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Sequence of NAAA_HUMAN

EC Number:3.5.1.60

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
N-(long-chain-acyl)ethanolamine deacylase
Q02083
Homo sapiens
359
40066
Reaction
N-(long-chain-acyl)ethanolamine + H2O = a long-chain carboxylate + ethanolamine
Other sequences found for EC No. 3.5.1.60

General information:

Sequence
show sequence in fasta format
  0 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
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
193190
Hong S.-B.,Li C.-M.,Rhee H.-J.,Park J.-H.,He X.,Levy B.,Yoo O.J.,Schuchman E.H.
Molecular cloning and characterization of a human cDNA and gene encoding a novel acid ceramidase-like protein.
Genomics
62
232-241
1999
193191
Tsuboi K.,Sun Y.-X.,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.
280
11082-11092
2005
193192
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
193193
Goodchild N.L.,Wilkinson D.A.,Mager D.L.
A human endogenous long terminal repeat provides a polyadenylation signal to a novel, alternatively spliced transcript in normal placenta.
Gene
121
287-294
1992
193194
West J.M.,Zvonok N.,Whitten K.M.,Wood J.T.,Makriyannis A.
Mass spectrometric characterization of human N-acylethanolamine-hydrolyzing acid amidase.
J. Proteome Res.
11
972-981
2012
193195
Zhao L.Y.,Tsuboi K.,Okamoto Y.,Nagahata S.,Ueda N.
Proteolytic activation and glycosylation of N-acylethanolamine-hydrolyzing acid amidase, a lysosomal enzyme involved in the endocannabinoid metabolism.
Biochim. Biophys. Acta
1771
1397-1405
2007
193196
Wang J.,Zhao L.Y.,Uyama T.,Tsuboi K.,Tonai T.,Ueda N.
Amino acid residues crucial in pH regulation and proteolytic activation of N-acylethanolamine-hydrolyzing acid amidase.
Biochim. Biophys. Acta
1781
710-717
2008
193197
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.
8
651-661
2009
193198
Uyama T.,Ikematsu N.,Inoue M.,Shinohara N.,Jin X.H.,Tsuboi K.,Tonai T.,Tokumura A.,Ueda N.
Generation of N-acylphosphatidylethanolamine by members of the phospholipase A/acyltransferase (PLA/AT) family.
J. Biol. Chem.
287
31905-31919
2012
193199
Gorelik A.,Gebai A.,Illes K.,Piomelli D.,Nagar B.
Molecular mechanism of activation of the immunoregulatory amidase NAAA.
Proc. Natl. Acad. Sci. U.S.A.
115
0-0
2018