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    Naaa N-acylethanolamine acid amidase [ Mus musculus (house mouse) ]

    Gene ID: 67111, updated on 21-Apr-2024

    Summary

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    Official Symbol
    Naaaprovided by MGI
    Official Full Name
    N-acylethanolamine acid amidaseprovided by MGI
    Primary source
    MGI:MGI:1914361
    See related
    Ensembl:ENSMUSG00000029413 AllianceGenome:MGI:1914361
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Mus musculus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
    Also known as
    Asahl; 2210023K21Rik; 3830414F09Rik
    Summary
    Predicted to enable N-(long-chain-acyl)ethanolamine deacylase activity; N-acylsphingosine amidohydrolase activity; and fatty acid amide hydrolase activity. Predicted to be involved in several processes, including N-acylethanolamine metabolic process; N-acylphosphatidylethanolamine metabolic process; and sphingosine metabolic process. Predicted to act upstream of or within lipid catabolic process. Located in lysosome. Is expressed in future brain and ventricular layer. Orthologous to human NAAA (N-acylethanolamine acid amidase). [provided by Alliance of Genome Resources, Apr 2022]
    Expression
    Ubiquitous expression in mammary gland adult (RPKM 35.5), lung adult (RPKM 32.3) and 25 other tissues See more
    Orthologs
    human all
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    Genomic context

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    Location:
    5 E2; 5 46.35 cM
    Exon count:
    11
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCm39 (GCF_000001635.27) 5 NC_000071.7 (92405519..92426040, complement)
    108.20200622 previous assembly GRCm38.p6 (GCF_000001635.26) 5 NC_000071.6 (92257660..92278181, complement)

    Chromosome 5 - NC_000071.7Genomic Context describing neighboring genes Neighboring gene predicted gene, 42112 Neighboring gene protein phosphatase, EF hand calcium-binding domain 2 Neighboring gene CapStarr-seq enhancer MGSCv37_chr5:92674514-92674783 Neighboring gene STARR-positive B cell enhancer ABC_E10329 Neighboring gene STARR-positive B cell enhancer ABC_E2750 Neighboring gene SDA1 domain containing 1 Neighboring gene STARR-seq mESC enhancer starr_13638 Neighboring gene predicted gene, 23031 Neighboring gene C-X-C motif chemokine ligand 9

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: Mouse ENCODE transcriptome data
    • Description: RNA profiling data sets generated by the Mouse ENCODE project.
    • BioProject: PRJNA66167
    • Publication: PMID 25409824
    • Analysis date: n/a

    Bibliography

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    Related articles in PubMed

    1. Targeting NAAA counters dopamine neuron loss and symptom progression in mouse models of parkinsonism. Palese F, et al. Pharmacol Res, 2022 Aug. PMID 35781057, Free PMC Article
    2. Genetic Blockade of NAAA Cell-specifically Regulates Fatty Acid Ethanolamides (FAEs) Metabolism and Inflammatory Responses. Xie X, et al. Front Pharmacol, 2021. PMID 35069223, Free PMC Article
    3. N-Acylethanolamine Acid Amidase contributes to disease progression in a mouse model of multiple sclerosis. Pontis S, et al. Pharmacol Res, 2020 Oct. PMID 32634582
    4. N-Acylethanolamine-hydrolyzing acid amidase inhibition increases colon N-palmitoylethanolamine levels and counteracts murine colitis. Alhouayek M, et al. FASEB J, 2015 Feb. PMID 25384424, Free PMC Article
    5. Antinociceptive effects of the N-acylethanolamine acid amidase inhibitor ARN077 in rodent pain models. Sasso O, et al. Pain, 2013 Mar. PMID 23218523, Free PMC Article

    See all (28) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. NAAA-regulated lipid signaling in monocytes controls the induction of hyperalgesic priming in mice.
      Title: NAAA-regulated lipid signaling in monocytes controls the induction of hyperalgesic priming in mice.
    2. N-Acylethanolamine Acid Amidase contributes to disease progression in a mouse model of multiple sclerosis.
      Title: N-Acylethanolamine Acid Amidase contributes to disease progression in a mouse model of multiple sclerosis.
    3. Both inhibitors reduced several markers of macrophage activation, such as mRNA expression of inflammatory mediators, as well as cytokine and prostaglandin production, with however some differences between FAAH and NAAA inhibition. Our results support an important role for inhibition of NAE hydrolysis and NAAA inhibition in particular in controlling macrophage activation, and thus inflammation.
      Title: N-acylethanolamine-hydrolyzing acid amidase and fatty acid amide hydrolase inhibition differentially affect N-acylethanolamine levels and macrophage activation.
    4. NAAA inhibition increases palmitoylethanolamide levels in the colon and reduces colon inflammation and systemic inflammation
      Title: N-Acylethanolamine-hydrolyzing acid amidase inhibition increases colon N-palmitoylethanolamine levels and counteracts murine colitis.
    5. NAAA regulates peripheral pain initiation by interrupting endogenous fatty acid ethanolamide signaling at PPAR-alpha.
      Title: Antinociceptive effects of the N-acylethanolamine acid amidase inhibitor ARN077 in rodent pain models.
    6. Results suggest that N-acylethanolamine-hydrolyzing acid amidase and fatty acid amide hydrolase cooperatively degrade anandamide and other N-acylethanolamines in macrophages.
      Title: Involvement of N-acylethanolamine-hydrolyzing acid amidase in the degradation of anandamide and other N-acylethanolamines in macrophages.
    Submit: New GeneRIF Correction

