ASAHL

NAAA
Identifiers
Aliases	NAAA , ASAHL, PLT, N-acylethanolamine acid amidase
External IDs	OMIM: 607469 MGI: 1914361 HomoloGene: 8686 GeneCards: NAAA
Gene location (Human)
Chr.	Chromosome 4 (human)
End	75,941,013 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	92,426,029 bp
RNA expression pattern
	Top expressed in
	monocyte; ; rectum; ; spleen; ; blood; ; lymph node; ; minor salivary gland; ; prostate; ; appendix; ; right lobe of liver; ; right coronary artery;
	Top expressed in
	lip; ; yolk sac; ; white adipose tissue; ; spleen; ; subcutaneous adipose tissue; ; visual cortex; ; carotid body; ; superior frontal gyrus; ; right lung lobe; ; olfactory epithelium;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transcription factor binding ; hydrolase activity ; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds ; fatty acid amide hydrolase activity ;
Cellular component	cytoplasm ; lysosome ; extracellular exosome ; lysosomal lumen ; presynapse ; extrinsic component of membrane ; membrane ;
Biological process	lipid metabolism ; neurotransmitter secretion ; biological process ; fatty acid metabolic process ; N-acylethanolamine metabolic process ; lipid catabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	27163
	67111
	ENSG00000138744
	ENSMUSG00000029413
	Q02083
	Q9D7V9
	NM_001042402 ; NM_014435 ; NM_001363719
	NM_001163687 ; NM_025972
	NP_001035861 ; NP_055250 ; NP_001350648
	NP_001157159 ; NP_080248
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated April 16, 2024

N-acylethanolamine-hydrolyzing acid amidase is an enzyme that in humans is encoded by the NAAA gene.^[5]^[6]^[7]

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.^[7]

Related Research Articles

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N-acylethanolamine acid amide hydrolase (NAAA) EC 3.5.1.- is a member of the choloylglycine hydrolase family, a subset of the N-terminal nucleophile hydrolase superfamily. NAAA has a molecular weight of 31 kDa. The activation and inhibition of its catalytic site is of medical interest as a potential treatment for obesity and chronic pain. While it was discovered within the last decade, its structural similarity to the more familiar acid ceramidase (AC) and functional similarity to fatty acid amide hydrolase (FAAH) allow it to be studied extensively.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000138744 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029413 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ 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.
1 2 "Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like".

External links

Human NAAA genome location and NAAA gene details page in the UCSC Genome Browser .

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. S2CID 12612022.
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. S2CID 69278.
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. S2CID 11515970.
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. Bibcode:2002PNAS...9916899M. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000138744 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029413 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10610717-5] 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.

[pmid1446826-6] 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.

[entrez-7] 1 2 "Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like".

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ASAHL

Contents

Function

Related Research Articles

References

External links

Further reading