Reviewed, UniProtKB/Swiss-Prot Q16613 (SNAT_HUMAN)

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

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

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

General annotation (Comments)

Function	Catalyzes the N-acetylation of serotonin into N-acetylserotonin. Controls the night/day rhythm of melatonin production in the pineal gland. Has a relative affinity for hydroxylated versus non-hydroxylated arylalkylamines.
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 YWHAZ; the interaction requires phosphorylation on Thr-31, and modulates the enzymatic activity of AANAT through preventing dephosphorylation and/or proteolysis and stabilizing substrate binding. Subsequently, a second molecule of AANAT can bind, via the phosphorylated Ser-205 site, the other YWHAZ monomer with similar effect By similarity.
Subcellular location	Cytoplasm Ref.3.
Tissue specificity	Highly expressed in pineal gland. Lower levels in the retina and in the Y79 retinoblastoma cell line. Weak expression in several brain regions and in the pituitary gland. Ref.1 Ref.4
Post-translational modification	Phosphorylated; cAMP-dependent phosphorylation on both N-terminal and C-terminal sites regulates AANAT activity through allowing interaction with 14-3-3 proteins and protecting the enzyme against proteasomal degradation By similarity.
Polymorphism	The variant Thr-129 shows significantly higher frequency in delayed sleep phase syndrome (DSPS). Expressed in the gastrointestinal tract (GIT), including oral cavity, esophagus, stomach and duodenum. Expressed in the entero-endocrine (EE) cells of the GIT wall.
Sequence similarities	Belongs to the acetyltransferase family. AANAT subfamily. Contains 1 N-acetyltransferase domain.
Biophysicochemical properties	Kinetic parameters: KM=0.13 mM for tryptamine KM=2.6 mM for 5-hydroxytryptamine KM=0.55 mM for phenylethylamine KM=10.6 mM for tyramine

Ontologies

Keywords
Biological process	Biological rhythms Melatonin biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	circadian rhythm Ref.1 Traceable author statement. Source: ProtInc melatonin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.1 Inferred from Experiment. Source: Reactome
Molecular function	aralkylamine N-acetyltransferase activity Ref.1 Inferred from Experiment. Source: Reactome
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_0000074580
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
Natural variations
	Natural variant	15	1	R → C: dbSNP rs34470791.		VAR_048168
	Natural variant	129	1	A → T in DSPS. dbSNP rs28936679. Ref.5		VAR_055086

Sequences

	Sequence		Length	Mass (Da)
	Q16613-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 7476612F3661E0D5	FASTA	207	23,344
	10 20 30 40 50 60 MSTQSTHPLK PEAPRLPPGI PESPSCQRRH TLPASEFRCL TPEDAVSAFE IEREAFISVL 70 80 90 100 110 120 GVCPLYLDEI RHFLTLCPEL SLGWFEEGCL VAFIIGSLWD KERLMQESLT LHRSGGHIAH 130 140 150 160 170 180 LHVLAVHRAF RQQGRGPILL WRYLHHLGSQ PAVRRAALMC EDALVPFYER FSFHAVGPCA 190 200 ITVGSLTFME LHCSLRGHPF LRRNSGC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human serotonin N-acetyltransferase (EC 2.3.1.87) gene (AANAT): structure, chromosomal localization, and tissue expression." Coon S.L., Mazuruk K., Bernard M., Roseboom P., Klein D.C., Rodriguez I.R. Genomics 34:76-84(1996) [PubMed: 8661026] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INDUCTION, TISSUE SPECIFICITY.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Testis.
[3]	"cAmp regulation of arylalkylamine N-acetyltransferase (AANAT, EC 2.3.1.87): a new cell line (1E7) provides evidence of intracellular AANAT activation." Coon S.L., Weller J.L., Korf H.-W., Namboodiri M.A., Rollag M., Klein D.C. J. Biol. Chem. 276:24097-24107(2001) [PubMed: 11313340] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Role of melatonin in upper gastrointestinal tract." Konturek S.J., Konturek P.C., Brzozowski T., Bubenik G.A. J. Physiol. Pharmacol. 58:23-52(2007) [PubMed: 18212399] [Abstract] Cited for: TISSUE SPECIFICITY.
[5]	"Significant association of the arylalkylamine N-acetyltransferase (AA-NAT) gene with delayed sleep phase syndrome." Hohjoh H., Takasu M., Shishikura K., Takahashi Y., Honda Y., Tokunaga K. Neurogenetics 4:151-153(2003) [PubMed: 12736803] [Abstract] Cited for: VARIANT DSPS THR-129.
+	Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases
EMBL GenBank DDBJ	U40391 Genomic DNA. Translation: AAC50555.1. U40347 mRNA. Translation: AAC50554.1. BC069434 mRNA. Translation: AAH69434.1. BC092430 mRNA. Translation: AAH92430.1. BC126332 mRNA. Translation: AAI26333.1. BC126334 mRNA. Translation: AAI26335.1.
IPI	IPI00003354.
RefSeq	NP_001079.1. NP_001160051.1.
UniGene	Hs.431417
3D structure databases
SMR	Q16613. Positions 19-196.
ModBase	Search...
Protein-protein interaction databases
STRING	Q16613.
PTM databases
PhosphoSite	Q16613.
Proteomic databases
PRIDE	Q16613.
Genome annotation databases
Ensembl	ENST00000250615; ENSP00000250615; ENSG00000129673; Homo sapiens. [Genome view] ENST00000392492; ENSP00000376282; ENSG00000129673; Homo sapiens. [Genome view]
GeneID	15.
KEGG	hsa:15.
UCSC	uc002jro.1. human.
Organism-specific databases
CTD	15.
GeneCards	GC17P071975.
HGNC	HGNC:19. AANAT.
MIM	600950. gene+phenotype.
PharmGKB	PA24366.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15095.
HOGENOM	HBG715289.
HOVERGEN	Q16613.
InParanoid	Q16613.
OMA	VPFYERF.
OrthoDB	EOG9GF60Z.
PhylomeDB	Q16613.
Enzyme and pathway databases
BRENDA	2.3.1.87. 247.
Reactome	REACT_15314. Hormone biosynthesis.
Gene expression databases
ArrayExpress	Q16613.
Bgee	Q16613.
CleanEx	HS_AANAT.
Genevestigator	Q16613.
GermOnline	ENSG00000129673. Homo sapiens.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GCN5-rel_AcTrfase. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	35.
PMAP-CutDB	Q16613.
SOURCE	Search...

Entry information

Entry name

SNAT_HUMAN

Accession

Primary (citable) accession number: Q16613
Secondary accession number(s): A0AVF2, Q562F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.