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Protein

Serotonin N-acetyltransferase

Gene

Aanat

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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.By similarity

Catalytic activityi

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

Kineticsi

    1. Vmax=1.5 nmol/h/mg enzyme in day
    2. Vmax=175 nmol/h/mg enzyme in night
    3. Vmax=22.2 nmol/h/mg enzyme in day in presence of bisubstrate inhibitor
    4. Vmax=0.46 nmol/h/mg enzyme in night in presence of bisubstrate inhibitor

    Pathwayi: melatonin biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes melatonin from serotonin.
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Acetylserotonin O-methyltransferase (Asmt), Serotonin N-acetyltransferase (Aanat)
    2. no protein annotated in this organism
    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 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 amide nitrogenBy similarity
    Sitei122 – 1221Important for the catalytic mechanism; involved in substrate deprotonationBy similarity
    Binding sitei157 – 1571Substrate; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    • 14-3-3 protein binding Source: UniProtKB
    • aralkylamine N-acetyltransferase activity Source: RGD
    • arylamine N-acetyltransferase activity Source: Ensembl

    GO - Biological processi

    • cellular response to cAMP Source: UniProtKB
    • circadian rhythm Source: RGD
    • entrainment of circadian clock by photoperiod Source: RGD
    • melatonin biosynthetic process Source: UniProtKB
    • N-terminal protein amino acid acetylation Source: UniProtKB
    • photoperiodism Source: RGD
    • response to calcium ion Source: RGD
    • response to cAMP Source: RGD
    • response to copper ion Source: RGD
    • response to corticosterone Source: RGD
    • response to cytokine Source: RGD
    • response to insulin Source: RGD
    • response to light stimulus Source: RGD
    • response to organic cyclic compound Source: RGD
    • response to prostaglandin E Source: RGD
    • response to zinc ion Source: RGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Biological rhythms, Melatonin biosynthesis

    Enzyme and pathway databases

    BRENDAi2.3.1.87. 5301.
    ReactomeiR-RNO-209931. Serotonin and melatonin biosynthesis.
    UniPathwayiUPA00837; UER00815.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serotonin N-acetyltransferase (EC:2.3.1.87By similarity)
    Short name:
    Serotonin acetylase
    Alternative name(s):
    Aralkylamine N-acetyltransferase
    Short name:
    AA-NAT
    Gene namesi
    Name:Aanat
    Synonyms:Snat
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    Proteomesi
    • UP000002494 Componenti: Chromosome 10

    Organism-specific databases

    RGDi2006. Aanat.

    Subcellular locationi

    • Cytoplasm By similarity

    GO - Cellular componenti

    • cytoplasm Source: RGD
    • perinuclear region of cytoplasm Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21Missing : Impaired light-induced proteasomal degradation. 1 Publication
    Mutagenesisi8 – 81K → R: No effect on light-induced proteasomal degradation; when associated with R-99, R-133 and R-168. 1 Publication
    Mutagenesisi37 – 371C → A: No effect on light-induced proteasomal degradation. 1 Publication
    Mutagenesisi61 – 611C → A: No effect on light-induced proteasomal degradation. 1 Publication
    Mutagenesisi99 – 991K → R: No effect onlight-induced proteasomal degradation; when associated with R-8, R-133 and R-168. 1 Publication
    Mutagenesisi133 – 1331K → R: No effect on light-induced proteasomal degradation; when associated with R-8, R-99 and R-168. 1 Publication
    Mutagenesisi168 – 1681K → R: No effect on proteasomal degradation; when associated with R-8, R-99 and R-133. 1 Publication

    Chemistry

    ChEMBLiCHEMBL1075242.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205Serotonin N-acetyltransferasePRO_0000074585Add
    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

    PaxDbiQ64666.

    PTM databases

    iPTMnetiQ64666.
    PhosphoSiteiQ64666.

    Expressioni

    Tissue specificityi

    Highly expressed at night in pinealocytes and in the retina. Expressed at very low levels in the hindbrain and midbrain.2 Publications

    Inductioni

    Exhibits night/day variations with an up to 150-fold increased expression at night. Up-regulation is due to a large degree to the release of norepinephrine from nerve terminals in the pineal gland and cAMP signaling pathway. Down-regulated by light-induced proteasomal degradation. In the retina, 10-fold increased expression at night.5 Publications

    Gene expression databases

    BgeeiENSRNOG00000011182.
    GenevisibleiQ64666. RN.

