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Literature summary for 3.4.11.3 extracted from

  • Werno, M.; Chamberlain, L.
    S-acylation of the insulin-responsive aminopeptidase (IRAP) quantitative analysis and identification of modified cysteines (2015), Sci. Rep., 5, 12413-12420 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.11.3

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of HA-tagged wild-type and mutant enzymes in HEK-293T cells Mus musculus

Protein Variants

Protein Variants Comment Organism
C103A/C114A no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected. Combined mutation of both C103A and C114A leads to a complete loss of IRAP S-acylation Mus musculus
C35A/C103A/C114A no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected. Combined mutation of both C103A and C114A leads to a complete loss of IRAP S-acylation Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane transmembrane enzyme Mus musculus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, zinc metalloprotease Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q8C129
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
S-acylation insulin-responsive aminopeptidase (IRAP) is identified as an S-acylated protein in adipocytes and other tissues, semi-quantitative acyl-RAC technique shows that approximately 60% of IRAP is S-acylated in 3T3-L1 adipocytes, palmitoylation. Mapping of the sites of S-acylation on IRAP to two cysteine residues, one of which is predicted to lie in the cytoplasmic side of the single transmembrane domain and the other which is just upstream of this transmembrane domain, these cysteines, C103, and C114, may be modified in a mutually-exclusive manner. Although S-acylation regulates the intracellular trafficking of several transmembrane proteins, no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected, suggesting that S-acylation is not essential for the movement of IRAP through the secretory pathway Mus musculus

Purification (Commentary)

Purification (Comment) Organism
recombinant HA-tagged wild-type and mutant enzymes from HEK-293T cells Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
3T3-L1 cell
-
 Mus musculus
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adipocyte
-
 Mus musculus
-

Synonyms

Synonyms Comment Organism
Insulin-responsive aminopeptidase
-
 Mus musculus
IRAP
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 Mus musculus
LNPEP
-
 Mus musculus

General Information

General Information Comment Organism
malfunction protein S-acylation (also referred to as palmitoylation) is a post-translational modification (PTM) involving the attachment of palmitate and other fatty acids to cysteine residues of proteins via thioester linkage, no effects of mutating the modified cysteines on the plasma membrane localisation of IRAP in transfected HEK-293T cells are detected Mus musculus
additional information insulin-responsive aminopeptidase (IRAP) is identified as an S-acylated protein in adipocytes and other tissues, semi-quantitative acyl-RAC technique shows that approximately 60% of IRAP is S-acylated in 3T3-L1 adipocytes Mus musculus