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O88816

- SNAT_MOUSE

UniProt

O88816 - SNAT_MOUSE

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Protein

Serotonin N-acetyltransferase

Gene

Aanat

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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 activityi

Acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei118 – 1181Important for the catalytic mechanism; involved in substrate deprotonationBy similarity
Sitei120 – 1201Important for the catalytic mechanism; involved in substrate deprotonationBy similarity
Binding sitei122 – 1221Substrate; via carbonyl oxygenBy similarity

GO - Molecular functioni

  1. aralkylamine N-acetyltransferase activity Source: UniProtKB
  2. arylamine N-acetyltransferase activity Source: MGI

GO - Biological processi

  1. cellular response to cAMP Source: UniProtKB
  2. circadian rhythm Source: UniProtKB
  3. melatonin biosynthetic process Source: UniProtKB
  4. N-terminal protein amino acid acetylation Source: UniProtKB
  5. response to calcium ion Source: Ensembl
  6. response to copper ion Source: Ensembl
  7. response to corticosterone Source: Ensembl
  8. response to cytokine Source: Ensembl
  9. response to insulin Source: Ensembl
  10. response to light stimulus Source: Ensembl
  11. response to prostaglandin E Source: Ensembl
  12. response to zinc ion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Biological rhythms, Melatonin biosynthesis

Enzyme and pathway databases

ReactomeiREACT_218437. Serotonin and melatonin biosynthesis.
UniPathwayiUPA00837; UER00815.

Names & Taxonomyi

Protein namesi
Recommended name:
Serotonin N-acetyltransferase (EC:2.3.1.87)
Short name:
Serotonin acetylase
Alternative name(s):
Aralkylamine N-acetyltransferase
Short name:
AA-NAT
Gene namesi
Name:Aanat
Synonyms:Snat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1328365. Aanat.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205Serotonin N-acetyltransferasePRO_0000074583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphothreonine; by PKABy similarity
Modified residuei203 – 2031PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO88816.

PTM databases

PhosphoSiteiO88816.

Expressioni

Tissue specificityi

Highly expressed in pineal gland at night. Expression in the retina has not been confirmed. Extrapineal expression could be strain-specific.1 Publication

Inductioni

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

Gene expression databases

BgeeiO88816.
CleanExiMM_AANAT.
ExpressionAtlasiO88816. baseline and differential.
GenevestigatoriO88816.

Interactioni

Subunit structurei

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliO88816.
SMRiO88816. Positions 28-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 194162N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni122 – 1243Acetyl-CoA bindingBy similarity
Regioni130 – 1356Acetyl-CoA bindingBy similarity
Regioni166 – 1683Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0454.
HOVERGENiHBG016332.
InParanoidiO88816.
KOiK00669.
OMAiLRRNSGC.
PhylomeDBiO88816.
TreeFamiTF331622.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88816-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLNINSLKPE ALHLPLGTSE FLGCQRRHTL PASEFRCLTP EDATSAFEIE
60 70 80 90 100
REAFISVSGT CPLYLDEIRH FLTLCPELSL GWFEEGCLVA FIIGSLWDKE
110 120 130 140 150
RLTQESLTLH RPGGRTAHLH VLAVHRTFRQ QGKGSVLLWR YLHHLGSQPA
160 170 180 190 200
VRRAVLMCED ALVPFYEKFG FQAVGPCAIT VGSLTFTELQ CSLRCHAFLR

RNSGC
Length:205
Mass (Da):23,069
Last modified:November 1, 1998 - v1
Checksum:iD2ECD070998CB643
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013358 mRNA. Translation: BAA31526.1.
AF004108 mRNA. Translation: AAD09408.1.
U83462 Genomic DNA. Translation: AAD08637.1.
CCDSiCCDS25671.1.
RefSeqiNP_033721.1. NM_009591.3.
UniGeneiMm.418559.
Mm.42233.

Genome annotation databases

EnsembliENSMUST00000153476; ENSMUSP00000122895; ENSMUSG00000020804.
GeneIDi11298.
KEGGimmu:11298.
UCSCiuc007mlo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013358 mRNA. Translation: BAA31526.1 .
AF004108 mRNA. Translation: AAD09408.1 .
U83462 Genomic DNA. Translation: AAD08637.1 .
CCDSi CCDS25671.1.
RefSeqi NP_033721.1. NM_009591.3.
UniGenei Mm.418559.
Mm.42233.

3D structure databases

ProteinModelPortali O88816.
SMRi O88816. Positions 28-193.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei O88816.

Proteomic databases

PRIDEi O88816.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000153476 ; ENSMUSP00000122895 ; ENSMUSG00000020804 .
GeneIDi 11298.
KEGGi mmu:11298.
UCSCi uc007mlo.2. mouse.

Organism-specific databases

CTDi 15.
MGIi MGI:1328365. Aanat.

Phylogenomic databases

eggNOGi COG0454.
HOVERGENi HBG016332.
InParanoidi O88816.
KOi K00669.
OMAi LRRNSGC.
PhylomeDBi O88816.
TreeFami TF331622.

Enzyme and pathway databases

UniPathwayi UPA00837 ; UER00815 .
Reactomei REACT_218437. Serotonin and melatonin biosynthesis.

Miscellaneous databases

NextBioi 278578.
PROi O88816.
SOURCEi Search...

Gene expression databases

Bgeei O88816.
CleanExi MM_AANAT.
ExpressionAtlasi O88816. baseline and differential.
Genevestigatori O88816.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view ]
Pfami PF00583. Acetyltransf_1. 1 hit.
[Graphical view ]
SUPFAMi SSF55729. SSF55729. 1 hit.
PROSITEi PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiSNAT_MOUSE
AccessioniPrimary (citable) accession number: O88816
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3