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.
N-glycosylated.
Belongs to the peptidase M1 family.
Ubiquitous.
APPILS, ARTS1, KIAA0525, UNQ584/PRO1154, ERAP1, Endoplasmic reticulum aminopeptidase 1, ARTS-1, Adipocyte-derived leucine aminopeptidase, Aminopeptidase PILS, Puromycin-insensitive leucyl-specific aminopeptidase, Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator, A-LAP, PILS-AP
Proteins
Immuno-oncology
107235Da
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