Recombinant Human Legumain(LGMN)

Function

Has a strict specificity for hydrolysis of asparaginyl bonds (PubMed:23776206). Can also cleave aspartyl bonds slowly, especially under acidic conditions (PubMed:23776206). Involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system (PubMed:9872320). Also involved in MHC class I antigen presentation in cross-presenting dendritic cells by mediating cleavage and maturation of Perforin-2 (MPEG1), thereby promoting antigen translocation in the cytosol (By similarity). Required for normal lysosomal protein degradation in renal proximal tubules (By similarity). Required for normal degradation of internalized EGFR (By similarity). Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity)

Subcellular Location

Lysosome

Tissue Specificity

Ubiquitous. Particularly abundant in kidney, heart and placenta

Subunit

Homodimer before autocatalytic removal of the propeptide (PubMed:23776206). Monomer after autocatalytic processing (PubMed:23776206). May interact with integrins (PubMed:23776206)

• Chen J.-M. et al. Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase. — J. Biol. Chem. (1997)
• Tanaka T. et al. Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and its chromosome assignment to 14q32.1. — Cytogenet. Cell Genet. (1996)
• Li W.B. et al. Full-length cDNA libraries and normalization. (JAN-)
• Heilig R. et al. The DNA sequence and analysis of human chromosome 14. — Nature (2003)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Chen J.-M. et al. Activation of human prolegumain by cleavage at a C-terminal asparagine residue. — Biochem. J. (2000)
• Manoury B. et al. An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation. — Nature (1998)
• Halfon S. et al. Autocatalytic activation of human legumain at aspartic acid residues. — FEBS Lett. (1998)