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Literature summary for 3.4.11.22 extracted from

  • Andrei-Selmer, C.; Knuppel, A.; Satyanarayana, C.; Heese, C.; Schu, P.V.
    A new class of mutants deficient in dodecamerization of aminopeptidase 1 and vacuolar transport (2001), J. Biol. Chem., 276, 11606-11614.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene APE1, DNA and amino acid sequence determination and analysis, single copy gene, expression of wild-type and mutant precursor enzymes in yeast Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information isolation and/or construction of mutant enzymes defective in autophagocytosis and vacuole biogenesis, the mutant enzyme accumulates in the Cvt vesicles of the secretory pathway in non-native conformation, overview Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol precursor protein of the enzyme Saccharomyces cerevisiae 5829
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vacuole the precursor enzyme is transported into the vacuole via the non-classic Cvt pathway by cytoplasmic double-membrane vesicles, which fuse with the vacuole releasing a single-membrane autophagic body into the vacuolar lumen where it is proteolytically maturated, overview Saccharomyces cerevisiae 5773
-

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification maturation of the cytosolic precursor protein to the mature enzyme in the vacuolar lumen Saccharomyces cerevisiae

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant precursor enzymes Saccharomyces cerevisiae

Subunits

Subunits Comment Organism
dodecamer homododecamer Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
aminopeptidase 1
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Saccharomyces cerevisiae
APE1
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Saccharomyces cerevisiae
pApe1p
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Saccharomyces cerevisiae
vacuolar aminopeptidase 1
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Saccharomyces cerevisiae