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Reviewed, UniProtKB/Swiss-Prot O88816 (SNAT_MOUSE)

Last modified November 3, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

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

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
O88816-1 [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: 9708862] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 9838107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: 129/Sv and C3H/He.
Tissue: Pineal gland.
[3]Roseboom P.H., Namboodiri M.A.A., Zimonjic D.B., Popescu N.C., Rodriguez I.R., Klein D.C.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 129/Sv.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB013358 mRNA. Translation: BAA31526.1.
AF004108 mRNA. Translation: AAD09408.1.
U83462 Genomic DNA. Translation: AAD08637.1.
IPIIPI00135086.
RefSeqNP_033721.1.
UniGeneMm.418559
Mm.42233

3D structure databases

HSSPHSSP built from PDB template 1CJW based on UniProtKB Q29495.
SMRO88816. Positions 23-194.
ModBaseSearch...

Protein-protein interaction databases

STRINGO88816.

PTM databases

PhosphoSiteO88816.

Proteomic databases

PRIDEO88816.

Genome annotation databases

EnsemblENSMUST00000021160; ENSMUSP00000021160; ENSMUSG00000020804; Mus musculus. [Genome view]
GeneID11298.
KEGGmmu:11298.
UCSCuc007mlo.1. mouse.

Organism-specific databases

CTD11298.
MGIMGI:1328365. Aanat.

Phylogenomic databases

HOGENOMO88816.
HOVERGENO88816.
OMALRRNSGC.

Enzyme and pathway databases

BRENDA2.3.1.87. 244.

Gene expression databases

ArrayExpressO88816.
BgeeO88816.
CleanExMM_AANAT.
GenevestigatorO88816.
GermOnlineENSMUSG00000020804. Mus musculus.

Family and domain databases

InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GCN5-rel_AcTrfase.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio278578.
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: November 3, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

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) · Sequences · References · Cross-references · Entry information · Relevant documents