Aminopeptidase PILS/ARTS1 Products

Description

The endoplasmic reticulum (ER) aminopeptidase 1 (ERAP1) is a 120 kDa protein localized to the lumen of the ER, which removes NH2-terminal residues from many antigenic precursors for MHC class I peptide presentation. Peptides that are presented by MHC class I on the surface of a cell must be 8-11 residues long, and ERAP1 specifically trims peptides of 9 amino acids or more. ERAP1 is also induced by interferon-gamma. The gene encoding human ERAP1 maps to chromosome 5q15. ERAP1 has previously been characterized as adipocyte-derived leucine aminopeptidase (A-LAP), puromycin-insensitive leucine-specific aminopeptidase (PILS-AP) and aminopeptidase regulator of TNFR1 shedding (ARTS-1). A-LAP is thought to inactivate several bioactive peptides, including angiotensin II and, subsequently, may be involved in the regulation of blood pressure. PILS-AP is described as playing a role in angiogenesis by regulating the proliferation and migration of endothelial cells, and ARTS-1 is characterized as a TNFR1 binding protein that promotes TNFR1 shedding. Further research will be necessary to fully elucidate the functions of this protein.

Bioinformatics

Product By Gene ID

51752

Alternate Names

Adipocyte-derived leucine aminopeptidase A-LAP A-LAPALAP Aminopeptidase PILS ARTS1 ARTS1aminopeptidase regulator of TNFR1 shedding ARTS-1PILSAP EC 3.4.11 EC 3.4.11.- EC 3.4.11.1 endoplasmic reticulum aminopeptidase 1 endoplasmic reticulum aminopeptidase associated with antigen processing ERAAP1 ERAP1 KIAA0525APPILS PILS-AP PILS-APERAAP Puromycin-insensitive leucyl-specific aminopeptidase Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator

Research Areas for Aminopeptidase PILS/ARTS1

Find related products by research area and learn more about each of the different research areas below.

Angiogenesis
Cardiovascular Biology
Cell Biology
Immunology