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{{DISPLAYTITLE:''NAGA'' (gene)}}
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{{Infobox_gene}}
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'''Alpha-N-acetylgalactosaminidase''' is an [[enzyme]] that in humans is encoded by the ''NAGA'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NAGA N-acetylgalactosaminidase, alpha-| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4668| accessdate = }}</ref>
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{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = N-acetylgalactosaminidase, alpha-
| HGNCid = 7631
| Symbol = NAGA
| AltSymbols =; D22S674; GALB
| OMIM = 104170
| ECnumber = 
| Homologene = 221
| MGIid = 1261422
| GeneAtlas_image1 = PBB_GE_NAGA_202943_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NAGA_202944_at_tn.png
| Function = {{GNF_GO|id=GO:0004553 |text = hydrolase activity, hydrolyzing O-glycosyl compounds}} {{GNF_GO|id=GO:0008456 |text = alpha-N-acetylgalactosaminidase activity}} {{GNF_GO|id=GO:0043169 |text = cation binding}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}  
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4668
    | Hs_Ensembl = ENSG00000198951
    | Hs_RefseqProtein = NP_000253
    | Hs_RefseqmRNA = NM_000262
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 22
    | Hs_GenLoc_start = 40784331
    | Hs_GenLoc_end = 40796719
    | Hs_Uniprot = P17050
    | Mm_EntrezGene = 17939
    | Mm_Ensembl = ENSMUSG00000022453
    | Mm_RefseqmRNA = NM_008669
    | Mm_RefseqProtein = NP_032695
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 15
    | Mm_GenLoc_start = 82157304
    | Mm_GenLoc_end = 82166570
    | Mm_Uniprot = Q3U6T2
  }}
}}
'''N-acetylgalactosaminidase, alpha-''', also known as '''NAGA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NAGA N-acetylgalactosaminidase, alpha-| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4668| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =
| summary_text = 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).<ref name="entrez">{{cite web | title = Entrez Gene: NAGA N-acetylgalactosaminidase, alpha-| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4668| accessdate = }}</ref>
| summary_text = NAGA encodes the lysosomal enzyme [[A-N-acetylgalactosaminidase|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]]).<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Cantz M, Ulrich-Bott B |title=Disorders of glycoprotein degradation. |journal=J. Inherit. Metab. Dis. |volume=13 |issue= 4 |pages= 523-37 |year= 1990 |pmid= 2122119 |doi=  }}
*{{cite journal  | vauthors=Cantz M, Ulrich-Bott B |title=Disorders of glycoprotein degradation. |journal=J. Inherit. Metab. Dis. |volume=13 |issue= 4 |pages= 523–37 |year= 1990 |pmid= 2122119 |doi=10.1007/BF01799510 }}
*{{cite journal  | author=Wang AM, Desnick RJ |title=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. |journal=Genomics |volume=10 |issue= 1 |pages= 133-42 |year= 1991 |pmid= 1646157 |doi=  }}
*{{cite journal  | vauthors=Wang AM, Desnick RJ | author2-link=Robert J. Desnick  |title=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. |journal=Genomics |volume=10 |issue= 1 |pages= 133–42 |year= 1991 |pmid= 1646157 |doi=10.1016/0888-7543(91)90493-X }}
*{{cite journal  | author=Wang AM, Bishop DF, Desnick RJ |title=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. |journal=J. Biol. Chem. |volume=265 |issue= 35 |pages= 21859-66 |year= 1991 |pmid= 2174888 |doi=  }}
*{{cite journal  | vauthors=Wang AM, Bishop DF, Desnick RJ |title=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. |journal=J. Biol. Chem. |volume=265 |issue= 35 |pages= 21859–66 |year= 1991 |pmid= 2174888 |doi=  }}
*{{cite journal  | author=Wang AM, Schindler D, Desnick R |title=Schindler disease: the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy. |journal=J. Clin. Invest. |volume=86 |issue= 5 |pages= 1752-6 |year= 1990 |pmid= 2243144 |doi= }}
*{{cite journal  | vauthors=Wang AM, Schindler D, Desnick R |title=Schindler disease: the molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes an infantile neuroaxonal dystrophy. |journal=J. Clin. Invest. |volume=86 |issue= 5 |pages= 1752–6 |year= 1990 |pmid= 2243144 |doi=10.1172/JCI114901  | pmc=296929  }}
