Naaa
entrez
497009
canonical
uniprot
Q5KTC7
canonical
ensembl
ENSRNOG00000002273
resolver
ensembl
ENSRNOG00055006332
resolver
ensembl
ENSRNOG00060018886
resolver
ensembl
ENSRNOG00065018387
resolver
ensp
ENSRNOP00000003102
resolver
ensp
ENSRNOP00055007979
resolver
ensp
ENSRNOP00060026603
resolver
ensp
ENSRNOP00065024565
resolver
enst
ENSRNOT00000003102
resolver
enst
ENSRNOT00055010296
resolver
enst
ENSRNOT00060032600
resolver
enst
ENSRNOT00065030855
resolver
genesymbol
Naaa
resolver
genesymbol_syn
Asahl
resolver
uniprot
Q3KRD3
resolver
uniprot_entry
NAAA_RAT
resolver
uniprot_sec
Q3KRD3
resolver
activity_regulation
ACTIVITY REGULATION: Stimulated by DTT (PubMed:11463796, PubMed:22860206). Stimulated by nonionic detergent of the polyoxyethylenep-t-octylphenylether type (Triton X-100 or Nonidet P-40) whereas 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate (CHAPS) and octyl alpha-D-glucopyranoside decrease the N-(long-chain-acyl)ethanolamine deacylase activity (PubMed:22860206). Polysorbate 20 (Tween 20) is inhibitory (PubMed:11463796). Stimulated by endogenous phospholipids such as choline- or ethanolamine-containing phospholipids, and dihydrolipoic acid (PubMed:22860206). {ECO:0000269|PubMed:11463796, ECO:0000269|PubMed:22860206}.
uniprot
proteins
amino_acid_sequence
MGTPAIRAACHGAHLALALLLLLSLSDPWLWATAPGTPPLFNVSLDAAPELRWLPMLQHYDPDFVRAAVAQVIGDRVPQWILEMIGEIVQKVESFLPQPFTSEIRGICDYLNLSLAEGVLVNLAYEASAFCTSIVAQDSQGRIYHGRNLDYPFGNALRKLTADVQFVKNGQIVFTATTFVGYVGLWTGQSPHKFTISGDERDKGWWWENMIAALSLGHSPISWLIRKTLTESEDFEAAVYTLAKTPLIADVYYIVGGTSPQEGVVITRDRGGPADIWPLDPLNGAWFRVETNYDHWEPVPKRDDRRTPAIKALNATGQAHLSLETLFQVLSVFPVYNNYTIYTTVMSAAEPDKYMTMIRNPS
uniprot
proteins
ec_number
3.5.1.23
uniprot
proteins
ec_number
3.5.1.60
uniprot
proteins
function
FUNCTION: Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N-palmitoylethanolamine > N-myristoylethanolamine > N-stearoylethanolamine > N-oleoylethanolamine > N-linoleoylethanolamine > N-arachidonoylethanolamine. {ECO:0000269|PubMed:11463796, ECO:0000269|PubMed:15655246, ECO:0000269|PubMed:22860206}.
uniprot
proteins
mass_dalton
40313
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:11463796, ECO:0000269|PubMed:15655246}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine. {ECO:0000250|UniProtKB:Q02083}.; PTM: 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. {ECO:0000250|UniProtKB:Q02083}.
uniprot
proteins
protein_family
Acid ceramidase family
uniprot
proteins
pubmed
11463796
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15655246
uniprot
proteins
pubmed
22860206
uniprot
proteins
sequence_length
362
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q02083}. Membrane {ECO:0000250|UniProtKB:Q02083}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q02083}.
uniprot
proteins