| Post Translational Modifications | N-glycosylated. 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. Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates (Probable). |
| Function | 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. Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine. |
| Protein Name | N-Acylethanolamine-Hydrolyzing Acid AmidaseAcid Ceramidase-Like ProteinAcylsphingosine Deacylase NaaaN-Acylsphingosine Amidohydrolase-LikeAsah-Like Protein Cleaved Into - N-Acylethanolamine-Hydrolyzing Acid Amidase Subunit Alpha - N-Acylethanolamine-Hydrolyzing Acid Amidase Subunit Beta |
| Database Links | Reactome: R-HSA-112310 |
| Cellular Localisation | LysosomeMembranePeripheral Membrane Protein |
| Alternative Antibody Names | Anti-N-Acylethanolamine-Hydrolyzing Acid Amidase antibodyAnti-Acid Ceramidase-Like Protein antibodyAnti-Acylsphingosine Deacylase Naaa antibodyAnti-N-Acylsphingosine Amidohydrolase-Like antibodyAnti-Asah-Like Protein Cleaved Into - N-Acylethanolamine-Hydrolyzing Acid Amidase Subunit Alpha - N-Acylethanolamine-Hydrolyzing Acid Amidase Subunit Beta antibodyAnti-NAAA antibodyAnti-ASAHL antibodyAnti-PLT antibody |
Information sourced from Uniprot.org
