ERAP1 : endoplasmic reticulum aminopeptidase 1
Description
The ERAP1 (endoplasmic reticulum aminopeptidase 1) is a protein-coding gene located on chromosome 5.
The ERAP1 gene provides instructions for making a protein called endoplasmic reticulum aminopeptidase 1 (ERAP1). ERAP1 is located in the endoplasmic reticulum, a cellular structure involved in protein processing and transport. ERAP1 is an aminopeptidase, which means it cuts proteins into smaller fragments called peptides. It has two primary functions, both essential for a healthy immune system. First, ERAP1 cleaves cytokine receptors on cell surfaces, reducing their ability to signal within the cell and impacting inflammation. Second, ERAP1 breaks down proteins into smaller peptides that the immune system can recognize. These peptides are transported to the cell surface and displayed by MHC class I proteins. If the immune system detects these peptides as foreign (like viral or bacterial peptides), it triggers the infected cell's self-destruction. ERAP1 plays a vital role in protecting the body against autoimmune disorders and cancer.
ERAP1 is an aminopeptidase that plays a crucial role in peptide trimming, a necessary step for the production of most HLA class I-binding peptides. Peptide trimming is crucial for adjusting the length of longer precursor peptides to fit them for presentation on MHC class I molecules. ERAP1 exhibits a strong preference for substrates ranging from 9 to 16 residues in length. It rapidly degrades 13-mer peptides into 9-mer peptides and then stops. ERAP1 preferentially hydrolyzes leucine residues and peptides with a hydrophobic C-terminus, while demonstrating weak activity towards peptides with charged C-termini. ERAP1 may contribute to the inactivation of peptide hormones. It may also participate in the regulation of blood pressure by inactivating angiotensin II and/or generating bradykinin in the kidneys.
ERAP1 is also known as A-LAP, ALAP, APPILS, ARTS-1, ARTS1, ERAAP, ERAAP1, PILS-AP, PILSAP.
