ASAHL

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

N-acylethanolamine-hydrolyzing acid amidase is an enzyme that in humans is encoded by the NAAA gene.{{cite journal | vauthors = Hong SB, Li CM, Rhee HJ, Park JH, He X, Levy B, Yoo OJ, Schuchman EH | title = Molecular cloning and characterization of a human cDNA and gene encoding a novel acid ceramidase-like protein | journal = Genomics | volume = 62 | issue = 2 | pages = 232–41 |date=Feb 2000 | pmid = 10610717 | doi = 10.1006/geno.1999.5953 }}{{cite journal | vauthors = Goodchild NL, Wilkinson DA, Mager DL | title = A human endogenous long terminal repeat provides a polyadenylation signal to a novel, alternatively spliced transcript in normal placenta | journal = Gene | volume = 121 | issue = 2 | pages = 287–94 |date=Dec 1992 | pmid = 1446826 | doi =10.1016/0378-1119(92)90133-A }}{{cite web | title = Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27163}}

Function

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.

References

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Further reading

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  • {{cite journal | vauthors=Schulze H, Schepers U, Sandhoff K |title=Overexpression and mass spectrometry analysis of mature human acid ceramidase. |journal=Biol. Chem. |volume=388 |issue= 12 |pages= 1333–43 |year= 2008 |pmid= 18020949 |doi= 10.1515/BC.2007.152 |s2cid=12612022 }}
  • {{cite journal | vauthors=Zhao LY, Tsuboi K, Okamoto Y |title=Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism. |journal=Biochim. Biophys. Acta |volume=1771 |issue= 11 |pages= 1397–405 |year= 2008 |pmid= 17980170 |doi= 10.1016/j.bbalip.2007.10.002 |display-authors=etal}}
  • {{cite journal | vauthors=Oh JH, Yang JO, Hahn Y |title=Transcriptome analysis of human gastric cancer. |journal=Mamm. Genome |volume=16 |issue= 12 |pages= 942–54 |year= 2006 |pmid= 16341674 |doi= 10.1007/s00335-005-0075-2 |s2cid=69278 |display-authors=etal}}
  • {{cite journal | vauthors=Tsuboi K, Sun YX, Okamoto Y |title=Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase. |journal=J. Biol. Chem. |volume=280 |issue= 12 |pages= 11082–92 |year= 2005 |pmid= 15655246 |doi= 10.1074/jbc.M413473200 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Huang Y, Tanimukai H, Liu F |title=Elevation of the level and activity of acid ceramidase in Alzheimer's disease brain. |journal=Eur. J. Neurosci. |volume=20 |issue= 12 |pages= 3489–97 |year= 2005 |pmid= 15610181 |doi= 10.1111/j.1460-9568.2004.03852.x |s2cid=11515970 |display-authors=etal}}
  • {{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}}
  • {{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |bibcode=2002PNAS...9916899M |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 |doi-access=free }}

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