LGMN

LGMN
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4N6N, 4N6O, 4FGU, 4AWB, 4AWA, 4AW9
Identifiers
Aliases	LGMN , AEP, LGMN1, PRSC1, legumain
External IDs	OMIM: 602620 MGI: 1330838 HomoloGene: 38075 GeneCards: LGMN
Gene location (Human) Chr. Chromosome 14 (human) [1] Band 14q32.12 Start 92,703,807 bp [1] End 92,748,679 bp [1]
Gene location (Mouse) Chr. Chromosome 12 (mouse) [2] Band 12|12 E Start 102,360,343 bp [2] End 102,406,072 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in synovial joint gallbladder synovial membrane right coronary artery left lobe of thyroid gland placenta rectum right lobe of thyroid gland spleen oocyte Top expressed in yolk sac kidney calvaria saccule proximal tubule Ankle joint superior frontal gyrus pontine nuclei utricle primitive streak More reference expression data BioGPS More reference expression data
Gene ontology Molecular function cysteine-type peptidase activity peptidase activity hydrolase activity cysteine-type endopeptidase activity tau protein binding Cellular component late endosome apical part of cell lysosomal lumen lysosome extracellular exosome endolysosome lumen extracellular region cytoplasm perinuclear region of cytoplasm Biological process negative regulation of neuron apoptotic process negative regulation of ERBB signaling pathway renal system process antigen processing and presentation of exogenous peptide antigen via MHC class II vitamin D metabolic process negative regulation of multicellular organism growth vacuolar protein processing receptor catabolic process proteolysis toll-like receptor signaling pathway proteolysis involved in cellular protein catabolic process response to acidic pH memory positive regulation of cell population proliferation associative learning negative regulation of gene expression cellular response to hepatocyte growth factor stimulus positive regulation of mitotic cell cycle cellular response to calcium ion positive regulation of monocyte chemotaxis dendritic spine organization activation of cysteine-type endopeptidase activity self proteolysis positive regulation of long-term synaptic potentiation cellular response to amyloid-beta positive regulation of endothelial cell chemotaxis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5641 19141 Ensembl ENSG00000100600 ENSMUSG00000021190 UniProt Q99538 O89017 RefSeq (mRNA) NM_001008530 NM_005606 NM_001363696 NM_001363699 NM_011175 NM_001378875 RefSeq (protein) NP_001008530 NP_005597 NP_001350625 NP_001350628 NP_035305 NP_001365804 Location (UCSC) Chr 14: 92.7 – 92.75 Mb Chr 12: 102.36 – 102.41 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Legumain is a protein that in humans is encoded by the LGMN gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000100600 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021190 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "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. doi:10.1042/bj3350111. 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. S2CID   32702742.
• 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. S2CID   4352065.
• 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. S2CID   46043484.
• Chen JM, Fortunato M, Barrett AJ (2001). "Activation of human prolegumain by cleavage at a C-terminal asparagine residue". Biochem. J. 352 (2): 327–34. doi:10.1042/bj3520327. 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. Bibcode:2002PNAS...9916899M. 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. S2CID   69278.