SNAT_CHICK
ID SNAT_CHICK Reviewed; 205 AA.
AC P79774;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Pineal gland;
RX PubMed=8978728; DOI=10.1046/j.1471-4159.1997.68010213.x;
RA Bernard M., Iuvone P.M., Cassone V.M., Roseboom P.H., Coon S.L.,
RA Klein D.C.;
RT "Avian melatonin synthesis: photic and circadian regulation of serotonin N-
RT acetyltransferase mRNA in the chicken pineal gland and retina.";
RL J. Neurochem. 68:213-224(1997).
RN [2]
RP INDUCTION.
RX PubMed=20345751; DOI=10.1111/j.1471-4159.2010.06698.x;
RA Haque R., Ali F.G., Biscoglia R., Abey J., Weller J., Klein D.,
RA Iuvone P.M.;
RT "CLOCK and NPAS2 have overlapping roles in the circadian oscillation of
RT arylalkylamine N-acetyltransferase mRNA in chicken cone photoreceptors.";
RL J. Neurochem. 113:1296-1306(2010).
CC -!- FUNCTION: Catalyzes the N-acetylation of serotonin into N-
CC acetylserotonin. {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 YWHAZ; the interaction
CC requires phosphorylation on Thr-29, and modulates the enzymatic
CC activity of AANAT through preventing dephosphorylation and/or
CC proteolysis and stabilizing substrate binding. Subsequently, a second
CC molecule of AANAT can bind, via the phosphorylated Ser-203 site, the
CC other ywhaz monomer with similar effect (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16613}.
CC -!- TISSUE SPECIFICITY: Expressed in follicular pineal cells and retinal
CC photoreceptors with five times more expression in the pineal gland.
CC {ECO:0000269|PubMed:8978728}.
CC -!- INDUCTION: Exhibits circadian rhythm pattern in the pineal gland with
CC highest levels at ZT 24. Expression in the retinal photoreceptor cells
CC oscillates in a circadian manner. {ECO:0000269|PubMed:20345751,
CC ECO:0000269|PubMed:8978728}.
CC -!- PTM: Phosphorylated; cAMP-dependent phosphorylation on both N-terminal
CC and C-terminal sites regulates AANAT activity through allowing
CC interaction with 14-3-3 proteins and protecting the enzyme against
CC proteasomal degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily.
CC {ECO:0000305}.
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DR EMBL; U46502; AAB40942.1; -; mRNA.
DR RefSeq; NP_990489.1; NM_205158.1.
DR RefSeq; XP_015150605.1; XM_015295119.1.
DR AlphaFoldDB; P79774; -.
DR SMR; P79774; -.
DR STRING; 9031.ENSGALP00000003020; -.
DR PaxDb; P79774; -.
DR Ensembl; ENSGALT00000003024; ENSGALP00000003020; ENSGALG00000001955.
DR GeneID; 396066; -.
DR KEGG; gga:396066; -.
DR CTD; 15; -.
DR VEuPathDB; HostDB:geneid_396066; -.
DR eggNOG; KOG4144; Eukaryota.
DR GeneTree; ENSGT00390000015579; -.
DR HOGENOM; CLU_061829_3_1_1; -.
DR InParanoid; P79774; -.
DR OMA; HFLNLCP; -.
DR OrthoDB; 1528352at2759; -.
DR PhylomeDB; P79774; -.
DR TreeFam; TF331622; -.
DR BRENDA; 2.3.1.87; 1306.
DR Reactome; R-GGA-209931; Serotonin and melatonin biosynthesis.
DR UniPathway; UPA00837; UER00815.
DR PRO; PR:P79774; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000001955; Expressed in skeletal muscle tissue.
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; IEA:Ensembl.
DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IDA:AgBase.
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:0071492; P:cellular response to UV-A; IDA:AgBase.
DR GO; GO:0007623; P:circadian rhythm; IBA:GO_Central.
DR GO; GO:0030187; P:melatonin biosynthetic process; IBA:GO_Central.
DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IEA:Ensembl.
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..205
FT /note="Serotonin N-acetyltransferase"
FT /id="PRO_0000074587"
FT DOMAIN 33..194
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT REGION 11..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 122..124
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 130..135
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT BINDING 166..168
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q29495"
FT SITE 118
FT /note="Important for the catalytic mechanism; involved in
FT substrate deprotonation"
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 MOD_RES 29
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 205 AA; 23187 MW; 40871147793A4D80 CRC64;
MPVLGAVPFL KPTPLQGPRN SPGRQRRHTL PASEFRCLSP EDAVSVFEIE REAFISVSGD
CPLHLDEIRH FLTLCPELSL GWFEEGRLVA FIIGSLWDQD RLSQAALTLH NPRGTAVHIH
VLAVHRTFRQ QGKGSILMWR YLQYLRCLPC ARRAVLMCED FLVPFYEKCG FVAVGPCQVT
VGTLAFTEMQ HEVRGHAFMR RNSGC
