LGMN: Difference between revisions

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Latest revision as of 17:54, 2 September 2017

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

↑ 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.
↑ 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.
↑ ^3.0 ^3.1 "Entrez Gene: LGMN legumain".

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 (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. 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.

This article on a gene on human chromosome 14 is a stub. You can help Wikipedia by expanding it.

[pmid8893817-1] 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.

[pmid9065484-2] 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.

[entrez-3] 3.0 ^3.1 "Entrez Gene: LGMN legumain".

[1]

[2]

[3]

@@ Line 1: / Line 1: @@
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+{{Infobox_gene}}
-{{GNF_Protein_box
+'''Legumain''' is a [[protein]] that in humans is encoded by the ''LGMN'' [[gene]].<ref name="pmid8893817">{{cite journal |vauthors=Tanaka T, Inazawa J, Nakamura Y | title = Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and its chromosome assignment to 14q32.1 | journal = Cytogenet Cell Genet | volume = 74 | issue = 1–2 | pages = 120–3 |date=Dec 1996 | pmid = 8893817 | pmc =  | doi =10.1159/000134397  }}</ref><ref name="pmid9065484">{{cite journal |vauthors=Chen JM, Dando PM, Rawlings ND, Brown MA, Young NE, Stevens RA, Hewitt E, Watts C, Barrett AJ | title = Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase | journal = J Biol Chem | volume = 272 | issue = 12 | pages = 8090–8 |date=Apr 1997 | pmid = 9065484 | pmc =  | doi =10.1074/jbc.272.12.8090  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LGMN legumain| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5641| accessdate = }}</ref>
- | image =
- | image_source =
- | PDB =
- | Name = Legumain
- | HGNCid = 9472
- | Symbol = LGMN
- | AltSymbols =; AEP; LGMN1; PRSC1
- | OMIM = 602620
- | ECnumber =
- | Homologene = 38075
- | MGIid = 1330838
-  | GeneAtlas_image1 = PBB_GE_LGMN_201212_at_tn.png
-  | Function = {{GNF_GO|id=GO:0001509 |text = legumain activity}}
- | Component = {{GNF_GO|id=GO:0005764 |text = lysosome}} {{GNF_GO|id=GO:0005770 |text = late endosome}} {{GNF_GO|id=GO:0045177 |text = apical part of cell}}
- | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0040015 |text = negative regulation of body size}}
- | Orthologs = {{GNF_Ortholog_box
-    | Hs_EntrezGene = 5641
-    | Hs_Ensembl = ENSG00000100600
-    | Hs_RefseqProtein = NP_001008530
-    | Hs_RefseqmRNA = NM_001008530
-    | Hs_GenLoc_db =
-    | Hs_GenLoc_chr = 14
-    | Hs_GenLoc_start = 92239910
-    | Hs_GenLoc_end = 92284765
-    | Hs_Uniprot = Q99538
-    | Mm_EntrezGene = 19141
-    | Mm_Ensembl = ENSMUSG00000021190
-    | Mm_RefseqmRNA = NM_011175
-    | Mm_RefseqProtein = NP_035305
-    | Mm_GenLoc_db =
-    | Mm_GenLoc_chr = 12
-    | Mm_GenLoc_start = 102795144
-    | Mm_GenLoc_end = 102840747
-    | Mm_Uniprot = Q3UE99
-  }}
-}}
-'''Legumain''', also known as '''LGMN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LGMN legumain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5641| accessdate = }}</ref>
 <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
 {{PBB_Summary
 | section_title =
-| summary_text = This gene encodes a cysteine protease 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.<ref name="entrez">{{cite web | title = Entrez Gene: LGMN legumain| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5641| accessdate = }}</ref>
+| summary_text = 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.<ref name="entrez" />
