NAGA (gene)

Alpha-N-acetylgalactosaminidase is an enzyme that in humans is encoded by the NAGA gene.[5]

NAGA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4DO5, 3H53, 3IGU, 4DO4, 4DO6, 3H54, 3H55
Identifiers
Aliases	NAGA, D22S674, GALB, alpha-N-acetylgalactosaminidase
External IDs	OMIM: 104170 MGI: 1261422 HomoloGene: 221 GeneCards: NAGA
Gene location (Human) Chr. Chromosome 22 (human)[1] Band 22q13.2 Start 42,058,334 bp[1] End 42,070,842 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15 E1|15 38.56 cM Start 82,329,532 bp[2] End 82,338,925 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • hydrolase activity, hydrolyzing O-glycosyl compounds • alpha-N-acetylgalactosaminidase activity • hydrolase activity • protein homodimerization activity • alpha-galactosidase activity • catalytic activity • hydrolase activity, acting on glycosyl bonds Cellular component • cytoplasm • lysosome • extracellular exosome Biological process • carbohydrate catabolic process • metabolism • glycoside catabolic process • glycolipid catabolic process • oligosaccharide metabolic process • glycosylceramide catabolic process • carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4668	17939
Ensembl	ENSG00000198951	ENSMUSG00000022453
UniProt	P17050	Q9QWR8
RefSeq (mRNA)	NM_000262 NM_001362848 NM_001362850	NM_008669 NM_001355546
RefSeq (protein)	NP_000253 NP_001349777 NP_001349779 NP_000253.1	NP_032695 NP_001342475
Location (UCSC)	Chr 22: 42.06 – 42.07 Mb	Chr 15: 82.33 – 82.34 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

NAGA encodes the lysosomal enzyme alpha-N-acetylgalactosaminidase, which cleaves alpha-N-acetylgalactosaminyl moieties from glycoconjugates. Mutations in NAGA have been identified as the cause of Schindler disease types I and II (type II also known as Kanzaki disease).[5]

References

1. GRCh38: Ensembl release 89: ENSG00000198951 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022453 - 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: NAGA N-acetylgalactosaminidase, alpha-".

Further reading

• Cantz M, Ulrich-Bott B (1990). "Disorders of glycoprotein degradation". J. Inherit. Metab. Dis. 13 (4): 523–37. doi:10.1007/BF01799510. PMID 2122119.
• Wang AM, Desnick RJ (1991). "Structural organization and complete sequence of the human alpha-N-acetylgalactosaminidase gene: homology with the alpha-galactosidase A gene provides evidence for evolution from a common ancestral gene". Genomics. 10 (1): 133–42. doi:10.1016/0888-7543(91)90493-X. PMID 1646157.
• Wang AM, Bishop DF, Desnick RJ (1991). "Human alpha-N-acetylgalactosaminidase-molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Homology with human alpha-galactosidase A suggests evolution from a common ancestral gene". J. Biol. Chem. 265 (35): 21859–66. PMID 2174888.
• Wang AM, Schindler D, Desnick R (1990). "Schindler disease: the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy". J. Clin. Invest. 86 (5): 1752–6. doi:10.1172/JCI114901. PMC 296929. PMID 2243144.
• Warner TG, Louie A, Potier M (1991). "Photolabeling of the alpha-neuraminidase/beta-galactosidase complex from human placenta with a photoreactive neuraminidase inhibitor". Biochem. Biophys. Res. Commun. 173 (1): 13–9. doi:10.1016/S0006-291X(05)81014-9. PMID 2256909.
• Yamauchi T, Hiraiwa M, Kobayashi H, et al. (1990). "Molecular cloning of two species of cDNAs for human alpha-N-acetylgalactosaminidase and expression in mammalian cells". Biochem. Biophys. Res. Commun. 170 (1): 231–7. doi:10.1016/0006-291X(90)91264-S. PMID 2372288.
• Tsuji S, Yamauchi T, Hiraiwa M, et al. (1989). "Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B)". Biochem. Biophys. Res. Commun. 163 (3): 1498–504. doi:10.1016/0006-291X(89)91149-2. PMID 2551294.
• Chabás A, Coll MJ, Aparicio M, Rodriguez Diaz E (1995). "Mild phenotypic expression of alpha-N-acetylgalactosaminidase deficiency in two adult siblings". J. Inherit. Metab. Dis. 17 (6): 724–31. doi:10.1007/BF00712015. PMID 7707696.
• Wang AM, Kanzaki T, Desnick RJ (1994). "The molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes angiokeratoma corporis diffusum with glycopeptiduria". J. Clin. Invest. 94 (2): 839–45. doi:10.1172/JCI117404. PMC 296165. PMID 8040340.
• de Jong J, van den Berg C, Wijburg H, et al. (1994). "alpha-N-acetylgalactosaminidase deficiency with mild clinical manifestations and difficult biochemical diagnosis". J. Pediatr. 125 (3): 385–91. doi:10.1016/S0022-3476(05)83281-0. PMID 8071745.
• Keulemans JL, Reuser AJ, Kroos MA, et al. (1996). "Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new mutations and the paradox between genotype and phenotype". J. Med. Genet. 33 (6): 458–64. doi:10.1136/jmg.33.6.458. PMC 1050630. PMID 8782044.
• Den Tandt WR, Scharpé S (1997). "Micromethod for the fluorimetric determination of plasma N-acetyl-alpha-D-galactosaminidase and study of some of its characteristics". Enzyme Protein. 49 (5–6): 273–80. doi:10.1159/000468637. PMID 9252785.
• Gaudet R, Savage JR, McLaughlin JN, et al. (1999). "A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin". Mol. Cell. 3 (5): 649–60. doi:10.1016/S1097-2765(00)80358-5. PMID 10360181.
• Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. Bibcode:1999Natur.402..489D. doi:10.1038/990031. PMID 10591208.
• Ohta M, Ohnishi T, Ioannou YA, et al. (2000). "Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides". Glycobiology. 10 (3): 251–61. doi:10.1093/glycob/10.3.251. PMID 10704524.
• Kodama K, Kobayashi H, Abe R, et al. (2001). "A new case of alpha-N-acetylgalactosaminidase deficiency with angiokeratoma corporis diffusum, with Ménière's syndrome and without mental retardation". Br. J. Dermatol. 144 (2): 363–8. doi:10.1046/j.1365-2133.2001.04028.x. PMID 11251574.
• Mohamad SB, Nagasawa H, Uto Y, Hori H (2003). "Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation". Comp. Biochem. Physiol., Part a Mol. Integr. Physiol. 132 (1): 1–8. doi:10.1016/S1095-6433(01)00522-0. PMID 12062184.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.

External links

• Overview of all the structural information available in the PDB for UniProt: P17050 (Human Alpha-N-acetylgalactosaminidase (NAGA)) at the PDBe-KB.