NLN (gene)

Neurolysin (metallopeptidase M3 family)
File:PBB Protein NLN image.jpg PDB rendering based on 1i1i.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1i1i​, 2o3e​
Identifiers
Symbols	NLN ; AGTBP; DKFZp564F123; KIAA1226
External IDs	Template:MGI HomoloGene: 69315
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Neurolysin (metallopeptidase M3 family), also known as NLN, is a human gene.

Further reading

• Nakajima D, Okazaki N, Yamakawa H; et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. PMID 12168954.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Serizawa A, Dando PM, Barrett AJ (1995). "Characterization of a mitochondrial metallopeptidase reveals neurolysin as a homologue of thimet oligopeptidase". J. Biol. Chem. 270 (5): 2092–8. PMID 7836437.CS1 maint: Multiple names: authors list (link)
• Vincent B, Vincent JP, Checler F (1997). "Purification and characterization of human endopeptidase 3.4.24.16. Comparison with the porcine counterpart indicates a unique cleavage site on neurotensin". Brain Res. 709 (1): 51–8. PMID 8869556.CS1 maint: Multiple names: authors list (link)
• Vincent B, Dauch P, Vincent JP, Checler F (1997). "Stably transfected human cells overexpressing rat brain endopeptidase 3.4.24.16: biochemical characterization of the activity and expression of soluble and membrane-associated counterparts". J. Neurochem. 68 (2): 837–45. PMID 9003076.CS1 maint: Multiple names: authors list (link)
• Krause DR, Piva TJ, Brown SB, Ellem KA (1997). "Characterization and localization of mitochondrial oligopeptidase (MOP) (EC 3.4.24.16) activity in the human cervical adenocarcinoma cell line HeLa". J. Cell. Biochem. 66 (3): 297–308. PMID 9257187.CS1 maint: Multiple names: authors list (link)
• Rioli V, Kato A, Portaro FC; et al. (1998). "Neuropeptide specificity and inhibition of recombinant isoforms of the endopeptidase 3.4.24.16 family: comparison with the related recombinant endopeptidase 3.4.24.15". Biochem. Biophys. Res. Commun. 250 (1): 5–11. doi:10.1006/bbrc.1998.8941. PMID 9735321.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Garrido PA, Vandenbulcke F, Ramjaun AR; et al. (1999). "Confocal microscopy reveals thimet oligopeptidase (EC 3.4.24.15) and neurolysin (EC 3.4.24.16) in the classical secretory pathway". DNA Cell Biol. 18 (4): 323–31. doi:10.1089/104454999315385. PMID 10235115.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nagase T, Ishikawa K, Kikuno R; et al. (2000). "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (5): 337–45. PMID 10574462.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lew RA, Boulos E, Stewart KM; et al. (2001). "Bradykinin analogues with beta-amino acid substitutions reveal subtle differences in substrate specificity between the endopeptidases EC 3.4.24.15 and EC 3.4.24.16". J. Pept. Sci. 6 (9): 440–5. doi:10.1002/1099-1387(200009)6:9<440::AID-PSC280>3.0.CO;2-K. PMID 11016880.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Norman MU, Lew RA, Smith AI, Hickey MJ (2003). "Metalloendopeptidases EC 3.4.24.15/16 regulate bradykinin activity in the cerebral microvasculature". Am. J. Physiol. Heart Circ. Physiol. 284 (6): H1942–8. doi:10.1152/ajpheart.00948.2002. PMID 12586639.CS1 maint: Multiple names: authors list (link)
• Norman MU, Reeve SB, Dive V; et al. (2003). "Endopeptidases 3.4.24.15 and 24.16 in endothelial cells: potential role in vasoactive peptide metabolism". Am. J. Physiol. Heart Circ. Physiol. 284 (6): H1978–84. doi:10.1152/ajpheart.01116.2002. PMID 12609826.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lim EJ, Sampath S, Coll-Rodriguez J; et al. (2007). "Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase". J. Biol. Chem. 282 (13): 9722–32. doi:10.1074/jbc.M609897200. PMID 17251185.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)