Serotonin N-acetyltransferase - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot Q64666 (SNAT_RAT)

Last modified November 3, 2009. Version 77. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
Induction	Exhibits night/day variations. 150-fold increase during night time in pineal gland. 10-fold increase in retina. On norepinephrine stimulation, inhibited by the proteosome inhibitors, c-Lact and MG132. Ref.1 Ref.2 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.
Sequence similarities	Belongs to the acetyltransferase family. AANAT subfamily. Contains 1 N-acetyltransferase domain.
Biophysicochemical properties	Kinetic parameters: X. V_max=1.5 nmol/h/mg enzyme in day V_max=175 nmol/h/mg enzyme in night V_max=22.2 nmol/h/mg enzyme in day in presence of bisubstrate inhibitor V_max=0.46 nmol/h/mg enzyme in night in presence of bisubstrate inhibitor

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Ontologies

Keywords
Biological process	Biological rhythms Melatonin biosynthesis
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	circadian rhythm Inferred from expression pattern. Source: RGD entrainment of circadian clock by photoperiod Ref.1 Traceable author statement. Source: RGD melatonin biosynthetic process Traceable author statement. Source: RGD response to cAMP Inferred from expression pattern. Source: RGD response to calcium ion Inferred from expression pattern. Source: RGD response to copper ion Inferred from direct assay. Source: RGD response to corticosterone stimulus Inferred from expression pattern. Source: RGD response to cytokine stimulus Inferred from expression pattern. Source: RGD response to insulin stimulus Inferred from direct assay. Source: RGD response to organic cyclic substance Inferred from direct assay. Source: RGD response to prostaglandin E stimulus Inferred from direct assay. Source: RGD response to zinc ion Inferred from direct assay. Source: RGD
Cellular component	cytoplasm Inferred from direct assay. Source: RGD
Molecular function	aralkylamine N-acetyltransferase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 205

205

Serotonin N-acetyltransferase

PRO_0000074585

Regions

Domain

33 – 194

162

N-acetyltransferase

Region

122 – 124

Acetyl-CoA binding By similarity

Region

130 – 135

Acetyl-CoA binding By similarity

Region

166 – 168

Acetyl-CoA binding By similarity

Sites

Binding site

122

Substrate; via carbonyl oxygen By similarity

Site

120

Important for the catalytic mechanism; involved in substrate deprotonation By similarity

Site

122

Important for the catalytic mechanism; involved in substrate deprotonation By similarity

Amino acid modifications

Modified residue

Phosphothreonine; by PKA By similarity

Modified residue

203

Phosphoserine By similarity

Experimental info

Sequence conflict

S → N in AAC52330. Ref.4

Sequence conflict

153

R → P in AAC52330. Ref.4

Sequence conflict

185

T → A in AAC52330. Ref.4

Sequence conflict

204 – 205

GC → DR in AAC52330. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

Q64666-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 2504E3082A26BF8E
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FASTA

205

23,142

        10         20         30         40         50         60 
MLSIHPLKPE ALHLPLGTSE FLGCQRRHTL PASEFRCLTP EDATSAFEIE REAFISVSGT 

        70         80         90        100        110        120 
CPLHLDEIRH FLTLCPELSL GWFEEGCLVA FIIGSLWDKE RLTQESLTLH RPGGRTAHLH 

       130        140        150        160        170        180 
VLAVHRTFRQ QGKGSVLLWR YLHHLGSQPA VRRAVLMCEN ALVPFYEKFG FQAMGPCAIT 

       190        200 
MGSLTFTELQ CSLRCHTFLR RNSGC

« Hide

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References

[1]	"Melatonin synthesis: analysis of the more than 150-fold nocturnal increase in serotonin N-acetyltransferase messenger ribonucleic acid in the rat pineal gland." Roseboom P.H., Coon S.L., Baler R., McCune S.K., Weller J.L., Klein D.C. Endocrinology 137:3033-3045(1996) [PubMed: 8770929] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: Sprague-Dawley. Tissue: Pineal gland.
[2]	"Diurnal variation in mRNA encoding serotonin N-acetyltransferase in pineal gland." Borjigin J., Wang M.M., Snyder S.H. Nature 378:783-785(1995) [PubMed: 8524412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION. Strain: Sprague-Dawley. Tissue: Pineal gland.
[3]	Kim T.-D., Kim K.-T. Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Pineal gland.
[4]	"Pineal serotonin N-acetyltransferase: expression cloning and molecular analysis." Coon S.L., Roseboom P.H., Baler R., Weller J.L., Namboodiri M.A.A., Koonin E.V., Klein D.C. Science 270:1681-1683(1995) [PubMed: 7502081] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-205, INDUCTION. Strain: Sprague-Dawley. Tissue: Pineal gland.
[5]	"Proteasomal proteolysis in the adrenergic induction of arylalkylamine-N-acetyltransferase in rat pinealocytes." Terriff D.L., Chik C.L., Price D.M., Ho A.K. Endocrinology 146:4795-4803(2005) [PubMed: 16099857] [Abstract] Cited for: PROTEAOSOMAL PROTEOLYSIS.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	U38306 mRNA. Translation: AAB38484.1. U40803 mRNA. Translation: AAA92711.1. DQ075321 mRNA. Translation: AAY86767.1. U29664 mRNA. Translation: AAC52330.1.
IPI	IPI00214500.
PIR	S68435.
RefSeq	NP_036950.1.
UniGene	Rn.88180
3D structure databases
HSSP	HSSP built from PDB template 1CJW based on UniProtKB Q29495.
SMR	Q64666. Positions 23-194.
ModBase	Search...
Protein-protein interaction databases
STRING	Q64666.
PTM databases
PhosphoSite	Q64666.
Genome annotation databases
Ensembl	ENSRNOT00000015221; ENSRNOP00000015221; ENSRNOG00000011182; Rattus norvegicus. [Genome view]
GeneID	25120.
KEGG	rno:25120.
UCSC	NM_012818. rat.
Organism-specific databases
CTD	25120.
RGD	2006. Aanat.
Phylogenomic databases
HOVERGEN	Q64666.
OMA	LRRNSGC.
Enzyme and pathway databases
BRENDA	2.3.1.87. 248.
Gene expression databases
ArrayExpress	Q64666.
Genevestigator	Q64666.
GermOnline	ENSRNOG00000011182. Rattus norvegicus.
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	605499.

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Entry information

Entry name

SNAT_RAT

Accession

Primary (citable) accession number: Q64666
Secondary accession number(s): Q4JL74, Q64553

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents