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O88816 (SNAT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.

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 several 14-3-3 proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when phosphorylated at Thr-29 By similarity. Phosphorylation on Ser-203 also allows binding to YWHAZ, but with lower affinity By similarity. The interaction with YWHAZ considerably increases affinity for arylalkylamines and acetyl-CoA and protects the enzyme from dephosphorylation and proteasomal degradation. It may also prevent thiol-dependent inactivation By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in pineal gland at night. Expression in the retina has not been confirmed. Extrapineal expression could be strain-specific. Ref.2

Induction

Exhibits night/day variations with a drastically increased expression at night in the pineal gland. Ref.1 Ref.2 Ref.3

Post-translational modification

cAMP-dependent phosphorylation on both N-terminal Thr-29 and C-terminal Ser-203 regulates AANAT activity by promoting interaction with 14-3-3 proteins By similarity.

Miscellaneous

Pineal melatonin synthesis is severely compromised in most inbred strains of mice. In C57BL/6, a polymorphism activates a cryptic splice site causing the production of an alternative form containing a premature stop codon. The predicted resulting protein would lack the putative catalytic and acetyl-CoA binding domains and therefore would be inactive.

Sequence similarities

Belongs to the acetyltransferase family. AANAT subfamily.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processBiological rhythms
Melatonin biosynthesis
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal protein amino acid acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

melatonin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from electronic annotation. Source: Ensembl

response to corticosterone

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to light stimulus

Inferred from electronic annotation. Source: Ensembl

response to prostaglandin E

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentperinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionaralkylamine N-acetyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

arylamine N-acetyltransferase activity

Inferred from direct assay PubMed 7545952. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Serotonin N-acetyltransferase
PRO_0000074583

Regions

Domain33 – 194162N-acetyltransferase
Region122 – 1243Acetyl-CoA binding By similarity
Region130 – 1356Acetyl-CoA binding By similarity
Region166 – 1683Acetyl-CoA binding By similarity

Sites

Binding site1221Substrate; via carbonyl oxygen By similarity
Site1181Important for the catalytic mechanism; involved in substrate deprotonation By similarity
Site1201Important for the catalytic mechanism; involved in substrate deprotonation By similarity

Amino acid modifications

Modified residue291Phosphothreonine; by PKA By similarity
Modified residue2031Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
O88816 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D2ECD070998CB643

FASTA20523,069
        10         20         30         40         50         60 
MLNINSLKPE ALHLPLGTSE FLGCQRRHTL PASEFRCLTP EDATSAFEIE REAFISVSGT 

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

       130        140        150        160        170        180 
VLAVHRTFRQ QGKGSVLLWR YLHHLGSQPA VRRAVLMCED ALVPFYEKFG FQAVGPCAIT 

       190        200 
VGSLTFTELQ CSLRCHAFLR RNSGC 

« Hide

References

[1]"Molecular cloning of serotonin N-acetyltransferase gene from the mouse and its daily expression in the retina."
Sakamoto K., Ishida N.
Neurosci. Lett. 250:181-184(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: BALB/c.
Tissue: Retina.
[2]"Natural melatonin 'knockdown' in C57BL/6J mice: rare mechanism truncates serotonin N-acetyltransferase."
Roseboom P.H., Namboodiri M.A.A., Zimonjic D.B., Popescu N.C., Rodriguez I.R., Gastel J.A., Klein D.C.
Brain Res. Mol. Brain Res. 63:189-197(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION, IDENTIFICATION OF A TRUNCATED FORM IN C57BL/6.
Strain: 129/Sv and C3H/He.
Tissue: Pineal gland.
[3]"Genetic variation of melatonin productivity in laboratory mice under domestication."
Kasahara T., Abe K., Mekada K., Yoshiki A., Kato T.
Proc. Natl. Acad. Sci. U.S.A. 107:6412-6417(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
Strain: C3H/He and C57BL/6J.
Tissue: Pineal gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB013358 mRNA. Translation: BAA31526.1.
AF004108 mRNA. Translation: AAD09408.1.
U83462 Genomic DNA. Translation: AAD08637.1.
CCDSCCDS25671.1.
RefSeqNP_033721.1. NM_009591.3.
UniGeneMm.418559.
Mm.42233.

3D structure databases

ProteinModelPortalO88816.
SMRO88816. Positions 28-193.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteO88816.

Proteomic databases

PRIDEO88816.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000153476; ENSMUSP00000122895; ENSMUSG00000020804.
GeneID11298.
KEGGmmu:11298.
UCSCuc007mlo.2. mouse.

Organism-specific databases

CTD15.
MGIMGI:1328365. Aanat.

Phylogenomic databases

eggNOGCOG0454.
HOVERGENHBG016332.
InParanoidO88816.
KOK00669.
OMALRRNSGC.
PhylomeDBO88816.
TreeFamTF331622.

Enzyme and pathway databases

UniPathwayUPA00837; UER00815.

Gene expression databases

ArrayExpressO88816.
BgeeO88816.
CleanExMM_AANAT.
GenevestigatorO88816.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio278578.
PROO88816.
SOURCESearch...

Entry information

Entry nameSNAT_MOUSE
AccessionPrimary (citable) accession number: O88816
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot