NAGA (gene)

N-acetylgalactosaminidase, alpha-

Rendering based on PDB 3H53.

Available structures
PDB	3H53, 3H54, 3H55, 3IGU

Identifiers

Symbols

NAGA; D22S674; GALB

External IDs

OMIM: 104170 MGI: 1261422 HomoloGene: 221 GeneCards: NAGA Gene

EC number

3.2.1.49

Gene Ontology
Molecular function	• hydrolase activity, hydrolyzing O-glycosyl compounds • alpha-galactosidase activity • alpha-N-acetylgalactosaminidase activity • protein homodimerization activity • cation binding
Cellular component	• cytoplasm • lysosome
Biological process	• oligosaccharide metabolic process • carbohydrate catabolic process • glycoside catabolic process • glycolipid catabolic process • glycosylceramide catabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 22:
42.43 – 42.47 Mb

Chr 15:
82.16 – 82.17 Mb

PubMed search

[1]

[2]

Alpha-N-acetylgalactosaminidase is an enzyme that in humans is encoded by the NAGA gene.^[1]

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).^[1]

References

^ ^a ^b "Entrez Gene: NAGA N-acetylgalactosaminidase, alpha-". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4668.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=296929.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=296165.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1050630.
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. 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. 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=545604.

Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases

Disaccharidase	Sucrase/Sucrase-isomaltase/Invertase · Maltase · Trehalase · Lactase

Glucosidases	Cellulase · Alpha-glucosidase (Acid, Neutral AB, Neutral C) · Beta-glucosidase (cytosolic) · Debranching enzyme

Other	Amylase (Alpha-Amylase) · Chitinase · Lysozyme · Neuraminidase (NEU1, NEU2, NEU3, NEU4, Bacterial neuraminidase, Viral neuraminidase) · Galactosidases (Alpha, Beta) · alpha-Mannosidase · Glucuronidase · Hyaluronidase · Pullulanase · Glucosylceramidase (lysosomal, non-lysosomal) · Galactosylceramidase · Alpha-N-acetylgalactosaminidase (NAGA) · Alpha-N-acetylglucosaminidase · Fucosidase · Hexosaminidase (HEXA, HEXB) · Iduronidase · Maltase-glucoamylase · Heparanase (HPSE2)

3.2.2: Hydrolysing
N-Glycosyl compounds

DNA glycosylases: Oxoguanine glycosylase

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

Metabolism: carbohydrate metabolism · glycoprotein enzymes

Anabolism

Dolichol kinase · GCS1 · Oligosaccharyltransferase

Catabolism

Neuraminidase · Beta-galactosidase · Hexosaminidase · mannosidase (alpha-Mannosidase, beta-mannosidase) · Aspartylglucosaminidase · Fucosidase · NAGA

Transport

SLC17A5

M6P tagging

N-acetylglucosamine-1-phosphate transferase

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

NAGA (gene)

References

Further reading