 }}
 ==References==
-{{reflist|2}}
+{{reflist}}
 ==Further reading==
 {{refbegin | 2}}
 {{PBB_Further_reading
 | citations =
-*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
+*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
-*{{cite journal  | author=Tanaka T, Inazawa J, Nakamura Y |title=Molecular cloning of a human cDNA encoding putative cysteine protease (PRSC1) and its chromosome assignment to 14q32.1. |journal=Cytogenet. Cell Genet. |volume=74 |issue= 1-2 |pages= 120-3 |year= 1996 |pmid= 8893817 |doi=  }}
+*{{cite journal  | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |name-list-format=vanc| author2=Yoshitomo-Nakagawa K  | author3=Maruyama K  | display-authors=3  | last4=Suyama  | first4=A  | last5=Sugano  | first5=S  }}
-*{{cite journal  | author=Chen JM, Dando PM, Rawlings ND, ''et al.'' |title=Cloning, isolation, and characterization of mammalian legumain, an asparaginyl endopeptidase. |journal=J. Biol. Chem. |volume=272 |issue= 12 |pages= 8090-8 |year= 1997 |pmid= 9065484 |doi=  }}
+*{{cite journal  | author=Chen JM |title=Cloning and expression of mouse legumain, a lysosomal endopeptidase |journal=Biochem. J. |volume=335 |issue=  Pt 1|pages= 111–7 |year= 1998 |pmid= 9742219 |doi=  | pmc=1219758  |name-list-format=vanc| author2=Dando PM  | author3=Stevens RA  | display-authors=3  | last4=Fortunato  | first4=M  | last5=Barrett  | first5=AJ  }}
-*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
+*{{cite journal  | author=Halfon S |title=Autocatalytic activation of human legumain at aspartic acid residues |journal=FEBS Lett. |volume=438 |issue= 1–2 |pages= 114–8 |year= 1998 |pmid= 9821970 |doi=10.1016/S0014-5793(98)01281-2  |name-list-format=vanc| author2=Patel S  | author3=Vega F  | display-authors=3  | last4=Zurawski  | first4=S  | last5=Zurawski  | first5=G  }}
-*{{cite journal  | author=Chen JM, Dando PM, Stevens RA, ''et al.'' |title=Cloning and expression of mouse legumain, a lysosomal endopeptidase. |journal=Biochem. J. |volume=335 ( Pt 1) |issue=  |pages= 111-7 |year= 1998 |pmid= 9742219 |doi=  }}
+*{{cite journal  | author=Manoury B |title=An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation |journal=Nature |volume=396 |issue= 6712 |pages= 695–9 |year= 1999 |pmid= 9872320 |doi= 10.1038/25379  |name-list-format=vanc| author2=Hewitt EW  | author3=Morrice N  | display-authors=3  | last4=Morrice  | first4=Nick  | last5=Dando  | first5=Pam M.  | last6=Barrett  | first6=Alan J. }}
-*{{cite journal  | author=Halfon S, Patel S, Vega F, ''et al.'' |title=Autocatalytic activation of human legumain at aspartic acid residues. |journal=FEBS Lett. |volume=438 |issue= 1-2 |pages= 114-8 |year= 1998 |pmid= 9821970 |doi=  }}
+*{{cite journal  |vauthors=Chen JM, Rawlings ND, Stevens RA, Barrett AJ |title=Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases |journal=FEBS Lett. |volume=441 |issue= 3 |pages= 361–5 |year= 1999 |pmid= 9891971 |doi=10.1016/S0014-5793(98)01574-9  }}
-*{{cite journal  | author=Manoury B, Hewitt EW, Morrice N, ''et al.'' |title=An asparaginyl endopeptidase processes a microbial antigen for class II MHC presentation. |journal=Nature |volume=396 |issue= 6712 |pages= 695-9 |year= 1999 |pmid= 9872320 |doi= 10.1038/25379 }}
+*{{cite journal  |vauthors=Chen JM, Fortunato M, Barrett AJ |title=Activation of human prolegumain by cleavage at a C-terminal asparagine residue |journal=Biochem. J. |volume=352 |issue=  2|pages= 327–34 |year= 2001 |pmid= 11085925 |doi= 10.1042/bj3520327| pmc=1221463  }}
-*{{cite journal  | author=Chen JM, Rawlings ND, Stevens RA, Barrett AJ |title=Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine endopeptidases. |journal=FEBS Lett. |volume=441 |issue= 3 |pages= 361-5 |year= 1999 |pmid= 9891971 |doi=  }}
