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endoplasmic reticulum aminopeptidase 2 (leukocyte-derived arginine aminopeptidase, L-RAP, ERAP2, LRAP)

Function: - aminopeptidase - role in peptide trimming - preferentially hydrolyzes the basic residues Arg & Lys heterodimer; with ERAP1 Cofactor: binds 1 Zn+2 per subunit (putative) Structure: - N-glycosylated - belongs to the peptidase M1 family Compartment: - endoplasmic reticulum membrane Alternative splicing: named isoforms=4 Expression: - ubiquitously expressed - highly expressed in spleen & leukocytes - induced by IFN-gamma Pathology: - defects in the expression of this gene may cause improper antigen processing, possibly leading to favor tumor escape from the immune surveillance

Related

endoplasmic reticulum aminopeptidase (ERAP)

General

aminopeptidase glycoprotein membrane protein

Properties

SIZE: entity length = 960 aa MW = 110 kD COMPARTMENT: endoplasmic reticulum MOTIF: transmembrane domain {21-40} N-glycosylation site {N85} N-glycosylation site {N119} Zn+2-binding site SITE: 370-370 glutamate residue {E371} Zn+2-binding site SITE: 374-374 N-glycosylation site {N405} tyrosine residue {Y455}

Database Correlations

UniProt Q6P179 Pfam PF01433

References

UniProt :accession Q6P179