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 Note: - uncertain whether Met-1 or Met-13 is the initiator

General

aminopeptidase glycoprotein metalloprotein

Properties

SIZE: entity length = 941 aa MW = 107 kD COMPARTMENT: endoplasmic reticulum MOTIF: transmembrane domain {2-21} N-glycosylation site {N70} N-glycosylation site {N154} Zn+2-binding site SITE: 353-353 glutamate residue {E354} Zn+2-binding site SITE: 357-357 N-glycosylation site {N414} tyrosine residue {Y438} Zn+2-binding site SITE: 476-476 N-glycosylation site {N760} N-glycosylation site {N901}

Database Correlations

OMIM 606832 UniProt Q9NZ08 Pfam PF01433 Kegg hsa:5175

References

UniProt :accession Q9HAU8