##gff-version 3 P11086 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8812853;Dbxref=PMID:8812853 P11086 UniProtKB Chain 2 282 . . . ID=PRO_0000159709;Note=Phenylethanolamine N-methyltransferase P11086 UniProtKB Binding site 35 35 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16363801,ECO:0000269|PubMed:17845018,ECO:0007744|PDB:2AN4,ECO:0007744|PDB:2G70,ECO:0007744|PDB:2G72;Dbxref=PMID:16363801,PMID:17845018 P11086 UniProtKB Binding site 40 40 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16363801,ECO:0000269|PubMed:17845018,ECO:0007744|PDB:2AN4,ECO:0007744|PDB:2G70,ECO:0007744|PDB:2G72;Dbxref=PMID:16363801,PMID:17845018 P11086 UniProtKB Binding site 79 80 . . . Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17845018,ECO:0007744|PDB:2G70,ECO:0007744|PDB:2G72;Dbxref=PMID:17845018 P11086 UniProtKB Binding site 85 85 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16363801,ECO:0000269|PubMed:17845018,ECO:0007744|PDB:2AN4,ECO:0007744|PDB:2G70,ECO:0007744|PDB:2G72;Dbxref=PMID:16363801,PMID:17845018 P11086 UniProtKB Binding site 101 101 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16363801,ECO:0000269|PubMed:17845018,ECO:0007744|PDB:2AN4,ECO:0007744|PDB:2G70,ECO:0007744|PDB:2G72;Dbxref=PMID:16363801,PMID:17845018 P11086 UniProtKB Binding site 106 106 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16363801,ECO:0000269|PubMed:17845018,ECO:0007744|PDB:2AN4,ECO:0007744|PDB:2G70,ECO:0007744|PDB:2G72;Dbxref=PMID:16363801,PMID:17845018 P11086 UniProtKB Binding site 158 159 . . . Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:17845018,ECO:0007744|PDB:2G70,ECO:0007744|PDB:2G72;Dbxref=PMID:17845018 P11086 UniProtKB Binding site 181 181 . . . Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:16363801,ECO:0000269|PubMed:17845018,ECO:0007744|PDB:2AN4,ECO:0007744|PDB:2G70,ECO:0007744|PDB:2G72;Dbxref=PMID:16363801,PMID:17845018 P11086 UniProtKB Binding site 219 219 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16363801,ECO:0007744|PDB:2AN4;Dbxref=PMID:16363801 P11086 UniProtKB Binding site 267 267 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:16363801,ECO:0007744|PDB:2AN4;Dbxref=PMID:16363801 P11086 UniProtKB Modified residue 7 7 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P11086 UniProtKB Natural variant 9 9 . . . ID=VAR_029351;Note=Slight increase in protein expression and enzyme activity with octopamine as substrate. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16277617;Dbxref=dbSNP:rs11569781,PMID:16277617 P11086 UniProtKB Natural variant 98 98 . . . ID=VAR_036829;Note=Significant decrease in protein expression and enzyme activity with octopamine as substrate. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16277617;Dbxref=dbSNP:rs36060376,PMID:16277617 P11086 UniProtKB Natural variant 112 112 . . . ID=VAR_036830;Note=No significant effect on protein expression and enzyme activity with octopamine as substrate. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16277617;Dbxref=dbSNP:rs34530498,PMID:16277617 P11086 UniProtKB Natural variant 175 175 . . . ID=VAR_036831;Note=No significant effect on protein expression and enzyme activity with octopamine as substrate. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16277617;Dbxref=dbSNP:rs34341496,PMID:16277617 P11086 UniProtKB Natural variant 188 188 . . . ID=VAR_037611;Note=S->C;Dbxref=dbSNP:rs5639 P11086 UniProtKB Natural variant 211 211 . . . ID=VAR_037612;Note=L->H;Dbxref=dbSNP:rs5640 P11086 UniProtKB Natural variant 217 217 . . . ID=VAR_037613;Note=L->Q;Dbxref=dbSNP:rs5641 P11086 UniProtKB Natural variant 254 254 . . . ID=VAR_037614;Note=R->H;Dbxref=dbSNP:rs5642 P11086 UniProtKB Natural variant 276 276 . . . ID=VAR_024547;Note=W->R;Dbxref=dbSNP:rs5643 P11086 UniProtKB Mutagenesis 35 35 . . . Note=Strongly increases KM for phenylethanolamine and S-adenosyl-L-methionine. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16363801;Dbxref=PMID:16363801 P11086 UniProtKB Mutagenesis 185 185 . . . Note=Strongly reduced enzyme activity towards phenylethanolamine. Increases affinity for S-adenosyl-L-methionine. E->A%2CQ;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16363801;Dbxref=PMID:16363801 P11086 UniProtKB Mutagenesis 185 185 . . . Note=Strongly reduced enzyme activity towards phenylethanolamine. Decreases affinity for phenylethanolamine and S-adenosyl-L-methionine 3-fold. E->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16363801;Dbxref=PMID:16363801 P11086 UniProtKB Mutagenesis 219 219 . . . Note=Reduced enzyme activity towards phenylethanolamine. Decreases affinity for phenylethanolamine 6-fold. Decreases affinity for S-adenosyl-L-methionine 2-fold. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16363801;Dbxref=PMID:16363801 P11086 UniProtKB Mutagenesis 267 267 . . . Note=Strongly reduced enzyme activity towards phenylethanolamine. Decreases affinity for phenylethanolamine 200-fold. Decreases affinity for S-adenosyl-L-methionine 3-fold. D->A%2CN;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16363801;Dbxref=PMID:16363801 P11086 UniProtKB Sequence conflict 169 170 . . . Note=SP->AQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 P11086 UniProtKB Helix 17 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 27 29 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 32 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Turn 42 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 53 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 73 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 85 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 90 92 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 95 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 104 114 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 124 134 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 140 150 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 151 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 161 163 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 173 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Turn 184 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 191 202 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 205 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 221 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 227 230 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 236 246 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 248 257 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Helix 260 262 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 265 267 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK P11086 UniProtKB Beta strand 271 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MIK