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Q99028 (COMT_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Catechol O-methyltransferase

EC=2.1.1.6
Gene names
Name:COMT
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length186 AA.
Sequence statusFragment.
Protein existenceEvidence 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 class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 186›186Catechol O-methyltransferase
PRO_0000090016

Regions

Region82 – 854S-adenosyl-L-methionine binding By similarity

Sites

Metal binding1061Magnesium By similarity
Metal binding1341Magnesium By similarity
Metal binding1351Magnesium By similarity
Binding site71S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site291S-adenosyl-L-methionine By similarity
Binding site371S-adenosyl-L-methionine By similarity
Binding site551S-adenosyl-L-methionine By similarity
Binding site561S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site841S-adenosyl-L-methionine; via amide nitrogen By similarity
Binding site1061S-adenosyl-L-methionine By similarity
Binding site1091Substrate By similarity
Binding site1351Substrate By similarity
Binding site1641Substrate By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q99028 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 493B8801F06C6262

FASTA18620,587
        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 

« Hide

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

ProteinModelPortalQ99028.
SMRQ99028. Positions 1-180.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000010805.

Chemistry

ChEMBLCHEMBL2176837.

Proteomic databases

PaxDbQ99028.
PRIDEQ99028.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG4122.
HOGENOMHOG000046392.
HOVERGENHBG005376.

Family and domain databases

InterProIPR025782. Catechol_O-MeTrfase.
IPR002935. O-MeTrfase_3.
[Graphical view]
PANTHERPTHR10509. PTHR10509. 1 hit.
PfamPF01596. Methyltransf_3. 1 hit.
[Graphical view]
PROSITEPS51682. SAM_OMT_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOMT_PIG
AccessionPrimary (citable) accession number: Q99028
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: December 11, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families