Q5H879 · COMT_HORSE
- ProteinCatechol O-methyltransferase
- GeneCOMT
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids269 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
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.
- 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
Note: Binds 1 Mg2+ ion per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 89 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 111 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 119 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 137 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 138 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 164-167 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: GASQ | ||||||
Binding site | 166 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 188 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 188 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 191 | substrate | ||||
Sequence: K | ||||||
Binding site | 216 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 217 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 217 | substrate | ||||
Sequence: N | ||||||
Binding site | 246 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | cytosol | |
Cellular Component | dendrite | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | catechol O-methyltransferase activity | |
Molecular Function | magnesium ion binding | |
Biological Process | catecholamine catabolic process | |
Biological Process | developmental process | |
Biological Process | dopamine metabolic process | |
Biological Process | lipid metabolic process | |
Biological Process | methylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCatechol O-methyltransferase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Equidae > Equus
Accessions
- Primary accessionQ5H879
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Isoform Soluble
Isoform Membrane-bound
Cell membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-4 | Cytoplasmic | ||||
Sequence: MLEP | ||||||
Transmembrane | 5-25 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: TPMLLAAFSLGLALLPLLFFL | ||||||
Topological domain | 26-269 | Extracellular | ||||
Sequence: RRWGWLLIGWNECILQPIHNLLMGDSKEQRILRHVLQHAVAGDPQSVLETIDAYCSQKEWAMNVGDKKGQFLDAVVQEQQPSVLLELGAYCGYSAVRMARLLPPGARLLTIEINPDYAAITQRMLDFAGLQDRVTVVLGASQDIIPQLKKKYDVDTLDVVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVIVPGAPDFLAHVRGSGRFECTHFSSYLEYSLWVVDGVEKAVYLGPGSPAQP |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 120 | |||||
Sequence: A → T |
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.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000318147 | 1-269 | Catechol O-methyltransferase | |||
Sequence: MLEPTPMLLAAFSLGLALLPLLFFLRRWGWLLIGWNECILQPIHNLLMGDSKEQRILRHVLQHAVAGDPQSVLETIDAYCSQKEWAMNVGDKKGQFLDAVVQEQQPSVLLELGAYCGYSAVRMARLLPPGARLLTIEINPDYAAITQRMLDFAGLQDRVTVVLGASQDIIPQLKKKYDVDTLDVVFLDHWKDRYLPDTLLLEECGLLRKGTVLLADNVIVPGAPDFLAHVRGSGRFECTHFSSYLEYSLWVVDGVEKAVYLGPGSPAQP | ||||||
Modified residue | 265 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- NameMembrane-bound
- SynonymsMB-COMT
- Length269
- Mass (Da)30,028
- Last updated2005-03-01 v1
- Checksum73A24585C6768C44
Q5H879-2
- NameSoluble
- SynonymsS-COMT
- Differences from canonical
- 1-47: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_031176 | 1-47 | in isoform Soluble | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB178284 EMBL· GenBank· DDBJ | BAD89294.1 EMBL· GenBank· DDBJ | mRNA | ||
AB178284 EMBL· GenBank· DDBJ | BAD89295.1 EMBL· GenBank· DDBJ | mRNA |