P40936 · INMT_MOUSE

  • Protein
    Indolethylamine N-methyltransferase
  • Gene
    Inmt
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Caution

Was originally thought to be a thioether S-methyltransferase but appears to be the ortholog of human INMT.

Catalytic activity

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 μMdimethyl selenide
1 μMdimethyl sulfide
1 μMS-adenosyl-L-methionine

pH Dependence

Optimum pH is 6.3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site21S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site26S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site64-65S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site70S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site86S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site91S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site143-144S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site164S-adenosyl-L-methionine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionamine N-methyltransferase activity
Molecular Functiondimethyl selenide methyltransferase activity
Molecular FunctionN-methyltransferase activity
Molecular FunctionS-adenosyl-L-methionine:beta-alanine N-methyltransferase activity
Molecular Functionthioether S-methyltransferase activity
Biological Processamine metabolic process
Biological Processmethylation
Biological Processresponse to toxic substance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Indolethylamine N-methyltransferase
  • EC number
  • Short names
    Indolamine N-methyltransferase
  • Alternative names
    • Aromatic alkylamine N-methyltransferase (Amine N-methyltransferase; Arylamine N-methyltransferase)
    • Thioether S-methyltransferase (TEMT)

Gene names

    • Name
      Inmt
    • Synonyms
      Temt

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P40936
  • Secondary accessions
    • Q9CZ50

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00001597131-264Indolethylamine N-methyltransferase
Modified residue14N6-succinyllysine
Modified residue97N6-succinyllysine

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in lung and liver (at protein level).

Gene expression databases

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    264
  • Mass (Da)
    29,460
  • Last updated
    1995-02-01 v1
  • Checksum
    58AC5BA580AFB2EE
MEGKVYIGGEDYEKEFTPKDYLTTYYSFHSGPVAEQEIVKFSLQNLYQTFSTGGVGGDVLIDIGSGPTIYQLLSACEVFREIIVTDYTPQNLQELQKWLKKEPGAYDWSSIVQHACELEGDRSRWQEKEAKLRRTVTRVLRCDVTKTPPLGSAQVPLADCVLTFLAMECACPDIDTYRAALRRLAGLLKPGGHLVTLVTLRFQHYMVGPKKFSGVYLEKEVVEKAIQDAGCQVLKCNCVSLSYSEAYCSHDGLCFVVARKGPSA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict92in Ref. 2; BAB28594

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp