ZFIN is now using GRCz12tu for Genomic Data
Gene
naga
- ID
- ZDB-GENE-051113-256
- Name
- N-acetylgalactosaminidase, alpha
- Symbol
- naga Nomenclature History
- Previous Names
-
- zgc:123333
- Type
- protein_coding_gene
- Location
- Chr: 4 Mapping Details/Browsers
- Genome Assembly
- GRCz12tu
- Annotation Status
- Current
- Description
- Predicted to enable alpha-galactosidase activity. Predicted to be involved in glycoside catabolic process and oligosaccharide metabolic process. Predicted to be located in lysosome. Predicted to be active in cytoplasm. Human ortholog(s) of this gene implicated in Kanzaki disease; Schindler disease type 1; angiokeratoma; and neuroaxonal dystrophy. Orthologous to human NAGA (alpha-N-acetylgalactosaminidase).
- Genome Resources
- Note
- None
- Comparative Information
-
- All Expression Data
- No data available
- Cross-Species Comparison
- High Throughput Data
- Thisse Expression Data
- No data available
Wild Type Expression Summary
- All Phenotype Data
- No data available
- Cross-Species Comparison
- Alliance
Phenotype Summary
Mutations
No data available
Human Disease
Disease Ontology Term | Multi-Species Data | OMIM Term | OMIM Phenotype ID |
---|---|---|---|
Kanzaki disease | Alliance | Kanzaki disease | 609242 |
Schindler disease type 1 | Alliance | Schindler disease, type I | 609241 |
Schindler disease type 1 | Alliance | Schindler disease, type III | 609241 |
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Domain, Family, and Site Summary
Type | InterPro ID | Name |
---|---|---|
Conserved_site | IPR000111 | Glycoside hydrolase family 27/36, conserved site |
Domain | IPR035373 | Alpha galactosidase A, C-terminal beta-sandwich domain |
Family | IPR002241 | Glycoside hydrolase, family 27 |
Homologous_superfamily | IPR013780 | Glycosyl hydrolase, all-beta |
Homologous_superfamily | IPR013785 | Aldolase-type TIM barrel |
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Domain Details Per Protein
Protein | Additional Resources | Length | Aldolase-type TIM barrel | Alpha galactosidase A, C-terminal beta-sandwich domain | Glycoside hydrolase, family 27 | Glycoside hydrolase family 27/36, conserved site | Glycoside hydrolase superfamily | Glycosyl hydrolase, all-beta |
---|---|---|---|---|---|---|---|---|
UniProtKB:A0A0R4IJL2 | InterPro | 437 |
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- Genome Browsers
Interactions and Pathways
No data available
Plasmids
No data available
No data available
Relationship | Marker Type | Marker | Accession Numbers | Citations |
---|---|---|---|---|
Encodes | cDNA | MGC:123333 | ZFIN Curated Data | |
Encodes | cDNA | MGC:162842 | ZFIN Curated Data |
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- Genome Browsers
Type | Accession # | Genome Assembly | Length (nt/aa) | Analysis |
---|---|---|---|---|
RNA | RefSeq:NM_001037388 (1) | 1764 nt | ||
Genomic | GenBank:FO904962 (1) | 93530 nt | ||
Polypeptide | UniProtKB:A0A0R4IJL2 (1) | 437 aa |
- Wang, M., Chen, Y., Zhu, M., Xu, B., Guo, W., Lyu, Y., Zhang, C. (2019) Pharmacological modulation of melanocortin-4 receptor by melanocortin receptor accessory protein 2 in Nile tilapia. General and comparative endocrinology. 282:113219
- Elkon, R., Milon, B., Morrison, L., Shah, M., Vijayakumar, S., Racherla, M., Leitch, C.C., Silipino, L., Hadi, S., Weiss-Gayet, M., Barras, E., Schmid, C.D., Ait-Lounis, A., Barnes, A., Song, Y., Eisenman, D.J., Eliyahu, E., Frolenkov, G.I., Strome, S.E., Durand, B., Zaghloul, N.A., Jones, S.M., Reith, W., Hertzano, R. (2015) RFX transcription factors are essential for hearing in mice. Nature communications. 6:8549
- Carlson, P., Smalley, D.M., and Van Beneden, R.J. (2013) Proteomic analysis of arsenic-exposed zebrafish (Danio rerio) identifies altered expression in proteins involved in fibrosis and lipid uptake in a gender-specific manner. Toxicological sciences : an official journal of the Society of Toxicology. 134(1):83-91
- Strausberg,R.L., Feingold,E.A., Grouse,L.H., Derge,J.G., Klausner,R.D., Collins,F.S., Wagner,L., Shenmen,C.M., Schuler,G.D., Altschul,S.F., Zeeberg,B., Buetow,K.H., Schaefer,C.F., Bhat,N.K., Hopkins,R.F., Jordan,H., Moore,T., Max,S.I., Wang,J., Hsieh,F., Diatchenko,L., Marusina,K., Farmer,A.A., Rubin,G.M., Hong,L., Stapleton,M., Soares,M.B., Bonaldo,M.F., Casavant,T.L., Scheetz,T.E., Brownstein,M.J., Usdin,T.B., Toshiyuki,S., Carninci,P., Prange,C., Raha,S.S., Loquellano,N.A., Peters,G.J., Abramson,R.D., Mullahy,S.J., Bosak,S.A., McEwan,P.J., McKernan,K.J., Malek,J.A., Gunaratne,P.H., Richards,S., Worley,K.C., Hale,S., Garcia,A.M., Gay,L.J., Hulyk,S.W., Villalon,D.K., Muzny,D.M., Sodergren,E.J., Lu,X., Gibbs,R.A., Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M., Madan,A., Young,A.C., Shevchenko,Y., Bouffard,G.G., Blakesley,R.W., Touchman,J.W., Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M., Butterfield,Y.S., Krzywinski,M.I., Skalska,U., Smailus,D.E., Schnerch,A., Schein,J.E., Jones,S.J., and Marra,M.A. (2002) Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America. 99(26):16899-903
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