    Variation

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    Alleles

    Alleles of this type are documented at Mouse Genome Informatics  (MGI)
    • Targeted (3)  1 citation
    • Endonuclease-mediated (2) 

    Pathways from PubChem

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    General gene information

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    Homology

    Gene Ontology Provided by MGI

    Function Evidence Code Pubs
    enables DNA-binding transcription factor binding ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables N-(long-chain-acyl)ethanolamine deacylase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables N-acylsphingosine amidohydrolase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables ceramidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables fatty acid amide hydrolase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds ISO
    Inferred from Sequence Orthology
    more info
    		  
    Process Evidence Code Pubs
    involved_in N-acylethanolamine metabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in N-acylphosphatidylethanolamine metabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in fatty acid metabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    acts_upstream_of_or_within lipid catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within lipid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in sphingosine metabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in lysosome IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in lysosome ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in membrane ISO
    Inferred from Sequence Orthology
    more info
    		  

    General protein information

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    Preferred Names
    N-acylethanolamine-hydrolyzing acid amidase
    Names
    ASAH-like protein
    acylsphingosine deacylase NAAA
    NP_001157159.1
    NP_080248.2

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001163687.1 → NP_001157159.1  N-acylethanolamine-hydrolyzing acid amidase isoform 2 precursor

      See identical proteins and their annotated locations for NP_001157159.1

      Status: VALIDATED

      Description
      Transcript Variant: This variant (2) uses an alternate in-frame splice site in the coding region, compared to variant 1. This results in a shorter isoform (2), compared to isoform 1.
      Source sequence(s)
      AC125542, AK008776, AK017141, AK133485
      Consensus CDS
      CCDS51545.1
      UniProtKB/TrEMBL
      G3XA18, Q3V023
      Related
      ENSMUSP00000124582.2, ENSMUST00000159345.8
      Conserved Domains (2) summary
      cd01903
      Location:120 → 349
      Ntn_AC_NAAA; AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also known as N-acylsphingosine amidohydrolase), and N-acylethanolamine-hydrolyzing acid amidase (NAAA). AC catalyzes the hydrolysis of ceramide to sphingosine and ...
      pfam15508
      Location:36 → 124
      NAAA-beta; beta subunit of N-acylethanolamine-hydrolyzing acid amidase

    2. NM_025972.4 → NP_080248.2  N-acylethanolamine-hydrolyzing acid amidase isoform 1 precursor

      See identical proteins and their annotated locations for NP_080248.2

      Status: VALIDATED

      Description
      Transcript Variant: This variant (1) represents the longer transcript and encodes the longer isoform (1).
      Source sequence(s)
      AB162194, AC125542, AK008776, AK133485
      Consensus CDS
      CCDS19428.1
      UniProtKB/Swiss-Prot
      Q5KTC6, Q99KM3, Q9D6B4, Q9D7V9
      UniProtKB/TrEMBL
      Q3V023
      Related
      ENSMUSP00000108726.4, ENSMUST00000113102.10
      Conserved Domains (2) summary
      cd01903
      Location:122 → 351
      Ntn_AC_NAAA; AC_NAAA This conserved domain includes two closely related proteins, acid ceramidase (AC, also known as N-acylsphingosine amidohydrolase), and N-acylethanolamine-hydrolyzing acid amidase (NAAA). AC catalyzes the hydrolysis of ceramide to sphingosine and ...
      pfam15508
      Location:36 → 126
      NAAA-beta; beta subunit of N-acylethanolamine-hydrolyzing acid amidase

    RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference GRCm39 C57BL/6J

    Genomic

    1. NC_000071.7 Reference GRCm39 C57BL/6J

      Range
      92405519..92426040 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q9D7V9.2 GenPept UniProtKB/Swiss-Prot:Q9D7V9

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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