UniProtKB - Q29495 (SNAT_SHEEP)
Serotonin N-acetyltransferase
AANAT
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.
1 PublicationCatalytic activityi
- EC:2.3.1.874 Publications
Kineticsi
- KM=0.29 mM for acetyl-CoA2 Publications
- KM=0.17 mM for tryptamine2 Publications
- KM=0.20 mM for tryptamine2 Publications
- KM=0.31 mM for 5-hydroxytryptamine2 Publications
- KM=3.4 mM for phenylethylamine2 Publications
- KM=3.4 mM for tyramine2 Publications
: melatonin biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes melatonin from serotonin.Curated This subpathway is part of the pathway melatonin biosynthesis, which is itself part of Aromatic compound metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes melatonin from serotonin, the pathway melatonin biosynthesis and in Aromatic compound metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 120 | Important for the catalytic mechanism; involved in substrate deprotonation2 Publications | 1 | |
Sitei | 122 | Important for the catalytic mechanism; involved in substrate deprotonation2 Publications | 1 | |
Binding sitei | 124 | Substrate; via amide nitrogen3 Publications | 1 | |
Binding sitei | 159 | Substrate; via carbonyl oxygen3 Publications | 1 |
GO - Molecular functioni
- aralkylamine N-acetyltransferase activity Source: UniProtKB
GO - Biological processi
- cellular response to cAMP Source: UniProtKB
- circadian rhythm Source: UniProtKB
- melatonin biosynthetic process Source: UniProtKB
- N-terminal protein amino acid acetylation Source: UniProtKB
Keywordsi
Molecular function | Acyltransferase, Transferase |
Biological process | Biological rhythms, Melatonin biosynthesis |
Enzyme and pathway databases
BRENDAi | 2.3.1.87, 2668 |
SABIO-RKi | Q29495 |
UniPathwayi | UPA00837;UER00815 |
Names & Taxonomyi
Protein namesi | Recommended name: Serotonin N-acetyltransferase (EC:2.3.1.874 Publications)Short name: Serotonin acetylase Alternative name(s): Aralkylamine N-acetyltransferase Short name: AA-NAT |
Gene namesi | Name:AANAT Synonyms:SNAT |
Organismi | Ovis aries (Sheep) |
Taxonomic identifieri | 9940 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Other locations
- perinuclear region of cytoplasm Source: UniProtKB
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 31 | T → A: Loss of PKA-promoted YWHAZ-binding; when associated with G-205. 1 Publication | 1 | |
Mutagenesisi | 57 | I → A: No effect on enzymatic activity; when associated with A-59. 1 Publication | 1 | |
Mutagenesisi | 59 | V → A: No effect on enzymatic activity; when associated with A-57. 1 Publication | 1 | |
Mutagenesisi | 63 – 65 | Missing : Drastic loss of enzymatic activity. 1 Publication | 3 | |
Mutagenesisi | 64 | P → A, G or W: Drastic loss of enzymatic activity. 1 Publication | 1 | |
Mutagenesisi | 120 | H → A: Reduces catalytic activity 270-fold and decreases affinity for acetyl-coenzyme A; when associated with A-122. 2 Publications | 1 | |
Mutagenesisi | 120 | H → Q: Decreases affinity for acetyl-coenzyme A and for substrate. 2 Publications | 1 | |
Mutagenesisi | 122 | H → A: Reduces catalytic activity 270-fold and decreases affinity for acetyl-coenzyme A; when associated with A-120. 2 Publications | 1 | |
Mutagenesisi | 122 | H → Q: Decreases affinity for acetyl-coenzyme A and for substrate. 2 Publications | 1 | |
Mutagenesisi | 160 | C → A: No effect on catalytic activity. 2 Publications | 1 | |
Mutagenesisi | 160 | C → S: Reduces catalytic activity. 2 Publications | 1 | |
Mutagenesisi | 161 | E → A: No effect. 1 Publication | 1 | |
Mutagenesisi | 168 | Y → F: Reduces catalytic activity 30-fold. 2 Publications | 1 | |
Mutagenesisi | 205 | S → G: Loss of PKA-promoted YWHAZ-binding; when associated with A-31. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL5452 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000074586 | 1 – 207 | Serotonin N-acetyltransferaseAdd BLAST | 207 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 31 | Phosphothreonine; by PKA3 Publications | 1 | |
Modified residuei | 205 | Phosphoserine; by PKA1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinPTM databases
iPTMneti | Q29495 |
Expressioni
Tissue specificityi
Inductioni
Interactioni
Subunit structurei
Monomer.
