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    AANAT aralkylamine N-acetyltransferase [ Ovis aries (sheep) ]

    Gene ID: 443531, updated on 10-Sep-2025
    Gene symbol
    AANAT
    Gene description
    aralkylamine N-acetyltransferase
    See related
    Ensembl:ENSOARG00020054683
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Ovis aries
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Caprinae; Ovis
    Also known as
    SNAT; AA-NAT
    NEW
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    See AANAT in Genome Data Viewer
    Location:
    chromosome: 11
    Exon count:
    4
    Annotation release Status Assembly Chr Location
    RS_2023_10 current ARS-UI_Ramb_v3.0 (GCF_016772045.2) 11 NC_056064.1 (54628621..54630556, complement)

    Chromosome 11 - NC_056064.1Genomic Context describing neighboring genes Neighboring gene rhomboid 5 homolog 2 Neighboring gene serotonin N-acetyltransferase-like Neighboring gene ubiquitin conjugating enzyme E2 O Neighboring gene uncharacterized LOC132657364 Neighboring gene sphingosine kinase 1

    Genomic Sequence:
    NC_056064.1 Chromosome 11 Reference ARS-UI_Ramb_v3.0 Primary Assembly

    Go to nucleotide: Graphics FASTA GenBank

    • Project title: Ovis aries Rambouillet Genome sequencing and assembly
    • BioProject: PRJNA414087
    • Analysis date: Thu Jan 09 10:41:41 2025

    Related articles in PubMed

    1. Interleukin-1 β Modulates Melatonin Secretion in Ovine Pineal Gland: Ex Vivo Study. Herman AP, et al. Biomed Res Int, 2015. PMID 26339621, Free PMC Article
    2. Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87). Pavlicek J, et al. J Biol Chem, 2008 May 23. PMID 18362150, Free PMC Article
    3. The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog. Hickman AB, et al. Cell, 1999 Apr 30. PMID 10319816
    4. Structurally constrained residues outside the binding motif are essential in the interaction of 14-3-3 and phosphorylated partner. Uhart M, et al. J Mol Biol, 2011 Mar 4. PMID 21216250
    5. Melatonin synthesis: analysis of the more than 150-fold nocturnal increase in serotonin N-acetyltransferase messenger ribonucleic acid in the rat pineal gland. Roseboom PH, et al. Endocrinology, 1996 Jul. PMID 8770929

    See all (7) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Our study proves that IL-1beta suppresses melatonin secretion and its action seems to be targeted on the reduction of pineal AA-NAT protein expression
      Title: Interleukin-1 β Modulates Melatonin Secretion in Ovine Pineal Gland: Ex Vivo Study.
    2. These results support that serotonin N-Acetyltransferase phosphorylation is not sufficient for complex formation with 14-3-3, as structurally constrained anchor residues play a critical function in stabilizing the protein-protein interaction.
      Title: Structurally constrained residues outside the binding motif are essential in the interaction of 14-3-3 and phosphorylated partner.
    3. structural kink and local rigidity imposed by Pro-64 may enhance activity by favoring configurations of Loop 1 that facilitate catalysis and do not become immobilized by intramolecular interactions
      Title: Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87).
    Submit: New GeneRIF Correction

    Markers

    Homology

    Gene Ontology Provided by RefSeq

    Function Evidence Code Pubs
    enables aralkylamine N-acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in circadian rhythm IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in melatonin biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in response to light stimulus IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Preferred Names
    serotonin N-acetyltransferase
    Names
    arylalkylamine N-acetyltransferase
    pineal serotonin N-acetyltransferase
    serotonin acetylase
    NP_001009461.1

    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_001009461.1 → NP_001009461.1  serotonin N-acetyltransferase

      See identical proteins and their annotated locations for NP_001009461.1

      Status: PROVISIONAL

      Source sequence(s)
      U29663
      UniProtKB/Swiss-Prot
      Q29495
      UniProtKB/TrEMBL
      M4MEU5, W5PB64
      Related
      ENSOARP00020079923.1, ENSOART00020176979.1
      Conserved Domains (1) summary
      cl17182
      Location:36 → 183
      NAT_SF; N-Acyltransferase superfamily: Various enyzmes that characteristicly catalyze the transfer of an acyl group to a substrate

    RefSeqs of Annotated Genomes: GCF_016772045.2-RS_2023_10

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

    Reference ARS-UI_Ramb_v3.0 Primary Assembly

    Genomic

    1. NC_056064.1 Reference ARS-UI_Ramb_v3.0 Primary Assembly

      Range
      54628621..54630556 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q29495.1 GenPept UniProtKB/Swiss-Prot:Q29495

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