LGMN
Description
The LGMN (legumain) is a protein-coding gene located on chromosome 14.
Legumain is a protein encoded by the LGMN gene in humans. It is a cysteine protease with a high specificity for cleaving asparaginyl bonds. This enzyme is involved in processing bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Legumain activation occurs under acidic conditions and is autocatalytic. Expression of the protein occurs after monocytes differentiate into dendritic cells, and a fully mature, active enzyme is produced following lipopolysaccharide expression in mature dendritic cells. Overexpression of this gene may be associated with most solid tumor types. A pseudogene of this gene exists on chromosome 13. While several alternatively spliced transcript variants have been described, only two have been confirmed biologically. These two variants encode the same isoform.
Legumain exhibits a high specificity for cleaving asparaginyl bonds (PubMed:23776206). It can also cleave aspartyl bonds, albeit at a slower rate, especially under acidic conditions (PubMed:23776206). Legumain plays a crucial role in processing proteins for MHC class II antigen presentation within the lysosomal/endosomal system (PubMed:9872320). Additionally, it participates in MHC class I antigen presentation in cross-presenting dendritic cells by mediating the cleavage and maturation of Perforin-2 (MPEG1), facilitating antigen translocation in the cytosol (By similarity). Legumain is essential for normal lysosomal protein degradation in renal proximal tubules (By similarity) and for the proper degradation of internalized EGFR (By similarity). Its role in EGFR degradation contributes to the regulation of cell proliferation (By similarity). {ECO:0000250|UniProtKB:O89017, ECO:0000269|PubMed:23776206, ECO:0000269|PubMed:9872320}
LGMN is also known as AEP, LGMN1, PRSC1.
