SNAT_MESAU
ID SNAT_MESAU Reviewed; 207 AA.
AC Q9R0A9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Serotonin N-acetyltransferase;
DE Short=Serotonin acetylase;
DE EC=2.3.1.87 {ECO:0000250|UniProtKB:Q29495};
DE AltName: Full=Aralkylamine N-acetyltransferase;
DE Short=AA-NAT;
GN Name=AANAT; Synonyms=SNAT;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Pineal gland;
RX PubMed=10407190; DOI=10.1016/s0169-328x(99)00175-8;
RA Gauer F., Poirel V.J., Garidou M.L., Simonneaux V., Pevet P.;
RT "Molecular cloning of the arylalkylamine-N-acetyltransferase and daily
RT variations of its mRNA expression in the syrian hamster pineal gland.";
RL Brain Res. Mol. Brain Res. 71:87-95(1999).
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:0000250|UniProtKB:Q29495}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-arylethylamine + acetyl-CoA = CoA + H(+) + N-acetyl-2-
CC arylethylamine; 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:0000250|UniProtKB:Q29495};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with several 14-3-3
CC proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when
CC phosphorylated at Thr-31 (By similarity). Phosphorylation on Ser-205
CC also allows binding to YWHAZ, but with lower affinity (By similarity).
CC The interaction with YWHAZ considerably increases affinity for
CC arylalkylamines and acetyl-CoA and protects the enzyme from
CC dephosphorylation and proteasomal degradation. It may also prevent
CC thiol-dependent inactivation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16613}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pineal gland and retina. Also
CC detected in heart and intestine. {ECO:0000269|PubMed:10407190}.
CC -!- INDUCTION: Exhibits night/day variations with an increased expression
CC at night in the pineal gland. {ECO:0000269|PubMed:10407190}.
CC -!- PTM: cAMP-dependent phosphorylation on both N-terminal Thr-31 and C-
CC terminal Ser-205 regulates AANAT activity by promoting interaction with
CC 14-3-3 proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily.
CC {ECO:0000305}.
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DR EMBL; AF092100; AAD55970.1; -; mRNA.
DR RefSeq; NP_001297491.1; NM_001310562.1.
DR AlphaFoldDB; Q9R0A9; -.
DR SMR; Q9R0A9; -.
DR GeneID; 101834092; -.
DR CTD; 15; -.
DR OrthoDB; 1528352at2759; -.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
DR GO; GO:0030187; P:melatonin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Biological rhythms; Cytoplasm; Melatonin biosynthesis;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..207
FT /note="Serotonin N-acetyltransferase"
FT /id="PRO_0000074582"
FT DOMAIN 35..194
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 124..126
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 132..137
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 168..170
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT SITE 120
FT /note="Important for the catalytic mechanism; involved in
FT substrate deprotonation"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT SITE 122
FT /note="Important for the catalytic mechanism; involved in
FT substrate deprotonation"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT MOD_RES 31
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O97756"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
SQ SEQUENCE 207 AA; 23385 MW; C179FC32F08C0734 CRC64;
MPMLSPHSLK PDTLHLPPGT SEFLGCQRRH TLPASEFRCL TPQDAISVFE IEREAFISVS
GTCPLYLDEI RHFLTLCPEL SLGWFEEGRL VAFIIGSLWD KERLTQESLT LHRPGGRTAH
LHVLAVHRTF RQQGKGSVLL WRYLHHLGSQ PAVRRAVLMC EDALVPFYEK FGFQAVGPCA
VTVGSLTFME LQCSLRCHAF LRRNSGC
