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Database: UniProt
Entry: G3SMY2_LOXAF
LinkDB: G3SMY2_LOXAF
Original site: G3SMY2_LOXAF 
ID   G3SMY2_LOXAF            Unreviewed;       207 AA.
AC   G3SMY2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
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|Ensembl:ENSLAFP00000000912.2};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000000912.2, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000000912.2, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000912.2,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000000912.2}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000912.2};
RG   Ensembl;
RL   Submitted (NOV-2023) 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}.
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DR   RefSeq; XP_010595231.1; XM_010596929.1.
DR   AlphaFoldDB; G3SMY2; -.
DR   STRING; 9785.ENSLAFP00000000912; -.
DR   Ensembl; ENSLAFT00000001085.2; ENSLAFP00000000912.2; ENSLAFG00000001085.2.
DR   GeneID; 100667906; -.
DR   KEGG; lav:100667906; -.
DR   CTD; 15; -.
DR   eggNOG; KOG4144; Eukaryota.
DR   GeneTree; ENSGT00390000015579; -.
DR   HOGENOM; CLU_061829_3_1_1; -.
DR   InParanoid; G3SMY2; -.
DR   OMA; HFLNLCP; -.
DR   OrthoDB; 1327238at2759; -.
DR   TreeFam; TF331622; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0004060; F:arylamine N-acetyltransferase activity; IEA:Ensembl.
DR   GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR   GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0030187; P:melatonin biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd04301; NAT_SF; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
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:UP000007646};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          35..196
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
SQ   SEQUENCE   207 AA;  23466 MW;  00059464B22AB495 CRC64;
     MSTQSVHALK LATLWLPPEV PDSPSRQRRH TLPASEFRCL SPEDATSVFE VEREAFISVS
     GLCPLYLDEI RHFLIMCPEL SLGWFEEGRL VAFIIGSLWD EERLTQESLT LHRPGGRTAH
     LHVLAVNHNF RQQGKGSVLL WRYLQHLGRQ PALCRVVLMC EDPLVPFYEK FGFRAVGPCA
     VTVVSLAFIE LQCSLRGHAF LRRNSGC
//
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