COMT_MOUSE
ID COMT_MOUSE Reviewed; 265 AA.
AC O88587; Q91XH4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Catechol O-methyltransferase {ECO:0000305};
DE EC=2.1.1.6 {ECO:0000250|UniProtKB:P21964};
GN Name=Comt {ECO:0000312|MGI:MGI:88470}; Synonyms=Comt1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9707588; DOI=10.1073/pnas.95.17.9991;
RA Gogos J.A., Morgan M., Luine V., Santha M., Ogawa S., Pfaff D.,
RA Karayiorgou M.;
RT "Catechol-O-methyltransferase-deficient mice exhibit sexually dimorphic
RT changes in catecholamine levels and behavior.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:9991-9996(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP MUTAGENESIS OF ARG-51, AND FUNCTION.
RX PubMed=18794526; DOI=10.1073/pnas.0807219105;
RA Du X., Schwander M., Moresco E.M.Y., Viviani P., Haller C.,
RA Hildebrand M.S., Pak K., Tarantino L., Roberts A., Richardson H., Koob G.,
RA Najmabadi H., Ryan A.F., Smith R.J.H., Mueller U., Beutler B.;
RT "A catechol-O-methyltransferase that is essential for auditory function in
RT mice and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:14609-14614(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the O-methylation, and thereby the inactivation, of
CC catecholamine neurotransmitters and catechol hormones. Also shortens
CC the biological half-lives of certain neuroactive drugs, like L-DOPA,
CC alpha-methyl DOPA and isoproterenol. {ECO:0000269|PubMed:18794526}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-
CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:134251; EC=2.1.1.6;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17878;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3-
CC methoxy-estrone + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:53108, ChEBI:CHEBI:1156, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136980;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53109;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53104,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:87602, ChEBI:CHEBI:136972;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53105;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53100,
CC ChEBI:CHEBI:1156, ChEBI:CHEBI:1189, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53101;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4-
CC methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:53096, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:62845, ChEBI:CHEBI:136975;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53097;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-
CC hydroxy-3-methoxy-17beta-estradiol + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:53092, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28744, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:89268; Evidence={ECO:0000250|UniProtKB:P21964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53093;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2-
CC methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:53088, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744,
CC ChEBI:CHEBI:28955, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53089;
CC Evidence={ECO:0000250|UniProtKB:P21964};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P22734};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P22734};
CC -!- SUBCELLULAR LOCATION: [Isoform Soluble]: Cytoplasm
CC {ECO:0000250|UniProtKB:P22734}.
CC -!- SUBCELLULAR LOCATION: [Isoform Membrane-bound]: Cell membrane
CC {ECO:0000250|UniProtKB:P22734}; Single-pass type II membrane protein
CC {ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:P22734}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Membrane-bound; Synonyms=MB-COMT;
CC IsoId=O88587-1; Sequence=Displayed;
CC Name=Soluble; Synonyms=S-COMT;
CC IsoId=O88587-2; Sequence=VSP_018779;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; AF076156; AAC33334.1; -; mRNA.
DR EMBL; AK148311; BAE28473.1; -; mRNA.
DR EMBL; AC133487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010402; AAH10402.1; -; mRNA.
DR CCDS; CCDS28021.1; -. [O88587-1]
DR RefSeq; NP_001104532.1; NM_001111062.1. [O88587-1]
DR RefSeq; NP_001104533.1; NM_001111063.1. [O88587-1]
DR RefSeq; NP_031770.2; NM_007744.3. [O88587-1]
DR PDB; 4P58; X-ray; 2.06 A; A=47-258.
DR PDB; 4P7F; X-ray; 1.37 A; A=44-265.
DR PDBsum; 4P58; -.
DR PDBsum; 4P7F; -.
DR AlphaFoldDB; O88587; -.
DR SMR; O88587; -.
DR STRING; 10090.ENSMUSP00000111272; -.
DR BindingDB; O88587; -.
DR ChEMBL; CHEMBL3286068; -.
DR DrugCentral; O88587; -.
DR GuidetoPHARMACOLOGY; 2472; -.
DR iPTMnet; O88587; -.
DR PhosphoSitePlus; O88587; -.
DR SwissPalm; O88587; -.
DR EPD; O88587; -.
DR jPOST; O88587; -.
DR MaxQB; O88587; -.
DR PaxDb; O88587; -.
DR PeptideAtlas; O88587; -.
DR PRIDE; O88587; -.
DR ProteomicsDB; 283350; -. [O88587-1]
DR ProteomicsDB; 283351; -. [O88587-2]
DR Antibodypedia; 213; 640 antibodies from 41 providers.
DR DNASU; 12846; -.
DR Ensembl; ENSMUST00000000335; ENSMUSP00000000335; ENSMUSG00000000326. [O88587-1]
DR Ensembl; ENSMUST00000115609; ENSMUSP00000111272; ENSMUSG00000000326. [O88587-1]
DR Ensembl; ENSMUST00000165430; ENSMUSP00000130077; ENSMUSG00000000326. [O88587-1]
DR GeneID; 12846; -.
DR KEGG; mmu:12846; -.
DR UCSC; uc007ynu.2; mouse. [O88587-1]
DR CTD; 1312; -.
DR MGI; MGI:88470; Comt.
DR VEuPathDB; HostDB:ENSMUSG00000000326; -.
DR eggNOG; KOG1663; Eukaryota.
DR GeneTree; ENSGT00940000155317; -.
DR HOGENOM; CLU_050461_5_0_1; -.
DR InParanoid; O88587; -.
DR OMA; WNELVLQ; -.
DR OrthoDB; 1274244at2759; -.
DR PhylomeDB; O88587; -.
DR TreeFam; TF329140; -.
DR Reactome; R-MMU-156581; Methylation.
DR Reactome; R-MMU-379397; Enzymatic degradation of dopamine by COMT.
DR Reactome; R-MMU-379398; Enzymatic degradation of Dopamine by monoamine oxidase.
DR SABIO-RK; O88587; -.
DR BioGRID-ORCS; 12846; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Comt; mouse.
DR PRO; PR:O88587; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O88587; protein.
DR Bgee; ENSMUSG00000000326; Expressed in white adipose tissue and 112 other tissues.
DR ExpressionAtlas; O88587; baseline and differential.
DR Genevisible; O88587; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0016206; F:catechol O-methyltransferase activity; IDA:MGI.
DR GO; GO:0102084; F:L-dopa O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0102938; F:orcinol O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0042424; P:catecholamine catabolic process; ISO:MGI.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IDA:MGI.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0042420; P:dopamine catabolic process; IDA:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; IDA:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:MGI.
DR GO; GO:0007565; P:female pregnancy; ISO:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR GO; GO:0048609; P:multicellular organismal reproductive process; ISO:MGI.
DR GO; GO:0045963; P:negative regulation of dopamine metabolic process; ISO:MGI.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050668; P:positive regulation of homocysteine metabolic process; ISO:MGI.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0048265; P:response to pain; ISO:MGI.
DR GO; GO:0007614; P:short-term memory; ISO:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR017128; Catechol_O-MeTrfase_euk.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
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 3D-structure; Alternative initiation; Catecholamine metabolism;
KW Cell membrane; Cytoplasm; Lipid metabolism; Magnesium; Membrane;
KW Metal-binding; Methyltransferase; Neurotransmitter degradation;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..265
FT /note="Catechol O-methyltransferase"
FT /id="PRO_0000020973"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..19
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 20..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 107
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 160..163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22734"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P22734"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform Soluble)"
FT /evidence="ECO:0000305"
FT /id="VSP_018779"
FT MUTAGEN 51
FT /note="R->L: Reduces methyltransferase activity against
FT norepinephrine."
FT /evidence="ECO:0000269|PubMed:18794526"
FT CONFLICT 162
FT /note="S -> P (in Ref. 1; AAC33334)"
FT /evidence="ECO:0000305"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 169..173
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:4P7F"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:4P7F"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:4P7F"
SQ SEQUENCE 265 AA; 29486 MW; E82E9307F6D8A6CF CRC64;
MLLAAVSLGL LLLAFLLLLR HLGWGLVAIG WFEFVQQPVH NLLMGGTKEQ RILRHVQQHA
KPGDPQSVLE AIDTYCSEKE WAMNVGDAKG QIMDAVIREY RPSLVLELGA YCGYSAVRMA
RLLPPGARLL TMEINPDYAA ITQQMLDFAG LQDKVSILIG ASQDLIPQLK KKYDVDTLDM
VFLDHWKDRY LPDTLLLEEC GLLRKGTVLL ADNVIVPGTP DFLAYVRGSS SFECTHYSSY
LEYMKVVDGL EKAVYQGPGS SPVKS
