Q99028 (COMT_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catechol O-methyltransferase
EC=2.1.1.6

Gene names

Name:

COMT

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	186 AA.
Sequence status	Fragment.
Protein existence	Evidence at protein level

General annotation (Comments)

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	S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity. Cell membrane; Single-pass type II membrane protein; Extracellular side By similarity.
Sequence similarities	Belongs to the methyltransferase superfamily. Catechol-O-methyltransferase family.

Ontologies

Keywords
Biological process	Catecholamine metabolism Neurotransmitter degradation
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	Magnesium Metal-binding S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	catecholamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW neurotransmitter catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	catechol O-methyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 186	›186	Catechol O-methyltransferase		PRO_0000090016
Regions
	Region	82 – 85	4	S-adenosyl-L-methionine binding By similarity
Sites
	Metal binding	106	1	Magnesium By similarity
	Metal binding	134	1	Magnesium By similarity
	Metal binding	135	1	Magnesium By similarity
	Binding site	7	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	37	1	S-adenosyl-L-methionine By similarity
	Binding site	55	1	S-adenosyl-L-methionine By similarity
	Binding site	106	1	S-adenosyl-L-methionine By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	135	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q99028 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 493B8801F06C6262	FASTA	186	20,587
	10 20 30 40 50 60 KERAMHVGRK KGQIVDTVVQ EQRPSVLLEL GAYCGYSAVR MARLLLPSAR LLTIELNPDN 70 80 90 100 110 120 AAIAQQVVDF AGLQDRVTVV VGASQDIIPQ LKKKYDVDTL DMVFLDHWKD RYLPDTLLLE 130 140 150 160 170 180 ECGLLRKGTV LLADNVICPG APDFLAHVRG CGRFECTHFS SYLEYSQMVD GLEKAVYKGP GSPAQP

References

[1]	"Human catechol-O-methyltransferase: cloning and expression of the membrane-associated form." Bertocci B., Miggiano V., da Prada M., Dembic Z., Lahm H.-W., Malherbe P. Proc. Natl. Acad. Sci. U.S.A. 88:1416-1420(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Immunoaffinity purification and partial amino acid sequence analysis of catechol-O-methyltransferase from pig liver." Bertocci B., Garotta G., da Prada M., Lahm H.-W., Zurcher G., Virgallita G., Miggiano V. Biochim. Biophys. Acta 1080:103-109(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Liver.

Cross-references

3D structure databases
ProteinModelPortal	Q99028.
SMR	Q99028. Positions 1-180.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000010805.
Proteomic databases
PaxDb	Q99028.
PRIDE	Q99028.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG4122.
HOGENOM	HOG000046392.
HOVERGEN	HBG005376.
OrthoDB	EOG4G1MH8.
Family and domain databases
InterPro	IPR025782. Catechol_O-MeTrfase. IPR002935. O-MeTrfase_3. [Graphical view]
PANTHER	PTHR10509. PTHR10509. 1 hit.
Pfam	PF01596. Methyltransf_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COMT_PIG

Accession

Primary (citable) accession number: Q99028

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program