Reviewed, UniProtKB/Swiss-Prot Q9R0A9 (SNAT_MESAU)

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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Catalyzes the N-acetylation of serotonin into N-acetylserotonin.
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 By similarity.
Tissue specificity	Highly expressed in pineal gland and retina.
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.
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)
	Q9R0A9-1 [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: Pineal gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF092100 mRNA. Translation: AAD55970.1.
3D structure databases
HSSP	HSSP built from PDB template 1CJW based on UniProtKB Q29495.
SMR	Q9R0A9. Positions 25-196.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q9R0A9.
Enzyme and pathway databases
BRENDA	2.3.1.87. 824.
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...

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:	October 13, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)