Naaa
entrez
67111
canonical
uniprot
Q9D7V9
canonical
ensembl
ENSMUSG00000029413
resolver
ensp
ENSMUSP00000108726
resolver
ensp
ENSMUSP00000124582
resolver
enst
ENSMUST00000113102
resolver
enst
ENSMUST00000159345
resolver
genesymbol
Naaa
resolver
genesymbol_syn
Asahl
resolver
uniprot
G3XA18
resolver
uniprot
Q3V023
resolver
uniprot
Q5KTC6
resolver
uniprot
Q99KM3
resolver
uniprot
Q9D6B4
resolver
uniprot_entry
G3XA18_MOUSE
resolver
uniprot_entry
NAAA_MOUSE
resolver
uniprot_entry
Q3V023_MOUSE
resolver
uniprot_sec
Q5KTC6
resolver
uniprot_sec
Q99KM3
resolver
uniprot_sec
Q9D6B4
resolver
amino_acid_sequence
MGTLATRAACHGAHLALALLLLLSLSGPWLSAVVPGTPPLFNVSLDAAPEQRWLPMLRHYDPDFLRTAVAQVIGDRVPQWVLGMVGEIVSKVESFLPQPFTDEIRSICDSLNLSLADGILVNLAYEASAFCTSIVAQDSQGHIYHGRNLDYPFGKILRKLTANVQFIKNGQIAFTGTTFVGYVGLWTGQSPHKFTISGDERDKGWWWENMIAALSLGHSPISWLIRKTLSESESFEAAVYTLAKTPLIADVYYIVGGTSPKEGVVITRDRGGPADIWPLDPLNGEWFRVETNYDHWKPAPKVDDRRTPAIKALNATGQAHLNLETLFQVLSLFPVYNNYTIYTTVMSAAEPDKYLTMIRNPS
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:0000250|UniProtKB:Q5KTC7}.
uniprot
proteins
mass_dalton
40075
uniprot
proteins
mutagenesis
MUTAGEN 112; /note="N->S: Loss of one glycosylation site."; /evidence="ECO:0000269|PubMed:30301806"; MUTAGEN 338; /note="N->S: Loss of one glycosylation site."; /evidence="ECO:0000269|PubMed:30301806
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:Q02083}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:30301806). Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine (By similarity). {ECO:0000250|UniProtKB:Q02083, ECO:0000269|PubMed:30301806}.; PTM: Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and beta subunit (PubMed:30301806). 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 (By similarity). {ECO:0000250|UniProtKB:Q02083, ECO:0000269|PubMed:30301806}.
uniprot
proteins
protein_family
Acid ceramidase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15655246
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
30301806
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