ID:SNAT_HUMAN DESCRIPTION: RecName: Full=Serotonin N-acetyltransferase; Short=Serotonin acetylase; EC=2.3.1.87; AltName: Full=Aralkylamine N-acetyltransferase; Short=AA-NAT; FUNCTION: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N- acetylserotonin, the penultimate step in the synthesis of melatonin. CATALYTIC ACTIVITY: Acetyl-CoA + a 2-arylethylamine = CoA + an N- acetyl-2-arylethylamine. BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for tryptamine; KM=2.6 mM for 5-hydroxytryptamine; KM=0.55 mM for phenylethylamine; KM=10.6 mM for tyramine; PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2. SUBUNIT: Monomer (By similarity). Interacts with several 14-3-3 proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when phosphorylated at Thr-31. Phosphorylation on Ser-205 also allows binding to YWHAZ, but with lower affinity. The interaction with YWHAZ considerably increases affinity for arylalkylamines and acetyl-CoA and protects the enzyme from dephosphorylation and proteasomal degradation (By similarity). It may also prevent thiol-dependent inactivation (By similarity). SUBCELLULAR LOCATION: Cytoplasm. TISSUE SPECIFICITY: Highly expressed in pineal gland and at lower levels in the retina. Weak expression in several brain regions and in the pituitary gland. PTM: cAMP-dependent phosphorylation on both N-terminal Thr-31 and C-terminal Ser-205 regulates AANAT activity by promoting interaction with 14-3-3 proteins. DISEASE: Defects in AANAT are a cause of susceptibility to delayed sleep phase syndrome (DSPS) [MIM:614163]. A circadian rhythm sleep disorder characterized by sleep-onset insomnia and difficulty in awakening at the desired time. Patients with DSPS have chronic difficulty in adjusting their sleep-onset and wake-up times to occupational, school, and social activities. Note=Susceptibility to delayed sleep phase syndrome can be conferred by variant Thr- 129. Thr-129 shows a significantly higher frequency in affected individuals than in healthy controls. SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily. SIMILARITY: Contains 1 N-acetyltransferase domain. WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=AANAT";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q16613
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
