Alpha-N-acetylglucosaminidase

Details

Name
Alpha-N-acetylglucosaminidase
Synonyms
  • 3.2.1.50
  • N-acetyl-alpha-glucosaminidase
  • NAG
  • UFHSD1
Gene Name
NAGLU
UniProtKB Entry
P54802Swiss-Prot
Organism
Humans
NCBI Taxonomy ID
9606
Amino acid sequence
>lcl|BSEQ0016076|Alpha-N-acetylglucosaminidase
MEAVAVAAAVGVLLLAGAGGAAGDEAREAAAVRALVARLLGPGPAADFSVSVERALAAKP
GLDTYSLGGGGAARVRVRGSTGVAAAAGLHRYLRDFCGCHVAWSGSQLRLPRPLPAVPGE
LTEATPNRYRYYQNVCTQSYSFVWWDWARWEREIDWMALNGINLALAWSGQEAIWQRVYL
ALGLTQAEINEFFTGPAFLAWGRMGNLHTWDGPLPPSWHIKQLYLQHRVLDQMRSFGMTP
VLPAFAGHVPEAVTRVFPQVNVTKMGSWGHFNCSYSCSFLLAPEDPIFPIIGSLFLRELI
KEFGTDHIYGADTFNEMQPPSSEPSYLAAATTAVYEAMTAVDTEAVWLLQGWLFQHQPQF
WGPAQIRAVLGAVPRGRLLVLDLFAESQPVYTRTASFQGQPFIWCMLHNFGGNHGLFGAL
EAVNGGPEAARLFPNSTMVGTGMAPEGISQNEVVYSLMAELGWRKDPVPDLAAWVTSFAA
RRYGVSHPDAGAAWRLLLRSVYNCSGEACRGHNRSPLVRRPSLQMNTSIWYNRSDVFEAW
RLLLTSAPSLATSPAFRYDLLDLTRQAVQELVSLYYEEARSAYLSKELASLLRAGGVLAY
ELLPALDEVLASDSRFLLGSWLEQARAAAVSEAEADFYEQNSRYQLTLWGPEGNILDYAN
KQLAGLVANYYTPRWRLFLEALVDSVAQGIPFQQHQFDKNVFQLEQAFVLSKQRYPSQPR
GDTVDLAKKIFLKYYPRWVAGSW
Number of residues
743
Molecular Weight
82264.92
Theoretical pI
6.52
GO Classification
Processes
adult behavior / amyloid precursor protein metabolic process / aorta morphogenesis / astrocyte activation / autophagy / cardiac muscle cell development / cell surface receptor signaling pathway via STAT / cellular lipid catabolic process / cellular response to organic cyclic compound / cellular response to oxidative stress / collagen metabolic process / cone retinal bipolar cell differentiation / cytoplasm organization / determination of adult lifespan / endothelium development / exploration behavior / ganglioside metabolic process / Golgi organization / hair follicle morphogenesis / heparan sulfate proteoglycan catabolic process / heparan sulfate proteoglycan metabolic process / heparin metabolic process / hormone metabolic process / left ventricular cardiac muscle tissue morphogenesis / limb development / liver development / maintenance of blood-brain barrier / microglia differentiation / microglial cell activation / mitral valve morphogenesis / motor behavior / multicellular organismal-level iron ion homeostasis / nerve development / proteasome-mediated ubiquitin-dependent protein catabolic process / protein processing / response to disaccharide / response to lipopolysaccharide / response to wounding / rod bipolar cell differentiation / sequestering of iron ion / superoxide metabolic process / toll-like receptor 4 signaling pathway / vesicle tethering
General Function
Involved in the degradation of heparan sulfate
Specific Function
alpha-N-acetylglucosaminidase activity
Pfam Domain Function
Signal Regions
1-23
Transmembrane Regions
Not Available
Cellular Location
Lysosome
Gene sequence
>lcl|BSEQ0016077|Alpha-N-acetylglucosaminidase (NAGLU)
ATGGAGGCGGTGGCGGTGGCCGCGGCGGTGGGGGTCCTTCTCCTGGCCGGGGCCGGGGGC
GCGGCAGGCGACGAGGCCCGGGAGGCGGCGGCCGTGCGGGCGCTCGTGGCCCGGCTGCTG
GGGCCAGGCCCCGCGGCCGACTTCTCCGTGTCGGTGGAGCGCGCTCTGGCTGCCAAGCCG
GGCTTGGACACCTACAGCCTGGGCGGCGGCGGCGCGGCGCGCGTGCGGGTGCGCGGCTCC
ACGGGCGTGGCGGCCGCCGCGGGGCTGCACCGCTACCTGCGCGACTTCTGTGGCTGCCAC
GTGGCCTGGTCCGGCTCTCAGCTGCGCCTGCCGCGGCCACTGCCAGCCGTGCCGGGGGAG
CTGACCGAGGCCACGCCCAACAGGTACCGCTATTACCAGAATGTGTGCACGCAAAGCTAC
TCTTTCGTGTGGTGGGACTGGGCCCGCTGGGAGCGAGAGATAGACTGGATGGCGCTGAAT