*{{cite journal  | author=Warner TG, Louie A, Potier M |title=Photolabeling of the alpha-neuraminidase/beta-galactosidase complex from human placenta with a photoreactive neuraminidase inhibitor. |journal=Biochem. Biophys. Res. Commun. |volume=173 |issue= 1 |pages= 13-9 |year= 1991 |pmid= 2256909 |doi=  }}
*{{cite journal  | vauthors=Warner TG, Louie A, Potier M |title=Photolabeling of the alpha-neuraminidase/beta-galactosidase complex from human placenta with a photoreactive neuraminidase inhibitor. |journal=Biochem. Biophys. Res. Commun. |volume=173 |issue= 1 |pages= 13–9 |year= 1991 |pmid= 2256909 |doi=10.1016/S0006-291X(05)81014-9 }}
*{{cite journal | author=Yamauchi T, Hiraiwa M, Kobayashi H, ''et al.'' |title=Molecular cloning of two species of cDNAs for human alpha-N-acetylgalactosaminidase and expression in mammalian cells. |journal=Biochem. Biophys. Res. Commun. |volume=170 |issue= 1 |pages= 231-7 |year= 1990 |pmid= 2372288 |doi= }}
*{{cite journal   |vauthors=Yamauchi T, Hiraiwa M, Kobayashi H, etal |title=Molecular cloning of two species of cDNAs for human alpha-N-acetylgalactosaminidase and expression in mammalian cells. |journal=Biochem. Biophys. Res. Commun. |volume=170 |issue= 1 |pages= 231–7 |year= 1990 |pmid= 2372288 |doi=10.1016/0006-291X(90)91264-S  }}
*{{cite journal | author=Tsuji S, Yamauchi T, Hiraiwa M, ''et al.'' |title=Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B). |journal=Biochem. Biophys. Res. Commun. |volume=163 |issue= 3 |pages= 1498-504 |year= 1989 |pmid= 2551294 |doi=  }}
*{{cite journal   |vauthors=Tsuji S, Yamauchi T, Hiraiwa M, etal |title=Molecular cloning of a full-length cDNA for human alpha-N-acetylgalactosaminidase (alpha-galactosidase B). |journal=Biochem. Biophys. Res. Commun. |volume=163 |issue= 3 |pages= 1498–504 |year= 1989 |pmid= 2551294 |doi=10.1016/0006-291X(89)91149-2 }}
*{{cite journal  | author=Chabás A, Coll MJ, Aparicio M, Rodriguez Diaz E |title=Mild phenotypic expression of alpha-N-acetylgalactosaminidase deficiency in two adult siblings. |journal=J. Inherit. Metab. Dis. |volume=17 |issue= 6 |pages= 724-31 |year= 1995 |pmid= 7707696 |doi= }}
*{{cite journal  | vauthors=Chabás A, Coll MJ, Aparicio M, Rodriguez Diaz E |title=Mild phenotypic expression of alpha-N-acetylgalactosaminidase deficiency in two adult siblings. |journal=J. Inherit. Metab. Dis. |volume=17 |issue= 6 |pages= 724–31 |year= 1995 |pmid= 7707696 |doi=10.1007/BF00712015  }}
*{{cite journal  | author=Wang AM, Kanzaki T, Desnick RJ |title=The molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes angiokeratoma corporis diffusum with glycopeptiduria. |journal=J. Clin. Invest. |volume=94 |issue= 2 |pages= 839-45 |year= 1994 |pmid= 8040340 |doi=  }}
*{{cite journal  | vauthors=Wang AM, Kanzaki T, Desnick RJ |title=The molecular lesion in the alpha-N-acetylgalactosaminidase gene that causes angiokeratoma corporis diffusum with glycopeptiduria. |journal=J. Clin. Invest. |volume=94 |issue= 2 |pages= 839–45 |year= 1994 |pmid= 8040340 |doi=10.1172/JCI117404  | pmc=296165 }}
*{{cite journal | author=de Jong J, van den Berg C, Wijburg H, ''et al.'' |title=alpha-N-acetylgalactosaminidase deficiency with mild clinical manifestations and difficult biochemical diagnosis. |journal=J. Pediatr. |volume=125 |issue= 3 |pages= 385-91 |year= 1994 |pmid= 8071745 |doi=  }}
*{{cite journal   |vauthors=de Jong J, van den Berg C, Wijburg H, etal |title=alpha-N-acetylgalactosaminidase deficiency with mild clinical manifestations and difficult biochemical diagnosis. |journal=J. Pediatr. |volume=125 |issue= 3 |pages= 385–91 |year= 1994 |pmid= 8071745 |doi=10.1016/S0022-3476(05)83281-0 }}
*{{cite journal | author=Keulemans JL, Reuser AJ, Kroos MA, ''et al.'' |title=Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new mutations and the paradox between genotype and phenotype. |journal=J. Med. Genet. |volume=33 |issue= 6 |pages= 458-64 |year= 1996 |pmid= 8782044 |doi=  }}
