ASAHL

NAAA
Identifiers
Aliases	NAAA, ASAHL, PLT, N-acylethanolamine acid amidase
External IDs	MGI: 1914361 HomoloGene: 8686 GeneCards: NAAA
Gene ontology Molecular function • transcription factor binding • hydrolase activity • hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Cellular component • cytoplasm • lysosome • extracellular exosome • lysosomal lumen • presynapse Biological process • biological process • lipid metabolic process • neurotransmitter secretion Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	27163	67111
Ensembl	ENSG00000138744	ENSMUSG00000029413
UniProt	Q02083	Q9D7V9
RefSeq (mRNA)	NM_001042402 NM_014435	NM_001163687 NM_025972
RefSeq (protein)	NP_001035861.1 NP_055250.2	NP_001157159.1 NP_080248.2
Location (UCSC)	Chr 4: 75.91 – 75.94 Mb	Chr 5: 92.26 – 92.28 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

N-acylethanolamine-hydrolyzing acid amidase is an enzyme that in humans is encoded by the NAAA gene.^[3][4][5]

This gene encodes an N-acylethanolamine-hydrolyzing enzyme which is highly similar to acid ceramidase. Multiple transcript variants encoding different isoforms have been found for this gene.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Hong SB, Li CM, Rhee HJ, Park JH, He X, Levy B, Yoo OJ, Schuchman EH (Feb 2000). "Molecular cloning and characterization of a human cDNA and gene encoding a novel acid ceramidase-like protein". Genomics. 62 (2): 232–41. doi:10.1006/geno.1999.5953. PMID 10610717.
4. Goodchild NL, Wilkinson DA, Mager DL (Dec 1992). "A human endogenous long terminal repeat provides a polyadenylation signal to a novel, alternatively spliced transcript in normal placenta". Gene. 121 (2): 287–94. doi:10.1016/0378-1119(92)90133-A. PMID 1446826.
5. "Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like".

Further reading

• Schulze H, Schepers U, Sandhoff K (2008). "Overexpression and mass spectrometry analysis of mature human acid ceramidase.". Biol. Chem. 388 (12): 1333–43. doi:10.1515/BC.2007.152. PMID 18020949.
• Zhao LY, Tsuboi K, Okamoto Y, et al. (2008). "Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.". Biochim. Biophys. Acta. 1771 (11): 1397–405. doi:10.1016/j.bbalip.2007.10.002. PMID 17980170.
• Oh JH, Yang JO, Hahn Y, et al. (2006). "Transcriptome analysis of human gastric cancer.". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674.
• Tsuboi K, Sun YX, Okamoto Y, et al. (2005). "Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase.". J. Biol. Chem. 280 (12): 11082–92. doi:10.1074/jbc.M413473200. PMID 15655246.
• Huang Y, Tanimukai H, Liu F, et al. (2005). "Elevation of the level and activity of acid ceramidase in Alzheimer's disease brain.". Eur. J. Neurosci. 20 (12): 3489–97. doi:10.1111/j.1460-9568.2004.03852.x. PMID 15610181.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• 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.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.