ASMT_MUSMM
ID ASMT_MUSMM Reviewed; 387 AA.
AC D3KU67;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Acetylserotonin O-methyltransferase;
DE EC=2.1.1.4 {ECO:0000250|UniProtKB:D3KU66};
DE AltName: Full=Hydroxyindole O-methyltransferase;
GN Name=Asmt; Synonyms=Hiomt;
OS Mus musculus molossinus (Japanese house mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=57486;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pineal gland;
RX PubMed=20308563; DOI=10.1073/pnas.0914399107;
RA Kasahara T., Abe K., Mekada K., Yoshiki A., Kato T.;
RT "Genetic variation of melatonin productivity in laboratory mice under
RT domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6412-6417(2010).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group onto N-
CC acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
CC {ECO:0000250|UniProtKB:D3KU66}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetylserotonin + S-adenosyl-L-methionine = H(+) + melatonin
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15573, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16796, ChEBI:CHEBI:17697, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.4;
CC Evidence={ECO:0000250|UniProtKB:D3KU66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15574;
CC Evidence={ECO:0000250|UniProtKB:D3KU66};
CC -!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
CC melatonin from serotonin: step 1/2. {ECO:0000250|UniProtKB:D3KU66}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Pineal melatonin synthesis is severely compromised in
CC most inbred strains. In many inbred strains, genetic defects in ASMT
CC have been identified. Melatonin production may have an impact on
CC gonadal development, testis development being significantly promoted in
CC melatonin-deficient C57BL/6J x Mus musculus molossinus animals.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-independent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01020}.
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DR EMBL; AB512672; BAI82193.1; -; mRNA.
DR AlphaFoldDB; D3KU67; -.
DR SMR; D3KU67; -.
DR PRIDE; D3KU67; -.
DR MGI; MGI:96090; Asmt.
DR UniPathway; UPA00837; UER00815.
DR GO; GO:0017096; F:acetylserotonin O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030187; P:melatonin biosynthetic process; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR031725; ASMT_dimerisation.
DR InterPro; IPR016461; COMT-like.
DR InterPro; IPR001077; O_MeTrfase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11746; PTHR11746; 1.
DR Pfam; PF16864; Dimerisation2; 1.
DR Pfam; PF00891; Methyltransf_2; 1.
DR PIRSF; PIRSF005739; O-mtase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51683; SAM_OMT_II; 1.
PE 2: Evidence at transcript level;
KW Lipid metabolism; Melatonin biosynthesis; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..387
FT /note="Acetylserotonin O-methyltransferase"
FT /id="PRO_0000414795"
FT REGION 355..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 266
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 170
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 216
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 246..248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 263
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01020"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 40978 MW; D1C30B8876BFD39B CRC64;
MHRGRSASAR QERDFRALMD LAHGFMASQV LFAGCALRVF DAAALGPVDA AALARSSGLS
PRGTRLLLDA CAGLGLLRRR RGAGPRGPAY TNSPLASTFL VAGSPLSQRS LLLYLAGTTY
LCWGHLADGV REGRSQYARA VGVDADDPFT AIYRSEAERL LFMRGLQETW SLCGGRVLAA
FDLSPFRVIC DLGGGSGALA RMAARLYPGS EVTVFETPDV VAAARAHFPP PADEDGAEPR
VRFLSGDFFR SPLPPADLYV LARVLHDWAD AACVELLRRV RGALRPGGAV LLVESVLSPG
GAGPTRTLLL SLTMLLQARG RERTEAEYRA LTARAGFSRL RLRRPRGPYH AMMAARGGGA
GARSDGGGGE ATSQTGSGTG REVGAQD