+*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
-*{{cite journal  | author=Chen JM, Fortunato M, Barrett AJ |title=Activation of human prolegumain by cleavage at a C-terminal asparagine residue. |journal=Biochem. J. |volume=352 Pt 2 |issue=  |pages= 327-34 |year= 2001 |pmid= 11085925 |doi=  }}
+*{{cite journal  | author=Li DN |title=Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo |journal=J. Biol. Chem. |volume=278 |issue= 40 |pages= 38980–90 |year= 2003 |pmid= 12860980 |doi= 10.1074/jbc.M305930200  |name-list-format=vanc| author2=Matthews SP  | author3=Antoniou AN  | display-authors=3  | last4=Mazzeo  | first4=D  | last5=Watts  | first5=C }}
-*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
+*{{cite journal  | author=Burster T |title=Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes |journal=J. Immunol. |volume=172 |issue= 9 |pages= 5495–503 |year= 2004 |pmid= 15100291 |doi=  10.4049/jimmunol.172.9.5495|name-list-format=vanc| author2=Beck A  | author3=Tolosa E  | display-authors=3  | last4=Marin-Esteban  | first4=V  | last5=Rötzschke  | first5=O  | last6=Falk  | first6=K  | last7=Lautwein  | first7=A  | last8=Reich  | first8=M  | last9=Brandenburg  | first9=J  }}
-*{{cite journal  | author=Li DN, Matthews SP, Antoniou AN, ''et al.'' |title=Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo. |journal=J. Biol. Chem. |volume=278 |issue= 40 |pages= 38980-90 |year= 2003 |pmid= 12860980 |doi= 10.1074/jbc.M305930200 }}
+*{{cite journal  | author=Gerhard DS |title=The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
-*{{cite journal  | author=Burster T, Beck A, Tolosa E, ''et al.'' |title=Cathepsin G, and not the asparagine-specific endoprotease, controls the processing of myelin basic protein in lysosomes from human B lymphocytes. |journal=J. Immunol. |volume=172 |issue= 9 |pages= 5495-503 |year= 2004 |pmid= 15100291 |doi=  }}
+*{{cite journal  | author=Murthy RV |title=Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer |journal=Clin. Cancer Res. |volume=11 |issue= 6 |pages= 2293–9 |year= 2005 |pmid= 15788679 |doi= 10.1158/1078-0432.CCR-04-1642  |name-list-format=vanc| author2=Arbman G  | author3=Gao J  | display-authors=3  | last4=Roodman  | first4=GD  | last5=Sun  | first5=XF }}
-*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
+*{{cite journal  | author=Oh JH |title=Transcriptome analysis of human gastric cancer |journal=Mamm. Genome |volume=16 |issue= 12 |pages= 942–54 |year= 2006 |pmid= 16341674 |doi= 10.1007/s00335-005-0075-2  |name-list-format=vanc| author2=Yang JO  | author3=Hahn Y  | display-authors=3  | last4=Kim  | first4=Mi-Rang  | last5=Byun  | first5=Sang-Soon  | last6=Jeon  | first6=Yeo-Jin  | last7=Kim  | first7=Jeong-Min  | last8=Song  | first8=Kyu-Sang  | last9=Noh  | first9=Seung-Moo }}
-*{{cite journal  | author=Murthy RV, Arbman G, Gao J, ''et al.'' |title=Legumain expression in relation to clinicopathologic and biological variables in colorectal cancer. |journal=Clin. Cancer Res. |volume=11 |issue= 6 |pages= 2293-9 |year= 2005 |pmid= 15788679 |doi= 10.1158/1078-0432.CCR-04-1642 }}
-*{{cite journal  | author=Oh JH, Yang JO, Hahn Y, ''et al.'' |title=Transcriptome analysis of human gastric cancer. |journal=Mamm. Genome |volume=16 |issue= 12 |pages= 942-54 |year= 2006 |pmid= 16341674 |doi= 10.1007/s00335-005-0075-2 }}
 }}
 {{refend}}
-{{protein-stub}}
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LGMN: Difference between revisions

Latest revision as of 17:54, 2 September 2017

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