ID A0A340X5V1_LIPVE Unreviewed; 267 AA. AC A0A340X5V1; DT 10-OCT-2018, integrated into UniProtKB/TrEMBL. DT 10-OCT-2018, sequence version 1. DT 24-JUL-2024, entry version 25. DE RecName: Full=Serotonin N-acetyltransferase {ECO:0000256|ARBA:ARBA00039398}; DE EC=2.3.1.87 {ECO:0000256|ARBA:ARBA00039114}; DE AltName: Full=Aralkylamine N-acetyltransferase {ECO:0000256|ARBA:ARBA00042928}; GN Name=AANAT {ECO:0000313|RefSeq:XP_007454465.1}; OS Lipotes vexillifer (Yangtze river dolphin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti; OC Lipotidae; Lipotes. OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007454465.1}; RN [1] {ECO:0000313|RefSeq:XP_007454465.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (APR-2024) to UniProtKB. CC -!- FUNCTION: Controls the night/day rhythm of melatonin production in the CC pineal gland. Catalyzes the N-acetylation of serotonin into N- CC acetylserotonin, the penultimate step in the synthesis of melatonin. CC {ECO:0000256|ARBA:ARBA00037098}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine CC + CoA + H(+); Xref=Rhea:RHEA:20497, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:55469, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, CC ChEBI:CHEBI:77827; EC=2.3.1.87; CC Evidence={ECO:0000256|ARBA:ARBA00036561}; CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis; CC melatonin from serotonin: step 1/2. {ECO:0000256|ARBA:ARBA00037926}. CC -!- SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily. CC {ECO:0000256|ARBA:ARBA00038182}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_007454465.1; XM_007454403.1. DR STRING; 118797.A0A340X5V1; -. DR GeneID; 103071739; -. DR KEGG; lve:103071739; -. DR CTD; 15; -. DR InParanoid; A0A340X5V1; -. DR OrthoDB; 1327238at2759; -. DR Proteomes; UP000265300; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IEA:TreeGrafter. DR GO; GO:0007623; P:circadian rhythm; IEA:TreeGrafter. DR GO; GO:0030187; P:melatonin biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009416; P:response to light stimulus; IEA:TreeGrafter. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR051635; SNAT-like. DR PANTHER; PTHR10908; SEROTONIN N-ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10908:SF0; SEROTONIN N-ACETYLTRANSFERASE; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108}; KW Melatonin biosynthesis {ECO:0000256|ARBA:ARBA00043260}; KW Reference proteome {ECO:0000313|Proteomes:UP000265300}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 105..256 FT /note="N-acetyltransferase" FT /evidence="ECO:0000259|PROSITE:PS51186" FT REGION 1..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..54 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 267 AA; 29115 MW; 430A2BED4E8811F1 CRC64; MWGEKVEEGG QGDVQDVGLC KGGTATSKKC TSADDQGKRQ TVTRGPSAEG PSSSQRPLLK LGPPRVAAAA RRSTQSIHYL KPVALRLPPG IPESPSHQRH HTLPTEFRCL IPEDAPAFIS VSGICPLNLD QVRHFLALCP ELSLDWFVEG CLVAFIVGSL WAEERLTLES LTLHRPGGRT AHLHVLAVHR PFWQQGKGSI LLXRHLHHLG GHSGVHPAVL TCEDRLVPFY QRFGFHPVGP CAVGSLAFXE TQCSLRGHAS PHRHTDC //