The endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1) is localized to the lumen of the ER, which removes NH2-terminal residues from many antigenic precursors for MHC class I peptide presentation. ERAP1 is also designated adipocyte-derived leucine aminopeptidase (A-LAP), puromycin-insensitive leucine-specific aminopeptidase (PILS-AP) and aminopeptidase regulator of TNFR1 shedding (ARTS-1). Peptides presented by MHC class I on the surface of a cell must be eight to eleven residues long and ERAP1 specifically trims peptides of nine amino acids or more. ERAP1 is induced by interferon-g and encoded for by the ARTS1 gene, which maps to human chromosome 5q15. ERAP1 is thought to inactivate several bioactive peptides, including angioten-sin II, and subsequently, may be involved in the regulation of blood pressure. It may have a role in angiogenesis by regulating the proliferation and migration of endothelial cells, and is characterized as a TNFR1 binding protein that promotes TNFR1 shedding.