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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.
Gene Name: | endoplasmic reticulum aminopeptidase 1 |
Family/Subfamily: | Exopeptidase , Metallopeptidase M1 |
Synonyms: | ERAP1, A-LAP, ALAP, APPILS, ARTS1, ERAAP, ERAAP1, KIAA0525, PILS-AP, Aminopeptidase PILS, ARTS-1, PILSAP |
Target Sequences: | AF106037 NP_057526.3 Q9NZ08 |
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