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]
^ abcGRCh38: Ensembl release 89: ENSG00000138744 – Ensembl, May 2017
^ abcGRCm38: 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.