Q9R0A9 (SNAT_MESAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serotonin N-acetyltransferase
Short name=Serotonin acetylase
EC=2.3.1.87

Alternative name(s):
Aralkylamine N-acetyltransferase
Short name=AA-NAT

Gene names

Name:	AANAT
Synonyms:	SNAT

Organism

Mesocricetus auratus (Golden hamster)

Taxonomic identifier

10036 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.
Catalytic activity	Acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine.
Pathway	Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.
Subunit structure	Monomer By similarity. Interacts with several 14-3-3 proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when phosphorylated at Thr-31 By similarity. Phosphorylation on Ser-205 also allows binding to YWHAZ, but with lower affinity By similarity. The interaction with YWHAZ considerably increases affinity for arylalkylamines and acetyl-CoA and protects the enzyme from dephosphorylation and proteasomal degradation. It may also prevent thiol-dependent inactivation By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Highly expressed in pineal gland and retina. Also detected in heart and intestine. Ref.1
Induction	Exhibits night/day variations with an increased expression at night in the pineal gland. Ref.1
Post-translational modification	cAMP-dependent phosphorylation on both N-terminal Thr-31 and C-terminal Ser-205 regulates AANAT activity by promoting interaction with 14-3-3 proteins By similarity.
Sequence similarities	Belongs to the acetyltransferase family. AANAT subfamily. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Biological process	Biological rhythms Melatonin biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	melatonin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW rhythmic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aralkylamine N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 207	207	Serotonin N-acetyltransferase		PRO_0000074582
Regions
	Domain	35 – 194	160	N-acetyltransferase
	Region	124 – 126	3	Acetyl-CoA binding By similarity
	Region	132 – 137	6	Acetyl-CoA binding By similarity
	Region	168 – 170	3	Acetyl-CoA binding By similarity
Sites
	Binding site	124	1	Substrate; via carbonyl oxygen By similarity
	Site	120	1	Important for the catalytic mechanism; involved in substrate deprotonation By similarity
	Site	122	1	Important for the catalytic mechanism; involved in substrate deprotonation By similarity
Amino acid modifications
	Modified residue	31	1	Phosphothreonine; by PKA By similarity
	Modified residue	205	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9R0A9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C179FC32F08C0734	FASTA	207	23,385
	10 20 30 40 50 60 MPMLSPHSLK PDTLHLPPGT SEFLGCQRRH TLPASEFRCL TPQDAISVFE IEREAFISVS 70 80 90 100 110 120 GTCPLYLDEI RHFLTLCPEL SLGWFEEGRL VAFIIGSLWD KERLTQESLT LHRPGGRTAH 130 140 150 160 170 180 LHVLAVHRTF RQQGKGSVLL WRYLHHLGSQ PAVRRAVLMC EDALVPFYEK FGFQAVGPCA 190 200 VTVGSLTFME LQCSLRCHAF LRRNSGC

References

[1]	"Molecular cloning of the arylalkylamine-N-acetyltransferase and daily variations of its mRNA expression in the syrian hamster pineal gland." Gauer F., Poirel V.J., Garidou M.L., Simonneaux V., Pevet P. Brain Res. Mol. Brain Res. 71:87-95(1999) [PubMed: 10407190] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Tissue: Pineal gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF092100 mRNA. Translation: AAD55970.1.
3D structure databases
ProteinModelPortal	Q9R0A9.
SMR	Q9R0A9. Positions 25-196.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG016332.
Family and domain databases
InterPro	IPR000182. AcTrfase_GCN5-related_dom. IPR016181. Acyl_CoA_acyltransferase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SNAT_MESAU

Accession

Primary (citable) accession number: Q9R0A9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program