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Protein

Acetylserotonin O-methyltransferase

Gene

Asmt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).By similarity

Catalytic activityi

S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + melatonin.

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
Binding sitei146 – 1461S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei163 – 1631S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei209 – 2091S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei252 – 2521S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei255 – 2551Proton donor/acceptorBy similarity
Binding sitei256 – 2561SubstrateBy similarity
Binding sitei302 – 3021SubstrateBy similarity
Binding sitei306 – 3061SubstrateBy similarity

GO - Molecular functioni

  • acetylserotonin O-methyltransferase activity Source: RGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: RGD

GO - Biological processi

  • melatonin biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Melatonin biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylserotonin O-methyltransferase (EC:2.1.1.4)
Alternative name(s):
Hydroxyindole O-methyltransferase
Gene namesi
Name:Asmt
Synonyms:Hiomt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi708472. Asmt.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Acetylserotonin O-methyltransferasePRO_0000414796Add
BLAST

Proteomic databases

PaxDbiB3GSH5.

Expressioni

Tissue specificityi

Expressed predominantly in the pineal gland (at protein level). Very low expression, if any, in the retina.2 Publications

Inductioni

Exhibits very slight night/day variation, if any.1 Publication

Gene expression databases

GenevisibleiB3GSH5. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001791.

Structurei

3D structure databases

ProteinModelPortaliB3GSH5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni235 – 2373S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-independent O-methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3178. Eukaryota.
ENOG410XS7T. LUCA.
GeneTreeiENSGT00530000064032.
HOGENOMiHOG000247024.
HOVERGENiHBG001526.
InParanoidiB3GSH5.
KOiK00543.
OMAiKSQYHIM.
OrthoDBiEOG7W1557.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR031725. ASMT_dimerisation.
IPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF16864. Dimerisation2. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B3GSH5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPGREGELD RDFRVLMSLA HGFMVSQVLF AALDLGIFDL AAQGPVAAEA
60 70 80 90 100
VAQTGGWSPR GTQLLMDACT RLGLLRGAGD GSYTNSALSS TFLVSGSPQS
110 120 130 140 150
QRCMLLYLAG TTYGCWAHLA AGVREGRNQY SRAVGISAED PFSAIYRSEP
160 170 180 190 200
ERLLFMRGLQ ETWSLCGGRV LTAFDLSRFR VICDLGGGSG ALAQEAARLY
210 220 230 240 250
PGSSVCVFDL PDVIAAARTH FLSPGARPSV RFVAGDFFRS RLPRADLFIL
260 270 280 290 300
ARVLHDWADG ACVELLGRLH RACRPGGALL LVEAVLAKGG AGPLRSLLLS
310 320 330 340 350
LNMMLQAEGW ERQASDYRNL ATRAGFPRLQ LRRPGGPYHA MLARRGPRPG
360 370 380 390 400
IITGVGSNTT GTGSFVTGIR RDVPGARSDA AGTGSGTGNT GSGIMLQGET
410 420 430
LESEVSAPQA GSDVGGAGNE PRSGTLKQGD WK
Length:432
Mass (Da):45,588
Last modified:July 22, 2008 - v1
Checksum:i0F782CD0AB6293F5
GO

Sequence cautioni

The sequence AAB61243.1 differs from that shown. Reason: Frameshift at several positions. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L78306 mRNA. Translation: AAB61243.1. Frameshift.
EU741665 mRNA. Translation: ACD87748.1.
CH474012 Genomic DNA. Translation: EDL89812.1.
RefSeqiNP_653360.2. NM_144759.2.
UniGeneiRn.10768.

Genome annotation databases

EnsembliENSRNOT00000001791; ENSRNOP00000001791; ENSRNOG00000001324.
GeneIDi246281.
KEGGirno:246281.
UCSCiRGD:708472. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L78306 mRNA. Translation: AAB61243.1. Frameshift.
EU741665 mRNA. Translation: ACD87748.1.
CH474012 Genomic DNA. Translation: EDL89812.1.
RefSeqiNP_653360.2. NM_144759.2.
UniGeneiRn.10768.

3D structure databases

ProteinModelPortaliB3GSH5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000001791.

Proteomic databases

PaxDbiB3GSH5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001791; ENSRNOP00000001791; ENSRNOG00000001324.
GeneIDi246281.
KEGGirno:246281.
UCSCiRGD:708472. rat.

Organism-specific databases

CTDi438.
RGDi708472. Asmt.

Phylogenomic databases

eggNOGiKOG3178. Eukaryota.
ENOG410XS7T. LUCA.
GeneTreeiENSGT00530000064032.
HOGENOMiHOG000247024.
HOVERGENiHBG001526.
InParanoidiB3GSH5.
KOiK00543.
OMAiKSQYHIM.
OrthoDBiEOG7W1557.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi623661.
PROiB3GSH5.

Gene expression databases

GenevisibleiB3GSH5. RN.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.150. 1 hit.
InterProiIPR031725. ASMT_dimerisation.
IPR016461. O-MeTrfase_COMT.
IPR001077. O_MeTrfase_2.
IPR029063. SAM-dependent_MTases.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF16864. Dimerisation2. 1 hit.
PF00891. Methyltransf_2. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF53335. SSF53335. 1 hit.
PROSITEiPS51683. SAM_OMT_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Circadian regulation of hydroxyindole-O-methyltransferase mRNA levels in rat pineal and retina."
    Gauer F., Craft C.M.
    Brain Res. 737:99-109(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY.
    Tissue: Pineal gland.
  2. "Significant sequence revision of rat acetylserotonin O-methyltransferase mRNA increases length of predicted protein."
    Amaral F.G., Coon S.L., Klein D.C.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human hydroxyindole-O-methyltransferase in pineal gland, retina and Y79 retinoblastoma cells."
    Bernard M., Donohue S.J., Klein D.C.
    Brain Res. 696:37-48(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiASMT_RAT
AccessioniPrimary (citable) accession number: B3GSH5
Secondary accession number(s): O09179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: July 22, 2008
Last modified: February 17, 2016
This is version 53 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. In many inbred strains, genetic defects in ASMT have been identified. Melatonin production may have an impact on gonadal development, testis development being significantly promoted in melatonin-deficient C57BL/6J x Mus musculus molossinus animals.

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.