##gff-version 3 O00238 UniProtKB Signal peptide 1 13 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O00238 UniProtKB Chain 14 502 . . . ID=PRO_0000024412;Note=Bone morphogenetic protein receptor type-1B O00238 UniProtKB Topological domain 14 126 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O00238 UniProtKB Transmembrane 127 148 . . . Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255 O00238 UniProtKB Topological domain 149 502 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O00238 UniProtKB Domain 174 203 . . . Note=GS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00585 O00238 UniProtKB Domain 204 494 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O00238 UniProtKB Region 1 25 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O00238 UniProtKB Active site 332 332 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 O00238 UniProtKB Binding site 210 218 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O00238 UniProtKB Binding site 231 231 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 O00238 UniProtKB Disulfide bond 32 53 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36898 O00238 UniProtKB Disulfide bond 34 38 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36898 O00238 UniProtKB Disulfide bond 47 71 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36898 O00238 UniProtKB Disulfide bond 81 95 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36898 O00238 UniProtKB Disulfide bond 96 102 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P36898 O00238 UniProtKB Alternative sequence 1 1 . . . ID=VSP_045100;Note=In isoform 2. M->MGWLEELNWQLHIFLLILLSMHTRANFLDNM;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 O00238 UniProtKB Natural variant 31 31 . . . ID=VAR_075520;Note=In AMD3%3B uncertain significance%3B mouse BMPR1B construct containing this mutation shows reduced GDF5-dependent receptor activation%2C mouse BMPR1B construct containing this mutation shows no loss of cell membrane localization. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26105076;Dbxref=dbSNP:rs745854387,PMID:26105076 O00238 UniProtKB Natural variant 31 31 . . . ID=VAR_041401;Note=In a gastric adenocarcinoma sample%3B somatic mutation. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs200035802,PMID:17344846 O00238 UniProtKB Natural variant 53 53 . . . ID=VAR_075521;Note=In AMD3%3B mouse BMPR1B construct containing this mutation shows loss of GDF5-dependent receptor activation%2C chicken BMPR1B construct containing this mutation does not show reduced chondrocyte differentiation%2C mouse BMPR1B construct containing this mutation shows no loss of cell membrane localization. C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24129431;Dbxref=dbSNP:rs863225041,PMID:24129431 O00238 UniProtKB Natural variant 149 149 . . . ID=VAR_041402;Note=R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34231464,PMID:17344846 O00238 UniProtKB Natural variant 200 200 . . . ID=VAR_023819;Note=In BDA2%3B in animal models loss of kinase activity and loss of positive regulation of chondrocyte differentiation. I->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14523231;Dbxref=dbSNP:rs121434417,PMID:14523231 O00238 UniProtKB Natural variant 224 224 . . . ID=VAR_041403;Note=R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35973133,PMID:17344846 O00238 UniProtKB Natural variant 297 297 . . . ID=VAR_041404;Note=In a metastatic melanoma sample%3B somatic mutation. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 O00238 UniProtKB Natural variant 325 325 . . . ID=VAR_076406;Note=In BDA1D%3B acts in a dominant-negative manner. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25758993;Dbxref=dbSNP:rs869025614,PMID:25758993 O00238 UniProtKB Natural variant 371 371 . . . ID=VAR_041405;Note=R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34970181,PMID:17344846 O00238 UniProtKB Natural variant 486 486 . . . ID=VAR_037967;Note=In brachydactyly type C and BDA2%3B with also additional features of symphalangism-1. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16957682;Dbxref=dbSNP:rs121434419,PMID:16957682 O00238 UniProtKB Natural variant 486 486 . . . ID=VAR_023820;Note=In BDA2%3B in animal models no effect on kinase activity but strongly decreased positive regulation of chondrocyte differentiation. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14523231;Dbxref=dbSNP:rs121434418,PMID:14523231 O00238 UniProtKB Helix 176 186 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Beta strand 190 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 194 197 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 200 203 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Beta strand 205 213 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Beta strand 216 223 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Beta strand 226 234 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 235 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 238 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Beta strand 261 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 270 272 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Beta strand 274 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 287 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 298 316 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Beta strand 337 340 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Beta strand 346 348 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 375 377 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 380 383 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 393 411 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Turn 426 430 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 437 444 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 455 459 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 461 473 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 478 480 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Helix 484 496 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY O00238 UniProtKB Turn 497 499 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MDY