SNAT_MACMU
ID SNAT_MACMU Reviewed; 204 AA.
AC O97756;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Serotonin N-acetyltransferase;
DE Short=Serotonin acetylase;
DE EC=2.3.1.87 {ECO:0000269|PubMed:12364461};
DE AltName: Full=Aralkylamine N-acetyltransferase;
DE Short=AA-NAT;
GN Name=AANAT; Synonyms=SNAT;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION, AND PHOSPHORYLATION AT THR-28.
RC TISSUE=Pineal gland;
RX PubMed=12364461; DOI=10.1210/jc.2002-020683;
RA Coon S.L., Del Olmo E., Young W.S. III, Klein D.C.;
RT "Melatonin synthesis enzymes in Macaca mulatta: focus on arylalkylamine N-
RT acetyltransferase (EC 2.3.1.87).";
RL J. Clin. Endocrinol. Metab. 87:4699-4706(2002).
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:0000269|PubMed:12364461}.
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:0000269|PubMed:12364461};
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-28 (By similarity). Phosphorylation on Ser-202
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 in the
CC photoreceptor outer segments in the retina. Expressed at about 100-fold
CC lower levels in the pituitary gland and testis. Not detected in other
CC tissues. {ECO:0000269|PubMed:12364461}.
CC -!- INDUCTION: Exhibits night/day variations with a 10-fold increased
CC protein levels and activity at night in the pineal gland and a 5-fold
CC increase in the retina. In both tissues, the mRNA levels remain
CC constant. {ECO:0000269|PubMed:12364461}.
CC -!- PTM: cAMP-dependent phosphorylation regulates AANAT activity by
CC promoting interaction with 14-3-3 proteins. Phosphorylation levels
CC exhibit night/day variations, with an increase during nighttime.
CC {ECO:0000269|PubMed:12364461}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily.
CC {ECO:0000305}.
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DR EMBL; U46661; AAD00061.2; -; mRNA.
DR RefSeq; NP_001040592.1; NM_001047127.1.
DR AlphaFoldDB; O97756; -.
DR SMR; O97756; -.
DR STRING; 9544.ENSMMUP00000034025; -.
DR iPTMnet; O97756; -.
DR Ensembl; ENSMMUT00000086699; ENSMMUP00000064346; ENSMMUG00000018970.
DR GeneID; 706924; -.
DR KEGG; mcc:706924; -.
DR CTD; 15; -.
DR VEuPathDB; HostDB:ENSMMUG00000018970; -.
DR VGNC; VGNC:69468; AANAT.
DR eggNOG; KOG4144; Eukaryota.
DR GeneTree; ENSGT00390000015579; -.
DR HOGENOM; CLU_061829_3_1_1; -.
DR InParanoid; O97756; -.
DR OMA; HKPGGHI; -.
DR OrthoDB; 1528352at2759; -.
DR TreeFam; TF331622; -.
DR BRENDA; 2.3.1.87; 3126.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000006718; Chromosome 16.
DR Bgee; ENSMMUG00000018970; Expressed in spermatid and 8 other tissues.
DR ExpressionAtlas; O97756; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acyltransferase; Biological rhythms; Cytoplasm; Melatonin biosynthesis;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..204
FT /note="Serotonin N-acetyltransferase"
FT /id="PRO_0000074581"
FT DOMAIN 32..193
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT BINDING 121..123
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 129..134
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 165..167
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT SITE 117
FT /note="Important for the catalytic mechanism; involved in
FT substrate deprotonation"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT SITE 119
FT /note="Important for the catalytic mechanism; involved in
FT substrate deprotonation"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT MOD_RES 28
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:12364461"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
SQ SEQUENCE 204 AA; 22891 MW; 40A5A415E554DF79 CRC64;
MSTQSTHPPK PEAPRLPPAI SSCQRRHTLP ASEFRCLTPE DAVSAFEIER EAFISVLGVC
PLYLDEIRHF LTLCPELSLG WFEEGCLVAF IIGSLWDKDR LMQESLTMHR PGGHIAHLHV
LAVHCAFRQQ GRGPILLWRY LHHLGSQPAV HRAALMCEDA LVPFYERFGF HAMGPCAITV
GSLSFTELHC SLQGHPFLRR NSGC
