SNAT_PANTR
ID SNAT_PANTR Reviewed; 207 AA.
AC Q5IS55;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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 (By
CC similarity). {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 -!- 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; AY665273; AAV74311.2; -; mRNA.
DR RefSeq; NP_001012442.1; NM_001012440.1.
DR RefSeq; XP_016786107.1; XM_016930618.1.
DR RefSeq; XP_016786108.1; XM_016930619.1.
DR AlphaFoldDB; Q5IS55; -.
DR SMR; Q5IS55; -.
DR STRING; 9598.ENSPTRP00000016459; -.
DR PaxDb; Q5IS55; -.
DR Ensembl; ENSPTRT00000017765; ENSPTRP00000016459; ENSPTRG00000009682.
DR GeneID; 503504; -.
DR KEGG; ptr:503504; -.
DR CTD; 15; -.
DR VGNC; VGNC:6317; AANAT.
DR eggNOG; KOG4144; Eukaryota.
DR GeneTree; ENSGT00390000015579; -.
DR HOGENOM; CLU_061829_3_1_1; -.
DR InParanoid; Q5IS55; -.
DR OMA; HKPGGHI; -.
DR OrthoDB; 1528352at2759; -.
DR TreeFam; TF331622; -.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000002277; Chromosome 17.
DR Bgee; ENSPTRG00000009682; Expressed in testis and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0004060; F:arylamine N-acetyltransferase activity; IEA:Ensembl.
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 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_0000074584"
FT DOMAIN 35..202
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 23338 MW; 4F82F0968A20B45B CRC64;
MSMQSTHPPK PEAPRLPPGI PESPSCQRRH TLPASEFRCL TPEDAVSAFE IEREAFISVL
GVCPLDLDEI RHFLTLCPEL SLGWFEEGCL VAFIIGSLWD KERLMQESLT LHRSGGHIAH
LHVLAVHRAF RQQGRGPILL WRYLHHLGSQ PAVRRAALMC EDALVPFYER FSFHAVGPCA
ITVGSLTFTE LHCSLRDHPF LRRNSGC
