endoplasmic reticulum aminopeptidase 1; ARTS-1; adipocyte-derived leucine aminopeptidase; A-LAP; aminopeptidase PILS; puromycin-insensitive leucyl-specific aminopeptidase; PILS-AP; type 1 tumor necrosis factor receptor shedding aminopeptidase regulator (ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154)

Function

• aminopeptidase
• role in peptide trimming
• strongly prefers substrates 9-16 residues long
• rapidly degrades 13-mer to a 9-mer & then stops
• preferentially hydrolyzes the residue Leu & peptides with a hydrophobic C-terminus
• weak activity toward peptides with charged C-terminus
• may play a role in inactivation of peptide hormones
• may be involved in regulation of blood pressure through the inactivation of angiotensin II &/or the generation of bradykinin in the kidney
• release of an N-terminal amino acid, Xaa-|-Xbb-, in which Xaa is preferably Leu, but may be other amino acids including Met, cys & Phe

Cofactor: binds 1 Zn+2 per subunit (putative)

Structure

• monomer
• may also exist as a heterodimer, with ERAP2
• N-glycosylated
• belongs to the peptidase M1 family

Compartment

endoplasmic reticulum membrane

Alternative splicing

named isoforms=2

Expression

• ubiquitous
• induced by IFN-gamma

Notes

• uncertain whether Met-1 or Met-13 is the initiator

More general terms

• aminopeptidase
• metalloprotein
• glycoprotein

Additional terms

• endoplasmic reticulum aminopeptidase (ERAP)

Database

• OMIM: https://mirror.omim.org/entry/606832
• Kegg: http://www.genome.jp/dbget-bin/www_bget?hsa:5175
• UniProt: http://www.uniprot.org/uniprot/Q9NZ08.html