ASAHL

Protein-coding gene in the species Homo sapiens
NAAA
Identifiers
AliasesNAAA, ASAHL, PLT, N-acylethanolamine acid amidase
External IDsOMIM: 607469; MGI: 1914361; HomoloGene: 8686; GeneCards: NAAA; OMA:NAAA - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for NAAA
Genomic location for NAAA
Band4q21.1Start75,913,660 bp[1]
End75,941,013 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for NAAA
Genomic location for NAAA
Band5|5 E2Start92,405,518 bp[2]
End92,426,029 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 5: 92.41 – 92.43 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000138744 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "Entrez Gene: ASAHL N-acylsphingosine amidohydrolase (acid ceramidase)-like".

External links

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.


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