| Function | Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney. |
| Protein Name | Endoplasmic Reticulum Aminopeptidase 1Arts-1Adipocyte-Derived Leucine AminopeptidaseA-LapAminopeptidase PilsPuromycin-Insensitive Leucyl-Specific AminopeptidasePils-ApVegf-Induced Aminopeptidase |
| Database Links | Reactome: R-MMU-983170 |
| Cellular Localisation | Endoplasmic Reticulum MembraneSingle-Pass Type Ii Membrane Protein |
| Alternative Protein Names | Endoplasmic Reticulum Aminopeptidase 1 proteinArts-1 proteinAdipocyte-Derived Leucine Aminopeptidase proteinA-Lap proteinAminopeptidase Pils proteinPuromycin-Insensitive Leucyl-Specific Aminopeptidase proteinPils-Ap proteinVegf-Induced Aminopeptidase proteinErap1 proteinAppils proteinArts1 protein |
Information sourced from Uniprot.org
