NLN (gene)

Neurolysin (metallopeptidase M3 family)
PDB rendering based on 1i1i.
Available structures PDB 1i1i, 2o3e
Identifiers
Symbols	NLN; AGTBP; DKFZp564F123; EP24.16; FLJ23002; KIAA1226; MEP; MOP
External IDs	OMIM: 611530 MGI: 1923055 HomoloGene: 69315 GeneCards: NLN Gene
EC number	3.4.24.16
Gene Ontology Molecular function • metalloendopeptidase activity • peptidase activity • metal ion binding Cellular component • cytoplasm • mitochondrion • mitochondrial intermembrane space Biological process • proteolysis Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	57486	75805
Ensembl	ENSG00000123213	ENSMUSG00000021710
UniProt	Q9BYT8	n/a
RefSeq (mRNA)	NM_020726	NM_029447.2
RefSeq (protein)	NP_065777	NP_083723.1
Location (UCSC)	Chr 5: 65.02 – 65.17 Mb	Chr 13: 104.81 – 104.9 Mb
PubMed search	[1]	[2]

Neurolysin, mitochondrial is a protein that in humans is encoded by the NLN gene.^[1][2]

References

1. ^ Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O (Jan 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. doi:10.1093/dnares/6.5.337. PMID 10574462. 
2. ^ "Entrez Gene: NLN neurolysin (metallopeptidase M3 family)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57486. 

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. doi:10.1093/dnares/9.3.99. PMID 12168954. 
• 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. doi:10.1074/jbc.270.5.2092. PMID 7836437. 
• 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. doi:10.1016/0006-8993(95)01260-5. PMID 8869556. 
• 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. doi:10.1046/j.1471-4159.1997.68020837.x. PMID 9003076. 
• 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. doi:10.1002/(SICI)1097-4644(19970901)66:3<297::AID-JCB3>3.0.CO;2-K. PMID 9257187. 
• 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. 
• 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. 
• 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. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• 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. 
• 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. 
• 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. 
• 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.