Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates. Major histocompatibility complex (MHC) class I molecules rely on aminopeptidases such as ERAP1 (MIM 606832) and LRAP to trim precursors to antigenic peptides in the endoplasmic reticulum (ER) following cleavage in the cytoplasm by tripeptidyl peptidase II (TPP2; MIM 190470) (Tanioka et al., 2003 [PubMed 12799365]).[supplied by OMIM, Mar 2008]
Function:
ERAP2 is an aminopeptidase that plays a central role in peptide trimming. Major histocompatibility complex (MHC) class I molecules rely on aminopeptidases such as ERAP2 to trim precursors to antigenic peptides in the endoplasmic reticulum (ER) following cleavage in the cytoplasm by tripeptidyl peptidase II. ERAP2 preferentially hydrolyzes the basic residues Arg and Lys.
Subcellular Location:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Similarity:
Belongs to the mut-7 family.
Contains 1 3'-5' exonuclease domain.
SWISS:
Q6P179
Gene ID:
64167
Database links:
Entrez Gene: 64167 Human
Omim: 609497 Human
SwissProt: Q6P179 Human
Unigene: 482910 Human
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