LGMN

Legumain
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4AW9​, 4AWA​, 4AWB​, 4FGU​, 4N6N​, 4N6O​
Identifiers
Symbols	LGMN ; AEP; LGMN1; PRSC1
External IDs	OMIM: 602620 MGI: 1330838 HomoloGene: 38075 ChEMBL: 4244 GeneCards: LGMN Gene
EC number	3.4.22.34
Gene ontology Molecular function • cysteine-type endopeptidase activity • peptidase activity Cellular component • lysosome • late endosome • lysosomal lumen • apical part of cell • extracellular exosome Biological process • toll-like receptor signaling pathway • renal system process • proteolysis • steroid metabolic process • response to acidic pH • antigen processing and presentation of exogenous peptide antigen via MHC class II • receptor catabolic process • negative regulation of multicellular organism growth • vitamin D metabolic process • negative regulation of neuron apoptotic process • small molecule metabolic process • innate immune response • proteolysis involved in cellular protein catabolic process • negative regulation of ERBB signaling pathway Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5641	19141
Ensembl	ENSG00000100600	ENSMUSG00000021190
UniProt	Q99538	O89017
RefSeq (mRNA)	NM_001008530	NM_011175
RefSeq (protein)	NP_001008530	NP_035305
Location (UCSC)	Chr 14: 92.7 – 92.75 Mb	Chr 12: 102.39 – 102.44 Mb
PubMed search

Legumain is a protein that in humans is encoded by the LGMN gene.^[1][2][3]

This gene encodes a cysteine protease, legumain, that has a strict specificity for hydrolysis of asparaginyl bonds. This enzyme may be involved in the processing of bacterial peptides and endogenous proteins for MHC class II presentation in the lysosomal/endosomal systems. Enzyme activation is triggered by acidic pH and appears to be autocatalytic. Protein expression occurs after monocytes differentiate into dendritic cells. A fully mature, active enzyme is produced following lipopolysaccharide expression in mature dendritic cells. Overexpression of this gene may be associated with the majority of solid tumor types. This gene has a pseudogene on chromosome 13. Several alternatively spliced transcript variants have been described, but the biological validity of only two has been determined. These two variants encode the same isoform.^[3]

References

1. Tanaka T, Inazawa J, Nakamura Y (Dec 1996). "Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and its chromosome assignment to 14q32.1". Cytogenet Cell Genet 74 (1–2): 120–3. doi:10.1159/000134397. PMID 8893817.
2. Chen JM, Dando PM, Rawlings ND, Brown MA, Young NE, Stevens RA, Hewitt E, Watts C, Barrett AJ (Apr 1997). "Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase". J Biol Chem 272 (12): 8090–8. doi:10.1074/jbc.272.12.8090. PMID 9065484.
3. "Entrez Gene: LGMN legumain".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Chen JM, Dando PM, Stevens RA, et al. (1998). "Cloning and expression of mouse legumain, a lysosomal endopeptidase". Biochem. J. 335 (Pt 1): 111–7. PMC 1219758. PMID 9742219.
• Halfon S, Patel S, Vega F, et al. (1998). "Autocatalytic activation of human legumain at aspartic acid residues". FEBS Lett. 438 (1–2): 114–8. doi:10.1016/S0014-5793(98)01281-2. PMID 9821970.
• Manoury B, Hewitt EW, Morrice N, et al. (1999). "An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation". Nature 396 (6712): 695–9. doi:10.1038/25379. PMID 9872320.
• Chen JM, Rawlings ND, Stevens RA, Barrett AJ (1999). "Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases". FEBS Lett. 441 (3): 361–5. doi:10.1016/S0014-5793(98)01574-9. PMID 9891971.
• Chen JM, Fortunato M, Barrett AJ (2001). "Activation of human prolegumain by cleavage at a C-terminal asparagine residue". Biochem. J. 352 Pt 2 (Pt 2): 327–34. doi:10.1042/0264-6021:3520327. PMC 1221463. PMID 11085925.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Li DN, Matthews SP, Antoniou AN, et al. (2003). "Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo". J. Biol. Chem. 278 (40): 38980–90. doi:10.1074/jbc.M305930200. PMID 12860980.
• Burster T, Beck A, Tolosa E, et al. (2004). "Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes". J. Immunol. 172 (9): 5495–503. doi:10.4049/jimmunol.172.9.5495. PMID 15100291.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Murthy RV, Arbman G, Gao J, et al. (2005). "Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer". Clin. Cancer Res. 11 (6): 2293–9. doi:10.1158/1078-0432.CCR-04-1642. PMID 15788679.
• Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.