N-acylethanolamine-hydrolyzing acid amidase

Details

Name
N-acylethanolamine-hydrolyzing acid amidase
Synonyms
  • 3.5.1.-
  • Acid ceramidase-like protein
  • ASAH-like protein
  • ASAHL
  • N-acylsphingosine amidohydrolase-like
  • PLT
Gene Name
NAAA
Organism
Humans
Amino acid sequence
>lcl|BSEQ0051335|N-acylethanolamine-hydrolyzing acid amidase
MRTADREARPGLPSLLLLLLAGAGLSAASPPAAPRFNVSLDSVPELRWLPVLRHYDLDLV
RAAMAQVIGDRVPKWVHVLIGKVVLELERFLPQPFTGEIRGMCDFMNLSLADCLLVNLAY
ESSVFCTSIVAQDSRGHIYHGRNLDYPFGNVLRKLTVDVQFLKNGQIAFTGTTFIGYVGL
WTGQSPHKFTVSGDERDKGWWWENAIAALFRRHIPVSWLIRATLSESENFEAAVGKLAKT
PLIADVYYIVGGTSPREGVVITRNRDGPADIWPLDPLNGAWFRVETNYDHWKPAPKEDDR
RTSAIKALNATGQANLSLEALFQILSVVPVYNNFTIYTTVMSAGSPDKYMTRIRNPSRK
Number of residues
359
Molecular Weight
40065.65
Theoretical pI
Not Available
GO Classification
Functions
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / transcription factor binding
Processes
lipid metabolic process / neurotransmitter secretion
Components
cytoplasm / extracellular exosome / lysosomal lumen / presynapse
General 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.
Specific Function
Hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Lysosome
Gene sequence
>lcl|BSEQ0051336|N-acylethanolamine-hydrolyzing acid amidase (NAAA)
ATGCGGACCGCGGACCGGGAGGCGCGCCCGGGGCTTCCGTCCCTGCTGCTGCTGCTGCTG
GCCGGGGCCGGGCTGTCAGCCGCCTCGCCCCCAGCAGCGCCGCGCTTCAACGTGAGCCTG
GACTCGGTCCCCGAGCTGCGCTGGCTGCCCGTGCTGCGGCACTACGACTTGGACTTGGTG
CGCGCCGCGATGGCGCAAGTCATCGGGGACAGAGTCCCCAAGTGGGTGCACGTGTTAATC
GGAAAAGTGGTCCTGGAGCTGGAGCGCTTCCTGCCCCAGCCCTTCACCGGCGAGATCCGC
GGCATGTGTGACTTCATGAACCTCAGCCTGGCGGACTGCCTTCTGGTCAACCTGGCCTAC
GAGTCCTCCGTGTTCTGCACCAGTATTGTGGCTCAAGACTCCAGAGGCCACATTTACCAT
GGTCGGAATTTGGATTATCCTTTTGGGAATGTCTTACGCAAGCTGACAGTGGATGTGCAA
TTCTTAAAGAATGGGCAGATTGCATTCACAGGAACTACTTTTATTGGCTATGTAGGATTA
TGGACTGGCCAGAGCCCACACAAGTTTACAGTTTCTGGTGATGAACGAGATAAAGGCTGG
TGGTGGGAGAATGCTATCGCTGCCCTGTTTCGGAGACACATTCCCGTCAGCTGGCTGATC
CGCGCTACCCTGAGTGAGTCGGAAAACTTCGAAGCAGCTGTTGGCAAGTTGGCCAAGACT
CCCCTTATTGCTGATGTTTATTACATTGTTGGTGGCACGTCCCCCCGGGAGGGGGTGGTC
ATCACGAGGAACAGAGATGGCCCAGCAGACATTTGGCCTCTAGATCCTTTGAATGGAGCG
TGGTTCCGAGTTGAGACAAATTACGACCACTGGAAGCCAGCACCCAAGGAAGATGACCGG
AGAACATCTGCCATCAAGGCCCTTAATGCTACAGGACAAGCAAACCTCAGCCTGGAGGCA
CTTTTCCAGATTTTGTCGGTGGTTCCAGTTTATAACAACTTCACAATTTATACTACGGTA
ATGAGCGCCGGTAGCCCAGACAAGTACATGACTAGGATCAGAAACCCGAGTAGAAAGTAA
Chromosome Location
4
Locus
4q21.1
External Identifiers
ResourceLink
UniProtKB IDQ02083
UniProtKB Entry NameNAAA_HUMAN
HGNC IDHGNC:736
General References
  1. Hong SB, Li CM, Rhee HJ, Park JH, He X, Levy B, Yoo OJ, Schuchman EH: Molecular cloning and characterization of a human cDNA and gene encoding a novel acid ceramidase-like protein. Genomics. 1999 Dec 1;62(2):232-41. doi: 10.1006/geno.1999.5953. [PubMed:10610717]
  2. Tsuboi K, Sun YX, Okamoto Y, Araki N, Tonai T, Ueda N: Molecular characterization of N-acylethanolamine-hydrolyzing acid amidase, a novel member of the choloylglycine hydrolase family with structural and functional similarity to acid ceramidase. J Biol Chem. 2005 Mar 25;280(12):11082-92. doi: 10.1074/jbc.M413473200. Epub 2005 Jan 17. [PubMed:15655246]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  4. Goodchild NL, Wilkinson DA, Mager DL: A human endogenous long terminal repeat provides a polyadenylation signal to a novel, alternatively spliced transcript in normal placenta. Gene. 1992 Nov 16;121(2):287-94. [PubMed:1446826]
  5. West JM, Zvonok N, Whitten KM, Wood JT, Makriyannis A: Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase. J Proteome Res. 2012 Feb 3;11(2):972-81. doi: 10.1021/pr200735a. Epub 2012 Jan 3. [PubMed:22040171]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. [PubMed:19159218]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB14009Medical Cannabisexperimental, investigationalunknowninhibitorDetails
DB14011NabiximolsinvestigationalunknowninhibitorDetails
DB09061Cannabidiolapproved, investigationalunknowninhibitorDetails