Q29495SNAT_SHEEPSerotonin N-acetyltransferaseSerotonin acetylase2.3.1.87Aralkylamine N-acetyltransferaseAA-NATAANATSNATOvis ariesSheepEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeCaprinaeOvisPineal serotonin N-acetyltransferase: expression cloning and molecular analysis.NUCLEOTIDE SEQUENCE [MRNA]TISSUE SPECIFICITYINDUCTIONcAMP regulation of arylalkylamine N-acetyltransferase (AANAT, EC 2.3.1.87): a new cell line (1E7) provides evidence of intracellular AANAT activation.INDUCTIONBIOPHYSICOCHEMICAL PROPERTIESRole of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-3-3-binding switch in melatonin synthesis.PHOSPHORYLATION AT THR-31INTERACTION WITH 14-3-3 PROTEINSIDENTIFICATION BY MASS SPECTROMETRYERRATUM OF PUBMED:11427721Cellular stabilization of the melatonin rhythm enzyme induced by nonhydrolyzable phosphonate incorporation.PHOSPHORYLATION AT THR-31INTERACTION WITH YWHAZIDENTIFICATION BY MASS SPECTROMETRYMelatonin synthesis: 14-3-3-dependent activation and inhibition of arylalkylamine N-acetyltransferase mediated by phosphoserine-205.FUNCTIONPHOSPHORYLATION AT THR-31 AND SER-205INDUCTIONINTERACTION WITH YWHAZMUTAGENESIS OF THR-31 AND SER-205Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87).CATALYTIC ACTIVITYMUTAGENESIS OF ILE-57; VAL-59; PRO-64 AND 63-CYS--LEU-65The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog.X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-195 IN COMPLEX WITH COA-S-ACETYLTRYPTAMINEIDENTIFICATION BY MASS SPECTROMETRYCATALYTIC ACTIVITYMUTAGENESIS OF HIS-120; HIS-122 AND TYR-168Melatonin biosynthesis: the structure of serotonin N-acetyltransferase at 2.5 A resolution suggests a catalytic mechanism.X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-201IDENTIFICATION BY MASS SPECTROMETRYMUTAGENESIS OF CYS-160Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation.X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-201 IN COMPLEX WITH THE ACETYL-COA AND SUBSTRATE ANALOG COA-S-ACETYLTRYPTAMINE AND YWHAZAFFINITY FOR ACETYL-COA AND SEROTONINInvestigation of the roles of catalytic residues in serotonin N-acetyltransferase.X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT PHE-168 IN COMPLEX WITH SUBSTRATE ANALOGCATALYTIC ACTIVITYBIOPHYSICOCHEMICAL PROPERTIESMUTAGENESIS OF HIS-120; HIS-122 AND TYR-168X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition.X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ACETYL-COA AND SUBSTRATE ANALOGSCATALYTIC ACTIVITYMUTAGENESIS OF CYS-160 AND GLU-161Controls 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.a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine + CoA + H(+)0.29 mM for acetyl-CoA0.17 mM for tryptamine0.2 mM for tryptamine0.31 mM for 5-hydroxytryptamine3.4 mM for phenylethylamine3.4 mM for tyramineAromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.Monomer. 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 a 10-fold lower affinity. The interaction with YWHAZ considerably increases affinity for arylalkylamines and acetyl-CoA and protects the enzyme from dephosphorylation and proteasomal degradation. It may also prevent thiol-dependent inactivation. The physiological stoichiometry of the interaction is not clear. In vitro studies show either 1:2 (i.e. 1 AANAT molecule per YWHAZ dimer) (PubMed:11427721) or 2:2 (PubMed:11336675).Q29495P63104true3CytoplasmHighest expression in the pineal gland, followed by retina. Expressed at much lower levels in brainstem and pituitary gland. AANAT activity also detected at low levels in the olfactory lobe.Exhibits night/day variations with a 7-fold increased activity at night. At the mRNA level, the nocturnal increase is lower than 2-fold.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.Belongs to the acetyltransferase family. AANAT subfamily.3D-structureAcyltransferaseBiological rhythmsCytoplasmMelatonin biosynthesisPhosphoproteinReference proteomeTransferaseacetyl-CoAsubstrateacetyl-CoAsubstrateacetyl-CoATAIAVAPAGWHAHQHAHQCACSEAYFSGMSTPSVHCLKPSPLHLPSGIPGSPGRQRRHTLPANEFRCLTPEDAAGVFEIEREAFISVSGNCPLNLDEVQHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESLALHRPRGHSAHLHALAVHRSFRQQGKGSVLLWRYLHHVGAQPAVRRAVLMCEDALVPFYQRFGFHPAGPCAIVVGSLTFTEMHCSLRGHAALRRNSDR
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