Reviewed, UniProtKB/Swiss-Prot P79774 (SNAT_CHICK)

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

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	205 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-29, 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-203 site, the other ywhaz monomer with similar effect By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in follicular pineal cells and retinal photoreceptors with five times more expression in the pineal gland. Ref.1
Induction	Exhibits circadian rhythm pattern in the pineal gland with highest levels at ZT 24. Expression in the retina is less defined with a slight increase at ZT 24. Ref.1
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 – 205	205	Serotonin N-acetyltransferase		PRO_0000074587
Regions
	Domain	33 – 194	162	N-acetyltransferase
	Region	122 – 124	3	Acetyl-CoA binding By similarity
	Region	130 – 135	6	Acetyl-CoA binding By similarity
	Region	166 – 168	3	Acetyl-CoA binding By similarity
Sites
	Binding site	122	1	Substrate; via carbonyl oxygen By similarity
	Site	118	1	Important for the catalytic mechanism; involved in substrate deprotonation By similarity
	Site	120	1	Important for the catalytic mechanism; involved in substrate deprotonation By similarity
Amino acid modifications
	Modified residue	29	1	Phosphothreonine; by PKA By similarity
	Modified residue	203	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P79774-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 40871147793A4D80	FASTA	205	23,187
	10 20 30 40 50 60 MPVLGAVPFL KPTPLQGPRN SPGRQRRHTL PASEFRCLSP EDAVSVFEIE REAFISVSGD 70 80 90 100 110 120 CPLHLDEIRH FLTLCPELSL GWFEEGRLVA FIIGSLWDQD RLSQAALTLH NPRGTAVHIH 130 140 150 160 170 180 VLAVHRTFRQ QGKGSILMWR YLQYLRCLPC ARRAVLMCED FLVPFYEKCG FVAVGPCQVT 190 200 VGTLAFTEMQ HEVRGHAFMR RNSGC

References

[1]

"Avian melatonin synthesis: photic and circadian regulation of serotonin N-acetyltransferase mRNA in the chicken pineal gland and retina." Bernard M., Iuvone P.M., Cassone V.M., Roseboom P.H., Coon S.L., Klein D.C. J. Neurochem. 68:213-224(1997) [PubMed: 8978728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Tissue: Pineal gland.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U46502 mRNA. Translation: AAB40942.1.
IPI	IPI00584277.
RefSeq	NP_990489.1.
UniGene	Gga.634
3D structure databases
HSSP	HSSP built from PDB template 1B6B based on UniProtKB Q29495.
SMR	P79774. Positions 17-194.
ModBase	Search...
Protein-protein interaction databases
STRING	P79774.
Genome annotation databases
Ensembl	ENSGALT00000003024; ENSGALP00000003020; ENSGALG00000001955; Gallus gallus. [Genome view]
GeneID	396066.
KEGG	gga:396066.
Organism-specific databases
CTD	396066.
Phylogenomic databases
HOVERGEN	P79774.
OMA	LRRNSGC.
Enzyme and pathway databases
BRENDA	2.3.1.87. 4.
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_CHICK

Accession

Primary (citable) accession number: P79774

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1997
Last modified:	November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)