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

Summary

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 DNA-binding transcription factor binding activity and hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides. Predicted to be involved in several processes, including N-acylethanolamine metabolic process; N-acylphosphatidylethanolamine metabolic process; and sphingosine metabolic 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, Nov 2024]
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

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_000071.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

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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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

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.
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.
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.
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.
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.
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.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (2)
Targeted (3) 1 citation

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables DNA-binding transcription factor binding	IEA Inferred from Electronic Annotation more info
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-(long-chain-acyl)ethanolamine deacylase activity	ISS Inferred from Sequence or Structural Similarity more info
enables N-acylsphingosine amidohydrolase activity	ISO Inferred from Sequence Orthology more info
enables N-acylsphingosine amidohydrolase activity	ISS Inferred from Sequence or Structural Similarity more info
enables fatty acid amide hydrolase activity	ISO Inferred from Sequence Orthology more info
enables fatty acid amide hydrolase activity	ISS Inferred from Sequence or Structural Similarity 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-acylethanolamine metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in N-acylphosphatidylethanolamine metabolic process	ISO Inferred from Sequence Orthology more info
involved_in N-acylphosphatidylethanolamine metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in fatty acid metabolic process	IEA Inferred from Electronic Annotation more info
involved_in fatty acid metabolic process	ISO Inferred from Sequence Orthology more info
involved_in fatty acid metabolic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in lipid catabolic process	IEA Inferred from Electronic Annotation more info
involved_in sphingosine metabolic process	ISO Inferred from Sequence Orthology more info
involved_in sphingosine metabolic process	ISS Inferred from Sequence or Structural Similarity 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 lysosome	ISS Inferred from Sequence or Structural Similarity more info
located_in membrane	ISO Inferred from Sequence Orthology more info
located_in membrane	ISS Inferred from Sequence or Structural Similarity 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

EC 3.5.1.23

EC 3.5.1.60

NP_080248.2

EC 3.5.1.23

EC 3.5.1.60

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)

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
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