Acetylserotonin O-methyltransferase

Details

Name
Acetylserotonin O-methyltransferase
Synonyms
  • 2.1.1.4
  • HIOMT
  • Hydroxyindole O-methyltransferase
Gene Name
ASMT
Organism
Humans
Amino acid sequence
>lcl|BSEQ0006846|Acetylserotonin O-methyltransferase
MGSSEDQAYRLLNDYANGFMVSQVLFAACELGVFDLLAEAPGPLDVAAVAAGVRASAHGT
ELLLDICVSLKLLKVETRGGKAFYRNTELSSDYLTTVSPTSQCSMLKYMGRTSYRCWGHL
ADAVREGRNQYLETFGVPAEELFTAIYRSEGERLQFMQALQEVWSVNGRSVLTAFDLSVF
PLMCDLGGGAGALAKECMSLYPGCKITVFDIPEVVWTAKQHFSFQEEEQIDFQEGDFFKD
PLPEADLYILARVLHDWADGKCSHLLERIYHTCKPGGGILVIESLLDEDRRGPLLTQLYS
LNMLVQTEGQERTPTHYHMLLSSAGFRDFQFKKTGAIYDAILARK
Number of residues
345
Molecular Weight
38452.51
Theoretical pI
4.82
GO Classification
Functions
acetylserotonin O-methyltransferase activity / identical protein binding / O-methyltransferase activity / protein homodimerization activity
Processes
cellular nitrogen compound metabolic process / indolalkylamine biosynthetic process / melatonin biosynthetic process / methylation / small molecule metabolic process / translation
Components
cytosol
General Function
Protein homodimerization activity
Specific Function
Isoform 1 catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine). Isoform 2 and isoform 3 lack enzyme activity.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0019436|Acetylserotonin O-methyltransferase (ASMT)
ATGGGATCCTCAGAGGACCAGGCCTATCGCCTCCTTAATGACTACGCCAACGGCTTCATG
GTGTCCCAGGTTCTCTTCGCCGCCTGCGAGCTGGGCGTGTTTGACCTTCTCGCCGAGGCC
CCAGGGCCCCTGGACGTGGCGGCAGTGGCTGCAGGTGTGAGGGCCAGCGCCCATGGGACA
GAGCTCCTGCTGGACATCTGTGTGTCCCTGAAGCTGCTGAAAGTGGAGACGAGGGGAGGA
AAAGCTTTCTATCGAAACACAGAGCTGTCCAGCGACTACCTGACCACGGTCAGCCCGACG
TCACAATGCAGCATGCTGAAGTACATGGGCAGGACCAGCTACCGGTGCTGGGGCCACCTG
GCAGACGCCGTGAGAGAAGGAAGGAACCAGTACCTGGAGACGTTTGGCGTTCCCGCTGAA
GAGCTTTTTACGGCCATCTACAGGTCCGAGGGCGAGCGGCTACAGTTCATGCAAGCTCTG
CAGGAGGTCTGGAGCGTCAACGGGAGAAGCGTGCTGACCGCCTTTGACCTGTCAGTGTTC
CCACTTATGTGTGACCTTGGTGGGACATGGATAAAGCTGGAAACCATCATTCTCAGCAAA
CTATCGCAAGGACAGAAAACCAAACACCGCGTGTTCTCACTCATAGGTGGGGCTGGAGCT
CTGGCTAAGGAATGCATGTCTCTGTACCCTGGATGTAAGATCACCGTTTTTGACATCCCA
GAAGTGGTGTGGACGGCAAAGCAGCACTTCTCATTCCAGGAGGAAGAACAGATTGACTTC
CAGGAAGGGGATTTCTTCAAAGACCCTCTTCCGGAAGCTGATCTGTACATCCTGGCCAGG
GTCCTCCATGACTGGGCAGACGGAAAGTGCTCACACCTGCTGGAGAGGATCTACCACACT
TGCAAGCCAGGTGGTGGCATTCTGGTAATTGAAAGCCTCCTGGATGAAGACAGGCGAGGT
CCTCTGCTCACGCAGCTCTACTCTCTGAACATGCTTGTGCAGACGGAAGGGCAGGAGAGG
ACCCCCACCCACTACCACATGCTCCTCTCTTCTGCTGGCTTCAGAGACTTCCAGTTTAAG
AAAACAGGAGCCATTTATGATGCCATTTTAGCCAGGAAATAA
Chromosome Location
X, Y
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP46597
UniProtKB Entry NameASMT_HUMAN
GenBank Protein ID607840
GenBank Gene IDU11090
HGNC IDHGNC:750
General References
  1. Rodriguez IR, Mazuruk K, Schoen TJ, Chader GJ: Structural analysis of the human hydroxyindole-O-methyltransferase gene. Presence of two distinct promoters. J Biol Chem. 1994 Dec 16;269(50):31969-77. [Article]
  2. Donohue SJ, Roseboom PH, Illnerova H, Weller JL, Klein DC: Human hydroxyindole-O-methyltransferase: presence of LINE-1 fragment in a cDNA clone and pineal mRNA. DNA Cell Biol. 1993 Oct;12(8):715-27. [Article]
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  6. Bernard M, Donohue SJ, Klein DC: Human hydroxyindole-O-methyltransferase in pineal gland, retina and Y79 retinoblastoma cells. Brain Res. 1995 Oct 23;696(1-2):37-48. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01065Melatoninapproved, nutraceutical, vet_approvedunknownDetails
DB01065Melatoninapproved, nutraceutical, vet_approvedunknownsubstrateDetails