P40936 · INMT_MOUSE
- ProteinIndolethylamine N-methyltransferase
- GeneInmt
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids264 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the N-methylation of tryptamine and structurally related compounds (By similarity).
Functions as a thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds
Functions as a thioether S-methyltransferase and is active with a variety of thioethers and the corresponding selenium and tellurium compounds, including 3-methylthiopropionaldehyde, dimethyl selenide, dimethyl telluride, 2-methylthioethylamine, 2-methylthioethanol, methyl-n-propyl sulfide and diethyl sulfide. Plays an important role in the detoxification of selenium compounds
Catalytic activity
- a tertiary amine + S-adenosyl-L-methionine = a methylated tertiary amine + H+ + S-adenosyl-L-homocysteine
Activity regulation
Inhibited by the S-adenosyl-L-methionine analog sinefungin and by the product S-adenosyl-L-homocysteine.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.4 μM | dimethyl selenide | |||||
1 μM | dimethyl sulfide | |||||
1 μM | S-adenosyl-L-methionine |
pH Dependence
Optimum pH is 6.3.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 21 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 26 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 64-65 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GS | ||||||
Binding site | 70 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 86 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 91 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 143-144 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: DV | ||||||
Binding site | 164 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | amine N-methyltransferase activity | |
Molecular Function | dimethyl selenide methyltransferase activity | |
Molecular Function | N-methyltransferase activity | |
Molecular Function | S-adenosyl-L-methionine:beta-alanine N-methyltransferase activity | |
Molecular Function | thioether S-methyltransferase activity | |
Biological Process | amine metabolic process | |
Biological Process | methylation | |
Biological Process | response to toxic substance |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameIndolethylamine N-methyltransferase
- EC number
- Short namesIndolamine N-methyltransferase
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP40936
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000159713 | 1-264 | Indolethylamine N-methyltransferase | |||
Sequence: MEGKVYIGGEDYEKEFTPKDYLTTYYSFHSGPVAEQEIVKFSLQNLYQTFSTGGVGGDVLIDIGSGPTIYQLLSACEVFREIIVTDYTPQNLQELQKWLKKEPGAYDWSSIVQHACELEGDRSRWQEKEAKLRRTVTRVLRCDVTKTPPLGSAQVPLADCVLTFLAMECACPDIDTYRAALRRLAGLLKPGGHLVTLVTLRFQHYMVGPKKFSGVYLEKEVVEKAIQDAGCQVLKCNCVSLSYSEAYCSHDGLCFVVARKGPSA | ||||||
Modified residue | 14 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 97 | N6-succinyllysine | ||||
Sequence: K |
Proteomic databases
PTM databases
Expression
Structure
Sequence
- Sequence statusComplete
- Length264
- Mass (Da)29,460
- Last updated1995-02-01 v1
- Checksum58AC5BA580AFB2EE
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 92 | in Ref. 2; BAB28594 | ||||
Sequence: L → M |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M88694 EMBL· GenBank· DDBJ | AAA62365.1 EMBL· GenBank· DDBJ | mRNA | ||
AK002281 EMBL· GenBank· DDBJ | BAB21985.1 EMBL· GenBank· DDBJ | mRNA | ||
AK013010 EMBL· GenBank· DDBJ | BAB28594.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013518 EMBL· GenBank· DDBJ | AAH13518.1 EMBL· GenBank· DDBJ | mRNA |