NAAA

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. [provided by RefSeq]

N-acylethanolamine acid amidase

Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine> N-myristoylethanolamine> N-lauroylethanolamine = N-stearoylethanolamine> N-arachidonoylethanolamine> N-oleoylethanolamine (PubMed:15655246, PubMed:17980170, PubMed:18793752, PubMed:30301806, PubMed:22825852).

Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine (PubMed:15655246).

Fatty acid metabolic process Source: UniProtKB
Lipid catabolic process Source: UniProtKB-KW
N-acylethanolamine metabolic process Source: UniProtKB
N-acylphosphatidylethanolamine metabolic process Source: UniProtKB
Sphingosine metabolic process Source: UniProtKB

Lysosome
Other locations
Membrane

N-glycosylated (PubMed:17980170, PubMed:18793752, PubMed:30301806). Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine.
A disulfide bond is seen in the crystal structure of the human protein, but the Cys residues are not conserved in rodents.
Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and beta subunit (PubMed:15655246, PubMed:22040171, PubMed:17980170, PubMed:18793752, PubMed:30301806). Cleavage gives rise to a conformation change that activates the enzyme (PubMed:17980170, PubMed:18793752, PubMed:30301806, PubMed:22040171). The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates (PubMed:17980170, PubMed:18793752) (Probable).