NAAA
entrez
27163
canonical
uniprot
Q02083
canonical
ensembl
ENSG00000138744
resolver
ensp
ENSP00000286733
resolver
ensp
ENSP00000427641
resolver
ensp
ENSP00000664598
resolver
ensp
ENSP00000664599
resolver
ensp
ENSP00000664600
resolver
ensp
ENSP00000664602
resolver
ensp
ENSP00000664603
resolver
ensp
ENSP00000664604
resolver
ensp
ENSP00000664605
resolver
ensp
ENSP00000664606
resolver
ensp
ENSP00000664607
resolver
ensp
ENSP00000714706
resolver
genesymbol
NAAA
resolver
genesymbol_syn
ASAHL
resolver
genesymbol_syn
PLT
resolver
hgnc
HGNC:736
resolver
uniprot
Q5KTF2
resolver
uniprot
Q96EY2
resolver
uniprot
Q9BRA8
resolver
uniprot_entry
NAAA_HUMAN
resolver
uniprot_sec
Q5KTF2
resolver
uniprot_sec
Q96EY2
resolver
uniprot_sec
Q9BRA8
resolver
activity_regulation
ACTIVITY REGULATION: Stimulated by DTT and Nonidet P-40. {ECO:0000269|PubMed:15655246}.
uniprot
proteins
amino_acid_sequence
MRTADREARPGLPSLLLLLLAGAGLSAASPPAAPRFNVSLDSVPELRWLPVLRHYDLDLVRAAMAQVIGDRVPKWVHVLIGKVVLELERFLPQPFTGEIRGMCDFMNLSLADCLLVNLAYESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGLWTGQSPHKFTVSGDERDKGWWWENAIAALFRRHIPVSWLIRATLSESENFEAAVGKLAKTPLIADVYYIVGGTSPREGVVITRNRDGPADIWPLDPLNGAWFRVETNYDHWKPAPKEDDRRTSAIKALNATGQANLSLEALFQILSVVPVYNNFTIYTTVMSAGSPDKYMTRIRNPSRK
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-lauroylethanolamine = N-stearoylethanolamine > N-arachidonoylethanolamine > N-oleoylethanolamine (PubMed:15655246, PubMed:17980170, PubMed:18793752, PubMed:22825852, PubMed:30301806). Also exhibits weak hydrolytic activity against the ceramides N-lauroylsphingosine and N-palmitoylsphingosine (PubMed:15655246). {ECO:0000269|PubMed:15655246, ECO:0000269|PubMed:17980170, ECO:0000269|PubMed:18793752, ECO:0000269|PubMed:22825852, ECO:0000269|PubMed:30301806}.
uniprot
proteins
mass_dalton
40066
uniprot
proteins
mutagenesis
MUTAGEN 116; /note="V->F: Decreased autoproteolytic cleavage and strongly reduced enzyme activity with liposome-bound substrate. Loss of enzyme activity with Triton-solubilized substrate."; /evidence="ECO:0000269|PubMed:30301806"; MUTAGEN 126; /note="C->A: Loss of autoproteolytic cleavage and loss of enzyme activity."; /evidence="ECO:0000269|PubMed:30301806"; MUTAGEN 126; /note="C->S: Loss of autoproteolytic cleavage and loss of enzyme activity."; /evidence="ECO:0000269|PubMed:17980170, ECO:0000269|PubMed:18793752"; MUTAGEN 142; /note="R->G: Loss of autoproteolytic cleavage and loss of enzyme activity."; /evidence="ECO:0000269|PubMed:18793752"; MUTAGEN 145; /note="D->A: Loss of autoproteolytic cleavage and loss of enzyme activity."; /evidence="ECO:0000269|PubMed:18793752"; MUTAGEN 152; /note="L->F: Strongly reduced enzyme activity both with liposome-bound and Triton-solubilized substrate."; /evidence="ECO:0000269|PubMed:30301806"; MUTAGEN 195; /note="E->A,Q: Abolishes decrease of enzyme activity at pH 6 and pH 7."; /evidence="ECO:0000269|PubMed:18793752"; MUTAGEN 287; /note="N->D: Loss of autoproteolytic cleavage and loss of enzyme activity."; /evidence="ECO:0000269|PubMed:18793752"; MUTAGEN 309; /note="N->Q: Loss of one glycosylation site."; /evidence="ECO:0000269|PubMed:17980170"; MUTAGEN 333; /note="N->Q: Loss of one glycosylation site."; /evidence="ECO:0000269|PubMed:17980170
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000269|PubMed:15655246, ECO:0000269|PubMed:17980170, ECO:0000269|PubMed:18793752, ECO:0000269|PubMed:22040171, ECO:0000269|PubMed:30301806}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:17980170, PubMed:18793752, PubMed:30301806). Tunicamycin treatment causes a reduction in specific activity against N-palmitoylethanolamine. {ECO:0000269|PubMed:15655246, ECO:0000269|PubMed:17980170, ECO:0000269|PubMed:18793752, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22040171, ECO:0000269|PubMed:30301806}.; PTM: A disulfide bond is seen in the crystal structure of the human protein, but the Cys residues are not conserved in rodents. {ECO:0000269|PubMed:30301806}.; PTM: Autoproteolytic cleavage at pH 4.5 gives rise to the alpha and beta subunit (PubMed:15655246, PubMed:17980170, PubMed:18793752, PubMed:22040171, PubMed:30301806). Cleavage gives rise to a conformation change that activates the enzyme (PubMed:17980170, PubMed:18793752, PubMed:22040171, PubMed:30301806). The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates (Probable) (PubMed:17980170, PubMed:18793752). {ECO:0000269|PubMed:15655246, ECO:0000269|PubMed:17980170, ECO:0000269|PubMed:18793752, ECO:0000269|PubMed:22040171, ECO:0000269|PubMed:30301806, ECO:0000305|PubMed:30301806}.
uniprot
proteins
protein_family
Acid ceramidase family
uniprot
proteins
pubmed
10610717
uniprot
proteins
pubmed
1446826
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15655246
uniprot
proteins
pubmed
17980170
uniprot
proteins
pubmed
18793752
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
22040171
uniprot
proteins
pubmed
22825852
uniprot
proteins
pubmed
30301806
uniprot
proteins
sequence_length
359
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000305|PubMed:10610717, ECO:0000305|PubMed:15655246, ECO:0000305|PubMed:18793752}. Membrane {ECO:0000269|PubMed:30301806}; Peripheral membrane protein {ECO:0000269|PubMed:30301806}.
uniprot
proteins