ASAHL

NAAA
Identifiers
Aliases	NAAA , ASAHL, PLT, N-acylethanolamine acid amidase
External IDs	OMIM: 607469; MGI: 1914361; HomoloGene: 8686; GeneCards: NAAA; OMA:NAAA - orthologs
Gene location (Human) Chr. Chromosome 4 (human) [1] Band 4q21.1 Start 75,913,660 bp [1] End 75,941,013 bp [1]
Gene location (Mouse) Chr. Chromosome 5 (mouse) [2] Band 5|5 E2 Start 92,405,518 bp [2] End 92,426,029 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte granulocyte rectum mucosa of transverse colon spleen mucosa of sigmoid colon blood lymph node minor salivary glands olfactory zone of nasal mucosa Top expressed in choroidal fissure tail of embryo lip yolk sac Epithelium of choroid plexus lumbar spinal ganglion granulocyte white adipose tissue spleen mesenteric lymph nodes More reference expression data BioGPS 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 Species Human Mouse Entrez 27163 67111 Ensembl ENSG00000138744 ENSMUSG00000029413 UniProt Q02083 Q9D7V9 RefSeq (mRNA) NM_001042402 NM_014435 NM_001363719 NM_001163687 NM_025972 RefSeq (protein) NP_001035861 NP_055250 NP_001350648 NP_001157159 NP_080248 Location (UCSC) Chr 4: 75.91 – 75.94 Mb Chr 5: 92.41 – 92.43 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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]

References

1. GRCh38: Ensembl release 89: ENSG00000138744 – Ensembl, May 2017
2. 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.
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.
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.
7. "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 .

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. 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.