NAGLU

NAGLU
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4XWH
Identifiers
Aliases	NAGLU , MPS-IIIB, MPS3B, NAG, UFHSD, CMT2V, N-acetyl-alpha-glucosaminidase
External IDs	OMIM: 609701; MGI: 1351641; HomoloGene: 222; GeneCards: NAGLU; OMA:NAGLU - orthologs
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17q21.2 Start 42,536,241 bp [1] End 42,544,449 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11|11 D Start 100,960,838 bp [2] End 100,968,498 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium body of pancreas gastric mucosa right lobe of liver thoracic aorta ascending aorta right lobe of thyroid gland right adrenal cortex left adrenal gland Descending thoracic aorta Top expressed in right kidney spermatocyte decidua stroma of bone marrow proximal tubule calvaria gastrula spermatid choroid plexus of fourth ventricle epithelium of lens More reference expression data BioGPS n/a
Gene ontology Molecular function alpha-N-acetylglucosaminidase activity hydrolase activity hydrolase activity, acting on glycosyl bonds Cellular component lysosome lysosomal lumen extracellular exosome Biological process metabolism inner ear receptor cell development lysosome organization glycosaminoglycan catabolic process retinal rod cell development cerebellar Purkinje cell layer development nervous system development middle ear morphogenesis locomotor rhythm Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 4669 27419 Ensembl ENSG00000108784 ENSMUSG00000001751 UniProt P54802 O88325 RefSeq (mRNA) NM_000263 NM_013792 RefSeq (protein) NP_000254 NP_038820 Location (UCSC) Chr 17: 42.54 – 42.54 Mb Chr 11: 100.96 – 100.97 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

N-acetylglucosaminidase, alpha is a protein that in humans is encoded by the NAGLU gene. ^[5]

Function

This gene encodes an enzyme that degrades heparan sulfate by hydrolysis of terminal N-acetyl-D-glucosamine residues in N-acetyl-alpha-D-glucosaminides.

Clinical significance

Defects in this gene are the cause of mucopolysaccharidosis type IIIB (MPS-IIIB), also known as Sanfilippo syndrome B. This disease is characterized by the lysosomal accumulation and urinary excretion of heparan sulfate. ^[5]

References

1. GRCh38: Ensembl release 89: ENSG00000108784 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000001751 – 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. "Entrez Gene: N-acetylglucosaminidase, alpha".

Further reading

• Weber B, Blanch L, Clements PR, Scott HS, Hopwood JJ (June 1996). "Cloning and expression of the gene involved in Sanfilippo B syndrome (mucopolysaccharidosis III B)". Human Molecular Genetics. 5 (6): 771–7. doi: 10.1093/hmg/5.6.771 . PMID   8776591.
• Clark AG, Glanowski S, Nielsen R, Thomas PD, Kejariwal A, Todd MA, Tanenbaum DM, Civello D, Lu F, Murphy B, Ferriera S, Wang G, Zheng X, White TJ, Sninsky JJ, Adams MD, Cargill M (December 2003). "Inferring nonneutral evolution from human-chimp-mouse orthologous gene trios". Science. 302 (5652): 1960–3. Bibcode:2003Sci...302.1960C. doi:10.1126/science.1088821. PMID   14671302. S2CID   6682593.
• Yogalingam G, Hopwood JJ (October 2001). "Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications". Human Mutation. 18 (4): 264–81. doi: 10.1002/humu.1189 . PMID   11668611. S2CID   25731955.
• Zhao HG, Li HH, Bach G, Schmidtchen A, Neufeld EF (June 1996). "The molecular basis of Sanfilippo syndrome type B". Proceedings of the National Academy of Sciences of the United States of America. 93 (12): 6101–5. Bibcode:1996PNAS...93.6101Z. doi: 10.1073/pnas.93.12.6101 . PMC   39196 . PMID   8650226.
• Winder-Rhodes SE, Garcia-Reitböck P, Ban M, Evans JR, Jacques TS, Kemppinen A, Foltynie T, Williams-Gray CH, Chinnery PF, Hudson G, Burn DJ, Allcock LM, Sawcer SJ, Barker RA, Spillantini MG (February 2012). "Genetic and pathological links between Parkinson's disease and the lysosomal disorder Sanfilippo syndrome". Movement Disorders. 27 (2): 312–5. doi:10.1002/mds.24029. PMID   22102531. S2CID   4834914.
• Sasaki T, Sukegawa K, Masue M, Fukuda S, Tomatsu S, Orii T (November 1991). "Purification and partial characterization of alpha-N-acetylglucosaminidase from human liver". Journal of Biochemistry. 110 (5): 842–6. doi: 10.1093/oxfordjournals.jbchem.a123668 . PMID   1783617.
• Vance JM, Pericak-Vance MA, Elston RC, Conneally PM, Namboodiri KK, Wappner RS, Yu PL (1980). "Evidence of genetic variation for alpha-N-acetyl-D-glucosaminidase in black and white populations: a new polymorphism". American Journal of Medical Genetics. 7 (2): 131–40. doi:10.1002/ajmg.1320070207. PMID   6781343.
• 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 (January 1998). "NAGLU mutations underlying Sanfilippo syndrome type B". American Journal of Human Genetics. 62 (1): 64–9. doi:10.1086/301685. PMC   1376809 . PMID   9443878.
• Ayala JM, Goyal S, Liverton NJ, Claremon DA, O'Keefe SJ, Hanlon WA (June 2000). "Serum-induced monocyte differentiation and monocyte chemotaxis are regulated by the p38 MAP kinase signal transduction pathway". Journal of Leukocyte Biology. 67 (6): 869–75. doi:10.1002/jlb.67.6.869. PMID   10857861. S2CID   28719955.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.