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 82,213,733 bp[2] End 82,223,126 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte stromal cell of endometrium gallbladder rectum placenta appendix right coronary artery blood smooth muscle tissue ascending aorta Top expressed in islet of Langerhans yolk sac stomach epithelium of stomach lacrimal gland small intestine pyloric antrum colon parotid gland duodenum 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
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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]