Reviewed, UniProtKB/Swiss-Prot Q5IS55 (SNAT_PANTR)

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

Pan troglodytes (Chimpanzee)

Taxonomic identifier

9598 [NCBI]

Taxonomic lineage

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

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 By similarity.
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.
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_0000074584
Regions
	Domain	35 – 202	168	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)
	Q5IS55-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 4F82F0968A20B45B	FASTA	207	23,338
	10 20 30 40 50 60 MSMQSTHPPK PEAPRLPPGI PESPSCQRRH TLPASEFRCL TPEDAVSAFE IEREAFISVL 70 80 90 100 110 120 GVCPLDLDEI RHFLTLCPEL SLGWFEEGCL VAFIIGSLWD KERLMQESLT LHRSGGHIAH 130 140 150 160 170 180 LHVLAVHRAF RQQGRGPILL WRYLHHLGSQ PAVRRAALMC EDALVPFYER FSFHAVGPCA 190 200 ITVGSLTFTE LHCSLRDHPF LRRNSGC

References

[1]	"Accelerated evolution of nervous system genes in the origin of Homo sapiens." Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L., Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T. Cell 119:1027-1040(2004) [PubMed: 15620360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY665273 mRNA. Translation: AAV74311.2.
RefSeq	NP_001012442.1.
3D structure databases
SMR	Q5IS55. Positions 19-196.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5IS55.
Genome annotation databases
Ensembl	ENSPTRT00000017765; ENSPTRP00000016459; ENSPTRG00000009682; Pan troglodytes. [Genome view]
GeneID	503504.
KEGG	ptr:503504.
Organism-specific databases
CTD	503504.
Phylogenomic databases
HOVERGEN	Q5IS55.
OMA	LRRNSGC.
Enzyme and pathway databases
BRENDA	2.3.1.87. 264977.
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_PANTR

Accession

Primary (citable) accession number: Q5IS55

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	February 15, 2005
Last modified:	November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)