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
- 分子量
- 40065.65
- Theoretical pI
- Not Available
- GO Classification
-
Functions水解酶活性,on carbon-nitrogen (but not peptide) bonds/transcription factor bindingProcesseslipid metabolic process/neurotransmitter secretionComponentscytoplasm/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
-
资源 Link UniProtKB ID Q02083 UniProtKB Entry Name NAAA_HUMAN HGNC ID HGNC:736 - General References
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- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]
- 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. [Article]