O02785 · SNAT_BOVIN
- ProteinSerotonin N-acetyltransferase
- GeneAANAT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids207 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
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
- a 2-arylethylamine + acetyl-CoA = an N-acetyl-2-arylethylamine + CoA + H+
Pathway
Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 120 | Important for the catalytic mechanism; involved in substrate deprotonation | ||||
Sequence: H | ||||||
Site | 122 | Important for the catalytic mechanism; involved in substrate deprotonation | ||||
Sequence: H | ||||||
Binding site | 124 | substrate | ||||
Sequence: L | ||||||
Binding site | 124-126 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: LAV | ||||||
Binding site | 132-137 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: QQGKGS | ||||||
Binding site | 159 | substrate | ||||
Sequence: M | ||||||
Binding site | 168-170 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: YQR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | aralkylamine N-acetyltransferase activity | |
Biological Process | circadian rhythm | |
Biological Process | melatonin biosynthetic process | |
Biological Process | response to light stimulus |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerotonin N-acetyltransferase
- EC number
- Short namesSerotonin acetylase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionO02785
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000074579 | 1-207 | Serotonin N-acetyltransferase | |||
Sequence: MSTPSIHCLKPSPLHLPSGIPGSPGRQRRHTLPANEFRCLTPKDAAGVFEIEREAFISVSGNCPLNLDEVRHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESLTLHRPGGRTAHLHALAVHHSFRQQGKGSVLLWRYLQHAGGQPAVRRAVLMCEDALVPFYQRFGFHPAGPCAVVVGSLTFTEMHCSLRGHAALRRNSDR | ||||||
Modified residue | 31 | Phosphothreonine; by PKA | ||||
Sequence: T | ||||||
Modified residue | 205 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
cAMP-dependent phosphorylation on both N-terminal Thr-31 and C-terminal Ser-205 regulates AANAT activity by promoting interaction with 14-3-3 proteins.
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
High levels in pineal gland and retina.
Induction
Exhibits night/day variations with an increased expression at night. Higher levels in pineal gland in early morning than in early afternoon (at protein level).
Interaction
Subunit
Monomer (By similarity).
Interacts with several 14-3-3 proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when phosphorylated at Thr-31 (By similarity).
Phosphorylation on Ser-205 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).
Interacts with several 14-3-3 proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when phosphorylated at Thr-31 (By similarity).
Phosphorylation on Ser-205 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).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-196 | N-acetyltransferase | ||||
Sequence: NEFRCLTPKDAAGVFEIEREAFISVSGNCPLNLDEVRHFLTLCPELSLGWFVEGRLVAFIIGSLWDEERLTQESLTLHRPGGRTAHLHALAVHHSFRQQGKGSVLLWRYLQHAGGQPAVRRAVLMCEDALVPFYQRFGFHPAGPCAVVVGSLTFTEMHCSLR |
Sequence similarities
Belongs to the acetyltransferase family. AANAT subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length207
- Mass (Da)22,997
- Last updated1997-07-01 v1
- Checksum734990F5CED18695
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AD000742 EMBL· GenBank· DDBJ | AAB58942.1 EMBL· GenBank· DDBJ | mRNA |