SNAT_BOVIN
ID SNAT_BOVIN Reviewed; 207 AA.
AC O02785;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
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:10036306};
DE AltName: Full=Aralkylamine N-acetyltransferase;
DE Short=AA-NAT;
GN Name=AANAT; Synonyms=SNAT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Pineal gland;
RX PubMed=10036306; DOI=10.1016/s0169-328x(98)00336-2;
RA Craft C.M., Murage J., Brown B., Zhan-Poe X.;
RT "Bovine arylalkylamine N-acetyltransferase activity correlated with mRNA
RT expression in pineal and retina.";
RL Brain Res. Mol. Brain Res. 65:44-51(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:0000269|PubMed:10036306}.
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:10036306};
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: High levels in pineal gland and retina.
CC {ECO:0000269|PubMed:10036306}.
CC -!- INDUCTION: Exhibits night/day variations with an increased expression
CC at night. Higher levels in pineal gland in early morning than in early
CC afternoon (at protein level). {ECO:0000269|PubMed:10036306}.
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; AD000742; AAB58942.1; -; mRNA.
DR RefSeq; NP_803475.1; NM_177509.2.
DR AlphaFoldDB; O02785; -.
DR SMR; O02785; -.
DR STRING; 9913.ENSBTAP00000019543; -.
DR PaxDb; O02785; -.
DR GeneID; 281583; -.
DR KEGG; bta:281583; -.
DR CTD; 15; -.
DR eggNOG; KOG4144; Eukaryota.
DR InParanoid; O02785; -.
DR OrthoDB; 1528352at2759; -.
DR UniPathway; UPA00837; UER00815.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030187; P:melatonin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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..207
FT /note="Serotonin N-acetyltransferase"
FT /id="PRO_0000074579"
FT DOMAIN 35..196
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; 22997 MW; 734990F5CED18695 CRC64;
MSTPSIHCLK PSPLHLPSGI PGSPGRQRRH TLPANEFRCL TPKDAAGVFE IEREAFISVS
GNCPLNLDEV RHFLTLCPEL SLGWFVEGRL VAFIIGSLWD EERLTQESLT LHRPGGRTAH
LHALAVHHSF RQQGKGSVLL WRYLQHAGGQ PAVRRAVLMC EDALVPFYQR FGFHPAGPCA
VVVGSLTFTE MHCSLRGHAA LRRNSDR
