ID   COMT_PIG                Reviewed;         186 AA.
AC   Q99028;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   05-OCT-2016, entry version 100.
DE   RecName: Full=Catechol O-methyltransferase;
DE            EC=2.1.1.6;
DE   Flags: Fragment;
GN   Name=COMT;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1847521; DOI=10.1073/pnas.88.4.1416;
RA   Bertocci B., Miggiano V., da Prada M., Dembic Z., Lahm H.-W.,
RA   Malherbe P.;
RT   "Human catechol-O-methyltransferase: cloning and expression of the
RT   membrane-associated form.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:1416-1420(1991).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   PubMed=1932084; DOI=10.1016/0167-4838(91)90135-M;
RA   Bertocci B., Garotta G., da Prada M., Lahm H.-W., Zurcher G.,
RA   Virgallita G., Miggiano V.;
RT   "Immunoaffinity purification and partial amino acid sequence analysis
RT   of catechol-O-methyltransferase from pig liver.";
RL   Biochim. Biophys. Acta 1080:103-109(1991).
CC   -!- FUNCTION: Catalyzes the O-methylation, and thereby the
CC       inactivation, of catecholamine neurotransmitters and catechol
CC       hormones. Also shortens the biological half-lives of certain
CC       neuroactive drugs, like L-DOPA, alpha-methyl DOPA and
CC       isoproterenol.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a catechol = S-
CC       adenosyl-L-homocysteine + a guaiacol.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250};
CC       Extracellular side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. Cation-dependent O-
CC       methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR   UniGene; Ssc.46647; -.
DR   UniGene; Ssc.53711; -.
DR   ProteinModelPortal; Q99028; -.
DR   STRING; 9823.ENSSSCP00000010805; -.
DR   BindingDB; Q99028; -.
DR   ChEMBL; CHEMBL2176837; -.
DR   PaxDb; Q99028; -.
DR   PeptideAtlas; Q99028; -.
DR   PRIDE; Q99028; -.
DR   eggNOG; KOG1663; Eukaryota.
DR   eggNOG; COG4122; LUCA.
DR   HOGENOM; HOG000046392; -.
DR   HOVERGEN; HBG005376; -.
DR   InParanoid; Q99028; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016206; F:catechol O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006584; P:catecholamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR017128; Catechol_O-MeTrfase_euk.
DR   InterPro; IPR002935; O-MeTrfase_3.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   PIRSF; PIRSF037177; Catechol_O-mtfrase_euk; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   1: Evidence at protein level;
KW   Catecholamine metabolism; Cell membrane; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Magnesium; Membrane; Metal-binding;
KW   Methyltransferase; Neurotransmitter degradation; Phosphoprotein;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN        <1    186       Catechol O-methyltransferase.
FT                                /FTId=PRO_0000090016.
FT   REGION       82     85       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01019}.
FT   METAL       106    106       Magnesium. {ECO:0000250}.
FT   METAL       134    134       Magnesium. {ECO:0000250}.
FT   METAL       135    135       Magnesium. {ECO:0000250}.
FT   BINDING       7      7       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01019}.
FT   BINDING      29     29       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01019}.
FT   BINDING      37     37       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01019}.
FT   BINDING      55     55       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01019}.
FT   BINDING      56     56       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01019}.
FT   BINDING      84     84       S-adenosyl-L-methionine; via amide
FT                                nitrogen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01019}.
FT   BINDING     106    106       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01019}.
FT   BINDING     109    109       Substrate. {ECO:0000250}.
FT   BINDING     135    135       Substrate. {ECO:0000250}.
FT   BINDING     164    164       Substrate. {ECO:0000250}.
FT   MOD_RES     182    182       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P22734}.
FT   NON_TER       1      1
SQ   SEQUENCE   186 AA;  20587 MW;  493B8801F06C6262 CRC64;
     KERAMHVGRK KGQIVDTVVQ EQRPSVLLEL GAYCGYSAVR MARLLLPSAR LLTIELNPDN
     AAIAQQVVDF AGLQDRVTVV VGASQDIIPQ LKKKYDVDTL DMVFLDHWKD RYLPDTLLLE
     ECGLLRKGTV LLADNVICPG APDFLAHVRG CGRFECTHFS SYLEYSQMVD GLEKAVYKGP
     GSPAQP
//