GGCATCAACCTGGCACTGGCCTGGAGCGGCCAGGAGGCCATCTGGCAGCGGGTGTACCTG
GCCTTGGGCCTGACCCAGGCAGAGATCAATGAGTTCTTTACTGGTCCTGCCTTCCTGGCC
TGGGGGCGAATGGGCAACCTGCACACCTGGGATGGCCCCCTGCCCCCCTCCTGGCACATC
AAGCAGCTTTACCTGCAGCACCGGGTCCTGGACCAGATGCGCTCCTTCGGCATGACCCCA
GTGCTGCCTGCATTCGCGGGGCATGTTCCCGAGGCTGTCACCAGGGTGTTCCCTCAGGTC
AATGTCACGAAGATGGGCAGTTGGGGCCACTTTAACTGTTCCTACTCCTGCTCCTTCCTT
CTGGCTCCGGAAGACCCCATATTCCCCATCATCGGGAGCCTCTTCCTGCGAGAGCTGATC
AAAGAGTTTGGCACAGACCACATCTATGGGGCCGACACTTTCAATGAGATGCAGCCACCT
TCCTCAGAGCCCTCCTACCTTGCCGCAGCCACCACTGCCGTCTATGAGGCCATGACTGCA
GTGGATACTGAGGCTGTGTGGCTGCTCCAAGGCTGGCTCTTCCAGCACCAGCCGCAGTTC
TGGGGGCCCGCCCAGATCAGGGCTGTGCTGGGAGCTGTGCCCCGTGGCCGCCTCCTGGTT
CTGGACCTGTTTGCTGAGAGCCAGCCTGTGTATACCCGCACTGCCTCCTTCCAGGGCCAG
CCCTTCATCTGGTGCATGCTGCACAACTTTGGGGGAAACCATGGTCTTTTTGGAGCCCTA
GAGGCTGTGAACGGAGGCCCAGAAGCTGCCCGCCTCTTCCCCAACTCCACCATGGTAGGC
ACGGGCATGGCCCCCGAGGGCATCAGCCAGAACGAAGTGGTCTATTCCCTCATGGCTGAG
CTGGGCTGGCGAAAGGACCCAGTGCCAGATTTGGCAGCCTGGGTGACCAGCTTTGCCGCC
CGGCGGTATGGGGTCTCCCACCCGGACGCAGGGGCAGCGTGGAGGCTACTGCTCCGGAGT
GTGTACAACTGCTCCGGGGAGGCCTGCAGGGGCCACAATCGTAGCCCGCTGGTCAGGCGG
CCGTCCCTACAGATGAATACCAGCATCTGGTACAACCGATCTGATGTGTTTGAGGCCTGG
CGGCTGCTGCTCACATCTGCTCCCTCCCTGGCCACCAGCCCCGCCTTCCGCTACGACCTG
CTGGACCTCACTCGGCAGGCAGTGCAGGAGCTGGTCAGCTTGTACTATGAGGAGGCAAGA
AGCGCCTACCTGAGCAAGGAGCTGGCCTCCCTGTTGAGGGCTGGAGGCGTCCTGGCCTAT
GAGCTGCTGCCGGCACTGGACGAGGTGCTGGCTAGTGACAGCCGCTTCTTGCTGGGCAGC
TGGCTAGAGCAGGCCCGAGCAGCGGCAGTCAGTGAGGCCGAGGCCGATTTCTACGAGCAG
AACAGCCGCTACCAGCTGACCTTGTGGGGGCCAGAAGGCAACATCCTGGACTATGCCAAC
AAGCAGCTGGCGGGGTTGGTGGCCAACTACTACACCCCTCGCTGGCGGCTTTTCCTGGAG
GCGCTGGTTGACAGTGTGGCCCAGGGCATCCCTTTCCAACAGCACCAGTTTGACAAAAAT
GTCTTCCAACTGGAGCAGGCCTTCGTTCTCAGCAAGCAGAGGTACCCCAGCCAGCCGCGA
GGAGACACTGTGGACCTGGCCAAGAAGATCTTCCTCAAATATTACCCCCGCTGGGTGGCC
GGCTCTTGGTGA
Chromosome Location
17
Locus
17q21.2
External Identifiers
ResourceLink
UniProtKB IDP54802
UniProtKB Entry NameANAG_HUMAN
GenBank Protein ID1171229
GenBank Gene IDU43572
GeneCard IDNAGLU
GenAtlas IDNAGLU
HGNC IDHGNC:7632
PDB ID(s)4XWH
KEGG IDhsa:4669
NCBI Gene ID4669
General References
  1. Zhao HG, Li HH, Bach G, Schmidtchen A, Neufeld EF: The molecular basis of Sanfilippo syndrome type B. Proc Natl Acad Sci U S A. 1996 Jun 11;93(12):6101-5. [Article]
  2. Weber B, Blanch L, Clements PR, Scott HS, Hopwood JJ: Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B). Hum Mol Genet. 1996 Jun;5(6):771-7. [Article]
  3. Zhao Z, Yazdani A, Shen Y, Sun Z, Bailey J, Caskey CT, Lee CC: Molecular dissection of a cosmid from a gene-rich region in 17q21 and characterization of a candidate gene for alpha-N-acetylglucosaminidase with two cDNA isoforms. Mamm Genome. 1996 Sep;7(9):686-90. [Article]
  4. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [Article]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [Article]
  7. Tetreault M, Gonzalez M, Dicaire MJ, Allard P, Gehring K, Leblanc D, Leclerc N, Schondorf R, Mathieu J, Zuchner S, Brais B: Adult-onset painful axonal polyneuropathy caused by a dominant NAGLU mutation. Brain. 2015 Jun;138(Pt 6):1477-83. doi: 10.1093/brain/awv074. Epub 2015 Mar 28. [Article]
  8. Zhao HG, Aronovich EL, Whitley CB: Genotype-phenotype correspondence in Sanfilippo syndrome type B. Am J Hum Genet. 1998 Jan;62(1):53-63. [Article]
