U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

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

Gene ID: 67111, updated on 16-Apr-2024

Summary

Go to the top of the page Help
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
NEW
Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help
See Naaa in Genome Data Viewer
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

Go to the top of the page Help

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help
  • 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

Go to the top of the pageHelp

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

Go to the top of the page Help

Alleles

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

Pathways from PubChem

Go to the top of the page

General gene information

Go to the top of the page Help

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

Go to the top of the page Help
Preferred Names
N-acylethanolamine-hydrolyzing acid amidase
Names
ASAH-like protein
acylsphingosine deacylase NAAA
NP_001157159.1
NP_080248.2

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

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.

Chemical Information
Molecular Biology Databases
Research Materials
Tools
Miscellaneous