U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

NAAA N-acylethanolamine acid amidase [ Orcinus orca (killer whale) ]

Gene ID: 101290237, updated on 8-Mar-2024

Summary

Go to the top of the page Help
Gene symbol
NAAA
Gene description
N-acylethanolamine acid amidase
See related
EnsemblRapid:ENSOORG00010022859
Gene type
protein coding
RefSeq status
MODEL
Organism
Orcinus orca
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti; Delphinidae; Orcinus
Orthologs
human mouse 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:
chromosome: 4
Exon count:
14
Annotation release Status Assembly Chr Location
RS_2023_02 current mOrcOrc1.1 (GCF_937001465.1) 4 NC_064562.1 (48713013..48749482)

Chromosome 4 - NC_064562.1Genomic Context describing neighboring genes Neighboring gene SDA1 domain containing 1 Neighboring gene mitochondrial import inner membrane translocase subunit Tim17-B-like Neighboring gene uncharacterized LOC125964288 Neighboring gene protein phosphatase with EF-hand domain 2

Genomic regions, transcripts, and products

Go to the top of the page Help
Genomic Sequence:
NC_064562.1 Chromosome 4 Reference mOrcOrc1.1 Primary Assembly

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the pageHelp

Related articles in PubMed

  1. Manual GO annotation of predictive protein signatures: the InterPro approach to GO curation. Burge S, et al. Database (Oxford), 2012. PMID 22301074, Free PMC Article

GeneRIFs: Gene References Into Functions

General gene information

Go to the top of the page Help

Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables fatty acid amide hydrolase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in fatty acid metabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in lysosome IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

Go to the top of the page Help
Preferred Names
N-acylethanolamine-hydrolyzing acid amidase

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs of Annotated Genomes: GCF_937001465.1-RS_2023_02

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

Reference mOrcOrc1.1 Primary Assembly

Genomic

  1. NC_064562.1 Reference mOrcOrc1.1 Primary Assembly

    Range
    48713013..48749482
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_033406507.2 → XP_033262398.1  N-acylethanolamine-hydrolyzing acid amidase isoform X3

    Conserved Domains (2) summary
    pfam15508
    Location:31 → 89
    NAAA-beta; beta subunit of N-acylethanolamine-hydrolyzing acid amidase
    cl00467
    Location:115 → 279
    Ntn_hydrolase; The Ntn hydrolases (N-terminal nucleophile) are a diverse superfamily of of enzymes that are activated autocatalytically via an N-terminally lcated nucleophilic amino acid. N-terminal nucleophile (NTN-) hydrolase superfamily, which contains a ...

  2. XM_049709405.1 → XP_049565362.1  N-acylethanolamine-hydrolyzing acid amidase isoform X2

  3. XM_012536869.3 → XP_012392323.1  N-acylethanolamine-hydrolyzing acid amidase isoform X1

    See identical proteins and their annotated locations for XP_012392323.1

    Conserved Domains (2) summary
    cd01903
    Location:115 → 344
    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:31 → 89
    NAAA-beta; beta subunit of N-acylethanolamine-hydrolyzing acid amidase

  4. XM_012536870.3 → XP_012392324.1  N-acylethanolamine-hydrolyzing acid amidase isoform X1

    See identical proteins and their annotated locations for XP_012392324.1

    Conserved Domains (2) summary
    cd01903
    Location:115 → 344
    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:31 → 89
    NAAA-beta; beta subunit of N-acylethanolamine-hydrolyzing acid amidase

  5. XM_033406505.2 → XP_033262396.1  N-acylethanolamine-hydrolyzing acid amidase isoform X1

    Conserved Domains (2) summary
    cd01903
    Location:115 → 344
    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:31 → 89
    NAAA-beta; beta subunit of N-acylethanolamine-hydrolyzing acid amidase

  6. XM_004280191.3 → XP_004280239.1  N-acylethanolamine-hydrolyzing acid amidase isoform X1

    See identical proteins and their annotated locations for XP_004280239.1

    Related
    ENSOORP00010030326.1, ENSOORT00010034221.1
    Conserved Domains (2) summary
    cd01903
    Location:115 → 344
    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:31 → 89
    NAAA-beta; beta subunit of N-acylethanolamine-hydrolyzing acid amidase

RNA

  1. XR_004477090.2 RNA Sequence

Nucleotide Protein
Heading Accession and Version

Gene LinkOut

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