Q5H879 · COMT_HORSE

  • Protein
    Catechol O-methyltransferase
  • Gene
    COMT
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

Function

function

Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.

Catalytic activity

  • a catechol + S-adenosyl-L-methionine = a guaiacol + S-adenosyl-L-homocysteine + H+
    This reaction proceeds in the forward direction.
    EC:2.1.1.6 (UniProtKB | ENZYME | Rhea)
  • 2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-estrone + S-adenosyl-L-homocysteine + H+
    This reaction proceeds in the forward direction.
  • 4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone + S-adenosyl-L-homocysteine + H+
    This reaction proceeds in the forward direction.
  • 2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone + S-adenosyl-L-homocysteine + H+
    This reaction proceeds in the forward direction.
  • 4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4-methoxy-17beta-estradiol + S-adenosyl-L-homocysteine + H+
    This reaction proceeds in the forward direction.
  • 2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-hydroxy-3-methoxy-17beta-estradiol + S-adenosyl-L-homocysteine + H+
    This reaction proceeds in the forward direction.
  • 2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-methoxy-17beta-estradiol + S-adenosyl-L-homocysteine + H+
    This reaction proceeds in the forward direction.

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site89S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site111S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site119S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site137S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site138S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site164-167S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site166S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site188Mg2+ (UniProtKB | ChEBI)
Binding site188S-adenosyl-L-methionine (UniProtKB | ChEBI)
Binding site191substrate
Binding site216Mg2+ (UniProtKB | ChEBI)
Binding site217Mg2+ (UniProtKB | ChEBI)
Binding site217substrate
Binding site246substrate

GO annotations

AspectTerm
Cellular Componentaxon
Cellular Componentcytosol
Cellular Componentdendrite
Cellular Componentmembrane
Cellular Componentplasma membrane
Molecular Functioncatechol O-methyltransferase activity
Molecular Functionmagnesium ion binding
Biological Processcatecholamine catabolic process
Biological Processdevelopmental process
Biological Processdopamine metabolic process
Biological Processlipid metabolic process
Biological Processmethylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Catechol O-methyltransferase
  • EC number

Gene names

    • Name
      COMT

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Equidae > Equus

Accessions

  • Primary accession
    Q5H879
  • Secondary accessions
    • Q5H878

Proteomes

Subcellular Location

Isoform Soluble

Cytoplasm

Isoform Membrane-bound

Cell membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-4Cytoplasmic
Transmembrane5-25Helical; Signal-anchor for type II membrane protein
Topological domain26-269Extracellular

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant120

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003181471-269Catechol O-methyltransferase
Modified residue265Phosphoserine

Keywords

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative initiation.

Q5H879-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Name
    Membrane-bound
  • Synonyms
    MB-COMT
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    269
  • Mass (Da)
    30,028
  • Last updated
    2005-03-01 v1
  • Checksum
    73A24585C6768C44
MLEPTPMLLAAFSLGLALLPLLFFLRRWGWLLIGWNECILQPIHNLLMGDSKEQRILRHVLQHAVAGDPQSVLETIDAYCSQKEWAMNVGDKKGQFLDAVVQEQQPSVLLELGAYCGYSAVRMARLLPPGARLLTIEINPDYAAITQRMLDFAGLQDRVTVVLGASQDIIPQLKKKYDVDTLDVVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVIVPGAPDFLAHVRGSGRFECTHFSSYLEYSLWVVDGVEKAVYLGPGSPAQP

Q5H879-2

  • Name
    Soluble
  • Synonyms
    S-COMT
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_0311761-47in isoform Soluble

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB178284
EMBL· GenBank· DDBJ
BAD89294.1
EMBL· GenBank· DDBJ
mRNA
AB178284
EMBL· GenBank· DDBJ
BAD89295.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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