Interacts with several 14-3-3 proteins, including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when phosphorylated at Thr-31. Phosphorylation on Ser-205 also allows binding to YWHAZ, but with a 10-fold lower affinity. 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. The physiological stoichiometry of the interaction is not clear. In vitro studies show either 1:2 (i.e. 1 AANAT molecule per YWHAZ dimer) (PubMed:11427721) or 2:2 (PubMed:11336675).
6 PublicationsBinary interactionsi
Q29495
With | #Exp. | IntAct |
---|---|---|
YWHAZ [P63104] from Homo sapiens. | 3 | EBI-446413,EBI-347088 |
Protein-protein interaction databases
IntActi | Q29495, 1 interactor |
MINTi | Q29495 |
STRINGi | 9940.ENSOARP00000007675 |
Chemistry databases
BindingDBi | Q29495 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q29495 |
SMRi | Q29495 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q29495 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 35 – 196 | N-acetyltransferasePROSITE-ProRule annotationAdd BLAST | 162 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 29 | DisorderedSequence analysisAdd BLAST | 29 | |
Regioni | 28 – 35 | YWHAZ-binding | 8 | |
Regioni | 124 – 126 | Acetyl-CoA binding3 Publications | 3 | |
Regioni | 132 – 137 | Acetyl-CoA binding3 Publications | 6 | |
Regioni | 168 – 170 | Acetyl-CoA binding3 Publications | 3 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG4144, Eukaryota |
OrthoDBi | 1528352at2759 |
Family and domain databases
IDEALi | IID50013 |
InterProi | View protein in InterPro IPR016181, Acyl_CoA_acyltransferase IPR000182, GNAT_dom |
Pfami | View protein in Pfam PF00583, Acetyltransf_1, 1 hit |
SUPFAMi | SSF55729, SSF55729, 1 hit |
PROSITEi | View protein in PROSITE PS51186, GNAT, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MSTPSVHCLK PSPLHLPSGI PGSPGRQRRH TLPANEFRCL TPEDAAGVFE
60 70 80 90 100
IEREAFISVS GNCPLNLDEV QHFLTLCPEL SLGWFVEGRL VAFIIGSLWD
110 120 130 140 150
EERLTQESLA LHRPRGHSAH LHALAVHRSF RQQGKGSVLL WRYLHHVGAQ
160 170 180 190 200
PAVRRAVLMC EDALVPFYQR FGFHPAGPCA IVVGSLTFTE MHCSLRGHAA
LRRNSDR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U29663 mRNA Translation: AAC48690.1 |
RefSeqi | NP_001009461.1, NM_001009461.1 |
Genome annotation databases
GeneIDi | 443531 |
KEGGi | oas:443531 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U29663 mRNA Translation: AAC48690.1 |
RefSeqi | NP_001009461.1, NM_001009461.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1B6B | X-ray | 2.50 | A/B | 28-201 | [»] | |
1CJW | X-ray | 1.80 | A | 30-195 | [»] | |
1IB1 | X-ray | 2.70 | E/F/G/H | 2-201 | [»] | |
1KUV | X-ray | 2.00 | A | 1-207 | [»] | |
1KUX | X-ray | 1.80 | A | 1-207 | [»] | |
1KUY | X-ray | 2.40 | A | 1-207 | [»] | |
1L0C | X-ray | 2.30 | A | 1-207 | [»] | |
AlphaFoldDBi | Q29495 | |||||
SMRi | Q29495 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | Q29495, 1 interactor |
MINTi | Q29495 |
STRINGi | 9940.ENSOARP00000007675 |
Chemistry databases
BindingDBi | Q29495 |
ChEMBLi | CHEMBL5452 |
PTM databases
iPTMneti | Q29495 |
Genome annotation databases
GeneIDi | 443531 |
KEGGi | oas:443531 |
Organism-specific databases
CTDi | 15 |
Phylogenomic databases
eggNOGi | KOG4144, Eukaryota |
OrthoDBi | 1528352at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00837;UER00815 |
BRENDAi | 2.3.1.87, 2668 |
SABIO-RKi | Q29495 |
Miscellaneous databases
EvolutionaryTracei | Q29495 |
PROi | PR:Q29495 |
Family and domain databases
IDEALi | IID50013 |
InterProi | View protein in InterPro IPR016181, Acyl_CoA_acyltransferase IPR000182, GNAT_dom |
Pfami | View protein in Pfam PF00583, Acetyltransf_1, 1 hit |
SUPFAMi | SSF55729, SSF55729, 1 hit |
PROSITEi | View protein in PROSITE PS51186, GNAT, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SNAT_SHEEP | |
Accessioni | Q29495Primary (citable) accession number: Q29495 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 2000 |
Last sequence update: | November 1, 1996 | |
Last modified: | May 25, 2022 | |
This is version 127 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families