  9. Schmidtchen A, Greenberg D, Zhao HG, Li HH, Huang Y, Tieu P, Zhao HZ, Cheng S, Zhao Z, Whitley CB, Di Natale P, Neufeld EF: NAGLU mutations underlying Sanfilippo syndrome type B. Am J Hum Genet. 1998 Jan;62(1):64-9. [Article]
  10. Beesley CE, Young EP, Vellodi A, Winchester BG: Identification of 12 novel mutations in the alpha-N-acetylglucosaminidase gene in 14 patients with Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB). J Med Genet. 1998 Nov;35(11):910-4. [Article]
  11. Bunge S, Knigge A, Steglich C, Kleijer WJ, van Diggelen OP, Beck M, Gal A: Mucopolysaccharidosis type IIIB (Sanfilippo B): identification of 18 novel alpha-N-acetylglucosaminidase gene mutations. J Med Genet. 1999 Jan;36(1):28-31. [Article]
  12. Weber B, Guo XH, Kleijer WJ, van de Kamp JJ, Poorthuis BJ, Hopwood JJ: Sanfilippo type B syndrome (mucopolysaccharidosis III B): allelic heterogeneity corresponds to the wide spectrum of clinical phenotypes. Eur J Hum Genet. 1999 Jan;7(1):34-44. [Article]
  13. Yogalingam G, Weber B, Meehan J, Rogers J, Hopwood JJ: Mucopolysaccharidosis type IIIB: characterisation and expression of wild-type and mutant recombinant alpha-N-acetylglucosaminidase and relationship with sanfilippo phenotype in an attenuated patient. Biochim Biophys Acta. 2000 Nov 15;1502(3):415-25. [Article]
  14. Tessitore A, Villani GR, Di Domenico C, Filocamo M, Gatti R, Di Natale P: Molecular defects in the alpha-N-acetylglucosaminidase gene in Italian Sanfilippo type B patients. Hum Genet. 2000 Dec;107(6):568-76. [Article]
  15. Coll MJ, Anton C, Chabas A: Allelic heterogeneity in Spanish patients with Sanfilippo disease type B. Identification of eight new mutations. J Inherit Metab Dis. 2001 Feb;24(1):83-4. [Article]
  16. Emre S, Terzioglu M, Tokatli A, Coskun T, Ozalp I, Weber B, Hopwood JJ: Sanfilippo syndrome in Turkey: Identification of novel mutations in subtypes A and B. Hum Mutat. 2002 Feb;19(2):184-5. [Article]
  17. Tanaka A, Kimura M, Lan HT, Takaura N, Yamano T: Molecular analysis of the alpha-N-acetylglucosaminidase gene in seven Japanese patients from six unrelated families with mucopolysaccharidosis IIIB (Sanfilippo type B), including two novel mutations. J Hum Genet. 2002;47(9):484-7. [Article]
  18. Lee-Chen GJ, Lin SP, Lin SZ, Chuang CK, Hsiao KT, Huang CF, Lien WC: Identification and characterisation of mutations underlying Sanfilippo syndrome type B (mucopolysaccharidosis type IIIB). J Med Genet. 2002 Feb;39(2):E3. [Article]
  19. Beesley C, Moraitou M, Winchester B, Schulpis K, Dimitriou E, Michelakakis H: Sanfilippo B syndrome: molecular defects in Greek patients. Clin Genet. 2004 Feb;65(2):143-9. [Article]
  20. Chinen Y, Tohma T, Izumikawa Y, Uehara H, Ohta T: Sanfilippo type B syndrome: five patients with an R565P homozygous mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa islands in Japan. J Hum Genet. 2005;50(7):357-9. Epub 2005 Jun 3. [Article]
  21. Beesley CE, Jackson M, Young EP, Vellodi A, Winchester BG: Molecular defects in Sanfilippo syndrome type B (mucopolysaccharidosis IIIB). J Inherit Metab Dis. 2005;28(5):759-67. [Article]

Associated Data

Bio-Entities
Bio-EntityType
Alpha-N-acetylglucosaminidase (Humans)protein
primary
Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
N-Acetylglucosamineapproved, investigational, nutraceuticalunknowntargetactivatorDetails
Human calcitoninapproved, investigationalnoenzymesubstrateDetails