INMT_RABIT
ID INMT_RABIT Reviewed; 263 AA.
AC O97972;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Indolethylamine N-methyltransferase;
DE Short=Indolamine N-methyltransferase;
DE EC=2.1.1.49;
DE EC=2.1.1.96;
DE AltName: Full=Aromatic alkylamine N-methyltransferase;
DE Short=Amine N-methyltransferase;
DE Short=Arylamine N-methyltransferase;
DE AltName: Full=Thioether S-methyltransferase;
GN Name=INMT;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 1-129, AND
RP CHARACTERIZATION.
RC TISSUE=Lung;
RX PubMed=9852119; DOI=10.1074/jbc.273.51.34502;
RA Thompson M.A., Weinshilboum R.M.;
RT "Rabbit lung indolethylamine N-methyltransferase. cDNA and gene cloning and
RT characterization.";
RL J. Biol. Chem. 273:34502-34510(1998).
RN [2]
RP CHARACTERIZATION.
RC TISSUE=Lung;
RX PubMed=7074100; DOI=10.1021/bi00535a054;
RA Irace G., Colonna G., Camardella M., Della Pietra G., Porta R.;
RT "Purification and molecular properties of rabbit lung indolamine N-
RT methyltransferase.";
RL Biochemistry 21:1464-1470(1982).
CC -!- FUNCTION: Catalyzes the N-methylation of tryptamine and structurally
CC related compounds (By similarity). Functions as thioether S-
CC methyltransferase and is active with a variety of thioethers and the
CC corresponding selenium and tellurium compounds, including 3-
CC methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-
CC methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and
CC diethyl sulfide. Plays an important role in the detoxification of
CC selenium compounds (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tertiary amine + S-adenosyl-L-methionine = a methylated
CC tertiary amine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:53928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:137982, ChEBI:CHEBI:137983;
CC EC=2.1.1.49;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary amine + S-adenosyl-L-methionine = a methylated
CC secondary amine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:53924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:137419, ChEBI:CHEBI:137984;
CC EC=2.1.1.49;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary amine + S-adenosyl-L-methionine = a methylated
CC primary amine + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:23136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65296, ChEBI:CHEBI:131823;
CC EC=2.1.1.49;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethyl sulfide + S-adenosyl-L-methionine = S-adenosyl-L-
CC homocysteine + trimethylsulfonium; Xref=Rhea:RHEA:19613,
CC ChEBI:CHEBI:17434, ChEBI:CHEBI:17437, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789; EC=2.1.1.96;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, also detected in liver
CC and at very low levels in brain.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. NNMT/PNMT/TEMT family. {ECO:0000305}.
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DR EMBL; AF077828; AAC97492.1; -; Genomic_DNA.
DR EMBL; AF077827; AAC97492.1; JOINED; Genomic_DNA.
DR EMBL; AF077826; AAC97491.1; -; mRNA.
DR RefSeq; NP_001075512.1; NM_001082043.1.
DR AlphaFoldDB; O97972; -.
DR SMR; O97972; -.
DR STRING; 9986.ENSOCUP00000021686; -.
DR BindingDB; O97972; -.
DR ChEMBL; CHEMBL3227915; -.
DR Ensembl; ENSOCUT00000024664; ENSOCUP00000021686; ENSOCUG00000024221.
DR GeneID; 100008695; -.
DR KEGG; ocu:100008695; -.
DR CTD; 11185; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00390000011708; -.
DR InParanoid; O97972; -.
DR OrthoDB; 1054662at2759; -.
DR TreeFam; TF313114; -.
DR SABIO-RK; O97972; -.
DR Proteomes; UP000001811; Chromosome 10.
DR Bgee; ENSOCUG00000024221; Expressed in lung and 18 other tissues.
DR ExpressionAtlas; O97972; baseline.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030748; F:amine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0102707; F:S-adenosyl-L-methionine:beta-alanine N-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004790; F:thioether S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR025820; NNMT/PNMT/TEMT_CS.
DR InterPro; IPR000940; NNMT_TEMT_trans.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10867; PTHR10867; 1.
DR Pfam; PF01234; NNMT_PNMT_TEMT; 1.
DR PIRSF; PIRSF000384; PNMTase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01100; NNMT_PNMT_TEMT; 1.
DR PROSITE; PS51681; SAM_MT_NNMT_PNMT_TEMT; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Detoxification; Direct protein sequencing; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..263
FT /note="Indolethylamine N-methyltransferase"
FT /id="PRO_0000159715"
FT BINDING 20
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 63..64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 142..143
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40936"
FT MOD_RES 96
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P40936"
SQ SEQUENCE 263 AA; 28955 MW; 42F368414BE8B459 CRC64;
MEGGFTGGDE YQKHFLPRDY LNTYYSFQSG PSPEAEMLKF NLECLHKTFG PGGLQGDTLI
DIGSGPTIYQ VLAACESFKD ITLSDFTDRN REELAKWLKK EPGAYDWTPA LKFACELEGN
SGRWQEKAEK LRATVKRVLK CDANLSNPLT PVVLPPADCV LTLLAMECAC CSLDAYRAAL
RNLASLLKPG GHLVTTVTLQ LSSYMVGERE FSCVALEKEE VEQAVLDAGF DIEQLLYSPQ
SYSASTAPNR GVCFLVARKK PGS
