompassing amino acids 250-350 functions autonomously in a metal-responsive manner, overview Saccharomyces cerevisiae BY4741 ADP + phosphate + Cd2+/out
-
?
additional information Pca1, a P1B-type ATPase, plays a critical role in cadmium resistance in Saccharomyces cerevisiae by extruding intracellular cadmium as a cadmium-specific efflux pump, regulation requires cysteine residues within the cytosolic domain. Mechanistic insights into the cadmium-dependent control of Pca1 expression, pathway for Pca1 turnover and the mechanism of cadmium sensing that leads to up-regulation of Pca1, overview. Pca1 degradation is dependent on the proteasome but not vacuolar proteases Saccharomyces cerevisiae ?
-
?
additional information Pca1, a P1B-type ATPase, plays a critical role in cadmium resistance in Saccharomyces cerevisiae by extruding intracellular cadmium as a cadmium-specific efflux pump, regulation requires cysteine residues within the cytosolic domain. Mechanistic insights into the cadmium-dependent control of Pca1 expression, pathway for Pca1 turnover and the mechanism of cadmium sensing that leads to up-regulation of Pca1, overview. Pca1 degradation is dependent on the proteasome but not vacuolar proteases Saccharomyces cerevisiae BY4741 ?
-
?

Subunits

Subunits Comment Organism
More Pca1 possesses a metal-responding degradation signal encompassing amino acids 250-350, which functions autonomously in a metal-responsive manner, being part of the cytosolic cysteine-rich N-terminal extension of nearly 400 residues Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
cadmium-transporting P1B-type ATPase
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Saccharomyces cerevisiae
PCA1
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Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP
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Saccharomyces cerevisiae