| Primary Identifier | IPR033528 | Type | Family |
| Short Name | ERAP2 |
| description | The ERAP2 aminopeptidase (endoplasmic reticulum aminopeptidase 2; MEROPS identifier M01.024) releases an amino acid from the N terminus of a peptide or protein but is unable to cleave Xaa-Pro and Pro-Xaa bonds. Preferentially, arginyl bonds are hydrolysed most efficiantly, followed by lysyl bonds []. ERAP2 is localized to the endoplasmic reticulum of B lymphocytes []and epithelial components of non-lymphoid tissue.Human ERAP1 and 2 co-localize in breast, endometrium, epididymus and ovary, whereas ERAP2 only is found in kidney, gall bladder and urinary bladder []. ERAP2 is important for antigen presentation on the cell surface by the major histocompatabiity complex (MHC). The proteasome degrades cytoplasmic proteins and generates peptides. Some of these peptides are transported to the lumen of the endoplasmic reticulum by a transport associated with antigen presntation (TAP). Trimming at the amino terminus by the aminopeptidases ERAP1 and ERAP2 generates a peptide of the correct length which can then associate with the MHC [, ]. Polymorphisms of ERAP2 have been implicated in ankylosing spondylitis [], Crohn's disease []and pre-eclampsia []. |
