ID D1KS23_SOLSE Unreviewed; 201 AA. AC D1KS23; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-NOV-2024, entry version 26. 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=aanat1a {ECO:0000313|EMBL:ACY66879.1}; GN ORFNames=JOB18_021697 {ECO:0000313|EMBL:KAG7485960.1}; OS Solea senegalensis (Senegalese sole). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Carangaria; Pleuronectiformes; Pleuronectoidei; Soleidae; Solea. OX NCBI_TaxID=28829 {ECO:0000313|EMBL:ACY66879.1}; RN [1] {ECO:0000313|EMBL:ACY66879.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Brain {ECO:0000313|EMBL:ACY66879.1}; RA Isorna E., Falcon J., Aliaga M., El M'rabet A., Servili A., RA Munoz-Cueto J.A.; RT "Identification of two arylalkylamine N-acetyltranferase 1 genes with RT different developmental expression profile in the flatfish Solea RT senegalensis."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:KAG7485960.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sse05_10M {ECO:0000313|EMBL:KAG7485960.1}; RX PubMed=34188074; RA Guerrero-Cozar I., Gomez-Garrido J., Berbel C., Martinez-Blanch J.F., RA Alioto T., Claros M.G., Gagnaire P.A., Manchado M.; RT "Chromosome anchoring in Senegalese sole (Solea senegalensis) reveals sex- RT associated markers and genome rearrangements in flatfish."; RL Sci. Rep. 11:0-0(2021). RN [3] {ECO:0000313|EMBL:KAG7485960.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sse05_10M {ECO:0000313|EMBL:KAG7485960.1}; RC TISSUE=Blood {ECO:0000313|EMBL:KAG7485960.1}; RA Guerrero-Cozar I., Gomez-Garrido J., Berbel C., Martinez-Blanch J.F., RA Alioto T., Claros M.G., Gagnaire P.A., Manchado M.; RL Submitted (MAR-2021) to the EMBL/GenBank/DDBJ databases. 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 EMBL; GQ340971; ACY66879.1; -; mRNA. DR EMBL; JAGKHQ010000018; KAG7485960.1; -; Genomic_DNA. DR AlphaFoldDB; D1KS23; -. DR OrthoDB; 1327238at2759; -. DR Proteomes; UP000693946; Linkage Group LG6. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IEA:UniProtKB-EC. 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 CDD; cd04301; NAT_SF; 1. DR FunFam; 3.40.630.30:FF:000021; Serotonin N-acetyltransferase; 1. 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:SF4; ARYLALKYLAMINE N-ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10908; 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 2: Evidence at transcript level; KW Acyltransferase {ECO:0000313|EMBL:ACY66879.1}; KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108}; KW Melatonin biosynthesis {ECO:0000256|ARBA:ARBA00043260}; KW Transferase {ECO:0000313|EMBL:ACY66879.1}. FT DOMAIN 29..190 FT /note="N-acetyltransferase" FT /evidence="ECO:0000259|PROSITE:PS51186" SQ SEQUENCE 201 AA; 23053 MW; 10836E9F15E04E69 CRC64; MSVVSAAPFK PLYMRSPVPR GRRHTLPASE FRSLSPEDAV SVFEIEREAF ISVSGECPLH LDEVRHFLTL CPELSLGWFE EGRLVAFIIG SLWDQERLTM DALTLHKPHG TTVHIHVLAV HRTFRQQGKG SILMWRYLQY LRCLPYVRRA VLMCEDFLVP FYQKSGFKAQ GPSEITVGPL AFIEMFYPVR GHAFMRRNSG C //