*{{cite journal   |vauthors=Keulemans JL, Reuser AJ, Kroos MA, etal |title=Human alpha-N-acetylgalactosaminidase (alpha-NAGA) deficiency: new mutations and the paradox between genotype and phenotype. |journal=J. Med. Genet. |volume=33 |issue= 6 |pages= 458–64 |year= 1996 |pmid= 8782044 |doi=10.1136/jmg.33.6.458  | pmc=1050630 }}
*{{cite journal  | author=Den Tandt WR, Scharpé S |title=Micromethod for the fluorimetric determination of plasma N-acetyl-alpha-D-galactosaminidase and study of some of its characteristics. |journal=Enzyme Protein |volume=49 |issue= 5-6 |pages= 273-80 |year= 1997 |pmid= 9252785 |doi=  }}
*{{cite journal  | vauthors=Den Tandt WR, Scharpé S |title=Micromethod for the fluorimetric determination of plasma N-acetyl-alpha-D-galactosaminidase and study of some of its characteristics. |journal=Enzyme Protein |volume=49 |issue= 5–6 |pages= 273–80 |year= 1997 |pmid= 9252785 |doi=  }}
*{{cite journal | author=Gaudet R, Savage JR, McLaughlin JN, ''et al.'' |title=A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin. |journal=Mol. Cell |volume=3 |issue= 5 |pages= 649-60 |year= 1999 |pmid= 10360181 |doi=  }}
*{{cite journal   |vauthors=Gaudet R, Savage JR, McLaughlin JN, etal |title=A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin |journal=Mol. Cell |volume=3 |issue= 5 |pages= 649–60 |year= 1999 |pmid= 10360181 |doi=10.1016/S1097-2765(00)80358-5 }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal   |vauthors=Dunham I, Shimizu N, Roe BA, etal |title=The DNA sequence of human chromosome 22 |journal=Nature |volume=402 |issue= 6761 |pages= 489–95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Ohta M, Ohnishi T, Ioannou YA, ''et al.'' |title=Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides. |journal=Glycobiology |volume=10 |issue= 3 |pages= 251-61 |year= 2000 |pmid= 10704524 |doi=  }}
*{{cite journal   |vauthors=Ohta M, Ohnishi T, Ioannou YA, etal |title=Human alpha-N-acetylgalactosaminidase: site occupancy and structure of N-linked oligosaccharides |journal=Glycobiology |volume=10 |issue= 3 |pages= 251–61 |year= 2000 |pmid= 10704524 |doi=10.1093/glycob/10.3.251 }}
*{{cite journal | author=Kodama K, Kobayashi H, Abe R, ''et al.'' |title=A new case of alpha-N-acetylgalactosaminidase deficiency with angiokeratoma corporis diffusum, with Ménière's syndrome and without mental retardation. |journal=Br. J. Dermatol. |volume=144 |issue= 2 |pages= 363-8 |year= 2001 |pmid= 11251574 |doi=  }}
*{{cite journal   |vauthors=Kodama K, Kobayashi H, Abe R, etal |title=A new case of alpha-N-acetylgalactosaminidase deficiency with angiokeratoma corporis diffusum, with Ménière's syndrome and without mental retardation |journal=Br. J. Dermatol. |volume=144 |issue= 2 |pages= 363–8 |year= 2001 |pmid= 11251574 |doi=10.1046/j.1365-2133.2001.04028.x }}
*{{cite journal  | author=Mohamad SB, Nagasawa H, Uto Y, Hori H |title=Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation. |journal=Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. |volume=132 |issue= 1 |pages= 1-8 |year= 2003 |pmid= 12062184 |doi=  }}
*{{cite journal  | vauthors=Mohamad SB, Nagasawa H, Uto Y, Hori H |title=Tumor cell alpha-N-acetylgalactosaminidase activity and its involvement in GcMAF-related macrophage activation |journal=Comp. Biochem. Physiol., Part a Mol. Integr. Physiol. |volume=132 |issue= 1 |pages= 1–8 |year= 2003 |pmid= 12062184 |doi=10.1016/S1095-6433(01)00522-0 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Collins JE, Wright CL, Edwards CA, ''et al.'' |title=A genome annotation-driven approach to cloning the human ORFeome. |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84 }}
*{{cite journal   |vauthors=Collins JE, Wright CL, Edwards CA, etal |title=A genome annotation-driven approach to cloning the human ORFeome |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84 | pmc=545604 }}
}}
}}
{{refend}}
{{refend}}
{{Sugar hydrolases}}
{{Glycoprotein metabolism enzymes}}
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[[Category:Human proteins]]


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Latest revision as of 12:25, 5 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. ↑ 1.0 1.1 "Entrez Gene: NAGA N-acetylgalactosaminidase, alpha-".

Further reading


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