| Tag | Content |
|---|
| CPLM ID | CPLM-010918 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | N-acylethanolamine-hydrolyzing acid amidase |
Protein Synonyms/Alias | Acid ceramidase-like protein; N-acylsphingosine amidohydrolase-like; ASAH-like protein; N-acylethanolamine-hydrolyzing acid amidase subunit alpha; N-acylethanolamine-hydrolyzing acid amidase subunit beta |
Gene Name | NAAA |
Gene Synonyms/Alias | ASAHL; PLT |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 239 | AAVGKLAKTPLIADV | ubiquitination | [1] | | 292 | ETNYDHWKPAPKEDD | ubiquitination | [1] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] |
Functional Description | 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. |
Sequence Annotation | ACT_SITE 126 126 Nucleophile (Probable).
CARBOHYD 37 37 N-linked (GlcNAc...).
CARBOHYD 107 107 N-linked (GlcNAc...).
CARBOHYD 309 309 N-linked (GlcNAc...).
CARBOHYD 333 333 N-linked (GlcNAc...). |
Keyword | Alternative splicing; Autocatalytic cleavage; Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase; Lysosome; Polymorphism; Reference proteome; Signal; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 359 AA |
Protein Sequence | MRTADREARP GLPSLLLLLL AGAGLSAASP PAAPRFNVSL DSVPELRWLP VLRHYDLDLV 60
RAAMAQVIGD RVPKWVHVLI GKVVLELERF LPQPFTGEIR GMCDFMNLSL ADCLLVNLAY 120
ESSVFCTSIV AQDSRGHIYH GRNLDYPFGN VLRKLTVDVQ FLKNGQIAFT GTTFIGYVGL 180
WTGQSPHKFT VSGDERDKGW WWENAIAALF RRHIPVSWLI RATLSESENF EAAVGKLAKT 240
PLIADVYYIV GGTSPREGVV ITRNRDGPAD IWPLDPLNGA WFRVETNYDH WKPAPKEDDR 300
RTSAIKALNA TGQANLSLEA LFQILSVVPV YNNFTIYTTV MSAGSPDKYM TRIRNPSRK 359 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:MGI. GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IDA:MGI. GO:0006629; P:lipid metabolic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |