UniProt functional annotation for P22734



	UniProt functional annotation for P22734

UniProt code: P22734.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

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. {ECO:0000269|PubMed:12237326, ECO:0000269|PubMed:16618795}.

Catalytic activity: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S- adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17878; Evidence={ECO:0000250|UniProtKB:P21964};

Catalytic activity: Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3- methoxy-estrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53108, ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136980; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53109; Evidence={ECO:0000250|UniProtKB:P21964};

Catalytic activity: Reaction=4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53104, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87602, ChEBI:CHEBI:136972; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53105; Evidence={ECO:0000250|UniProtKB:P21964};

Catalytic activity: Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53100, ChEBI:CHEBI:1156, ChEBI:CHEBI:1189, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53101; Evidence={ECO:0000250|UniProtKB:P21964};

Catalytic activity: Reaction=4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4- methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53096, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:62845, ChEBI:CHEBI:136975; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53097; Evidence={ECO:0000250|UniProtKB:P21964};

Catalytic activity: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2- hydroxy-3-methoxy-17beta-estradiol + H(+) + S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:53092, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:89268; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53093; Evidence={ECO:0000250|UniProtKB:P21964};

Catalytic activity: Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2- methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53088, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:28955, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000250|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53089; Evidence={ECO:0000250|UniProtKB:P21964};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:16618795};

Biophysicochemical properties: Kinetic parameters: KM=30 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:16618795}; Vmax=377 nmol/h/mg enzyme {ECO:0000269|PubMed:16618795};

Subcellular location: [Isoform Soluble]: Cytoplasm {ECO:0000269|PubMed:1765063}.

Subcellular location: [Isoform Membrane-bound]: Cell membrane {ECO:0000269|PubMed:1765063}; Single-pass type II membrane protein {ECO:0000255}; Extracellular side {ECO:0000305|PubMed:1765063}.

Ptm: The N-terminus is blocked.

Similarity: Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01019}.

Sequence caution: Sequence=AAA40881.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAA40882.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



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. {ECO:0000269\|PubMed:12237326, ECO:0000269\|PubMed:16618795}.


Catalytic activity:		Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S- adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000250\|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17878; Evidence={ECO:0000250\|UniProtKB:P21964};
Catalytic activity:		Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-hydroxy-3- methoxy-estrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53108, ChEBI:CHEBI:1156, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:136980; Evidence={ECO:0000250\|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53109; Evidence={ECO:0000250\|UniProtKB:P21964};
Catalytic activity:		Reaction=4-hydroxyestrone + S-adenosyl-L-methionine = 4-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53104, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87602, ChEBI:CHEBI:136972; Evidence={ECO:0000250\|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53105; Evidence={ECO:0000250\|UniProtKB:P21964};
Catalytic activity:		Reaction=2-hydroxyestrone + S-adenosyl-L-methionine = 2-methoxyestrone + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53100, ChEBI:CHEBI:1156, ChEBI:CHEBI:1189, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000250\|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53101; Evidence={ECO:0000250\|UniProtKB:P21964};
Catalytic activity:		Reaction=4-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 4- methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53096, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:62845, ChEBI:CHEBI:136975; Evidence={ECO:0000250\|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53097; Evidence={ECO:0000250\|UniProtKB:P21964};
Catalytic activity:		Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2- hydroxy-3-methoxy-17beta-estradiol + H(+) + S-adenosyl-L- homocysteine; Xref=Rhea:RHEA:53092, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:89268; Evidence={ECO:0000250\|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53093; Evidence={ECO:0000250\|UniProtKB:P21964};
Catalytic activity:		Reaction=2-hydroxy-17beta-estradiol + S-adenosyl-L-methionine = 2- methoxy-17beta-estradiol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:53088, ChEBI:CHEBI:15378, ChEBI:CHEBI:28744, ChEBI:CHEBI:28955, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; Evidence={ECO:0000250\|UniProtKB:P21964}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53089; Evidence={ECO:0000250\|UniProtKB:P21964};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269\|PubMed:16618795};
Biophysicochemical properties:		Kinetic parameters: KM=30 uM for S-adenosyl-L-methionine {ECO:0000269\|PubMed:16618795}; Vmax=377 nmol/h/mg enzyme {ECO:0000269\|PubMed:16618795};
Subcellular location:		[Isoform Soluble]: Cytoplasm {ECO:0000269\|PubMed:1765063}.
Subcellular location:		[Isoform Membrane-bound]: Cell membrane {ECO:0000269\|PubMed:1765063}; Single-pass type II membrane protein {ECO:0000255}; Extracellular side {ECO:0000305\|PubMed:1765063}.
Ptm:		The N-terminus is blocked.
Similarity:		Belongs to the class I-like SAM-binding methyltransferase superfamily. Cation-dependent O-methyltransferase family. {ECO:0000255\|PROSITE-ProRule:PRU01019}.
Sequence caution:		Sequence=AAA40881.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; Sequence=AAA40882.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};