NAGA (gene)

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; OMA:NAGA - orthologs
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 82,213,733 bp [2] End 82,223,126 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte granulocyte stromal cell of endometrium gonad gallbladder rectum placenta appendix Descending thoracic aorta olfactory zone of nasal mucosa Top expressed in islet of Langerhans choroid plexus of fourth ventricle yolk sac right kidney decidua stomach stroma of bone marrow epithelium of stomach lacrimal gland neural layer of retina More reference expression data BioGPS 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: 82.21 – 82.22 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

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. S2CID   21567863.
• 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. doi: 10.1016/S0021-9258(18)45818-8 . 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. S2CID   28205039.
• 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. S2CID   23355968.
• 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. A. 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 .