    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 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

    GO - Molecular functioni

    • 14-3-3 protein binding Source: UniProtKB

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000015221.

    Chemistry

    BindingDBiQ64666.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64666.
    SMRiQ64666. Positions 23-194.
    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

    eggNOGiKOG4144. Eukaryota.
    COG0454. LUCA.
    GeneTreeiENSGT00390000015579.
    HOGENOMiHOG000115812.
    HOVERGENiHBG016332.
    InParanoidiQ64666.
    KOiK00669.
    OMAiTFTELHC.
    OrthoDBiEOG091G0KJP.
    PhylomeDBiQ64666.
    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.

    Q64666-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLSIHPLKPE ALHLPLGTSE FLGCQRRHTL PASEFRCLTP EDATSAFEIE
    60 70 80 90 100
    REAFISVSGT CPLHLDEIRH FLTLCPELSL GWFEEGCLVA FIIGSLWDKE
    110 120 130 140 150
    RLTQESLTLH RPGGRTAHLH VLAVHRTFRQ QGKGSVLLWR YLHHLGSQPA
    160 170 180 190 200
    VRRAVLMCEN ALVPFYEKFG FQAMGPCAIT MGSLTFTELQ CSLRCHTFLR

    RNSGC
    Length:205
    Mass (Da):23,142
    Last modified:November 1, 1996 - v1
    Checksum:i2504E3082A26BF8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331S → N in AAC52330 (PubMed:7502081).Curated
    Sequence conflicti153 – 1531R → P in AAC52330 (PubMed:7502081).Curated
    Sequence conflicti185 – 1851T → A in AAC52330 (PubMed:7502081).Curated
    Sequence conflicti204 – 2052GC → DR in AAC52330 (PubMed:7502081).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U38306 mRNA. Translation: AAB38484.1.
    U40803 mRNA. Translation: AAA92711.1.
    DQ075321 mRNA. Translation: AAY86767.1.
    U29664 mRNA. Translation: AAC52330.1.
    PIRiS68435.
    RefSeqiNP_036950.1. NM_012818.2.
    XP_006247854.1. XM_006247792.1.
    XP_006247855.1. XM_006247793.1.
    UniGeneiRn.88180.

    Genome annotation databases

    EnsembliENSRNOT00000015221; ENSRNOP00000015221; ENSRNOG00000011182.
    GeneIDi25120.
    KEGGirno:25120.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U38306 mRNA. Translation: AAB38484.1.
    U40803 mRNA. Translation: AAA92711.1.
    DQ075321 mRNA. Translation: AAY86767.1.
    U29664 mRNA. Translation: AAC52330.1.
    PIRiS68435.
    RefSeqiNP_036950.1. NM_012818.2.
    XP_006247854.1. XM_006247792.1.
    XP_006247855.1. XM_006247793.1.
    UniGeneiRn.88180.

    3D structure databases

    ProteinModelPortaliQ64666.
    SMRiQ64666. Positions 23-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000015221.

    Chemistry

    BindingDBiQ64666.
    ChEMBLiCHEMBL1075242.

    PTM databases

    iPTMnetiQ64666.
    PhosphoSiteiQ64666.

    Proteomic databases

    PaxDbiQ64666.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSRNOT00000015221; ENSRNOP00000015221; ENSRNOG00000011182.
    GeneIDi25120.
    KEGGirno:25120.

    Organism-specific databases

    CTDi15.
    RGDi2006. Aanat.

    Phylogenomic databases

    eggNOGiKOG4144. Eukaryota.
    COG0454. LUCA.
    GeneTreeiENSGT00390000015579.
    HOGENOMiHOG000115812.
    HOVERGENiHBG016332.
    InParanoidiQ64666.
    KOiK00669.
    OMAiTFTELHC.
    OrthoDBiEOG091G0KJP.
    PhylomeDBiQ64666.
    TreeFamiTF331622.

    Enzyme and pathway databases

    UniPathwayiUPA00837; UER00815.
    BRENDAi2.3.1.87. 5301.
    ReactomeiR-RNO-209931. Serotonin and melatonin biosynthesis.

    Miscellaneous databases

    PROiQ64666.

    Gene expression databases

    BgeeiENSRNOG00000011182.
    GenevisibleiQ64666. RN.

    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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSNAT_RAT
    AccessioniPrimary (citable) accession number: Q64666
    Secondary accession number(s): Q4JL74, Q64553
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: September 7, 2016
    This is version 129 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.