##gff-version 3 O75899 UniProtKB Signal peptide 1 41 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Chain 42 941 . . . ID=PRO_0000012952;Note=Gamma-aminobutyric acid type B receptor subunit 2 O75899 UniProtKB Topological domain 42 483 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Transmembrane 484 504 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Topological domain 505 522 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Transmembrane 523 543 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Topological domain 544 551 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Transmembrane 552 572 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Topological domain 573 597 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Transmembrane 598 618 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Topological domain 619 654 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Transmembrane 655 675 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Topological domain 676 691 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Transmembrane 692 712 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Topological domain 713 720 . . . Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Transmembrane 721 741 . . . Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Topological domain 742 941 . . . Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Region 763 790 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite O75899 UniProtKB Coiled coil 781 819 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Modified residue 776 776 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Modified residue 779 779 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Modified residue 819 819 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Modified residue 884 884 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Modified residue 893 893 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Modified residue 913 913 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Modified residue 916 916 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Modified residue 920 920 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Modified residue 924 924 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q80T41 O75899 UniProtKB Glycosylation 90 90 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22660477;Dbxref=PMID:22660477 O75899 UniProtKB Glycosylation 298 298 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 O75899 UniProtKB Glycosylation 389 389 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22660477;Dbxref=PMID:22660477 O75899 UniProtKB Glycosylation 404 404 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22660477,ECO:0000269|PubMed:24305054;Dbxref=PMID:22660477,PMID:24305054 O75899 UniProtKB Glycosylation 453 453 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22660477;Dbxref=PMID:22660477 O75899 UniProtKB Disulfide bond 108 135 . . . . O75899 UniProtKB Disulfide bond 237 266 . . . . O75899 UniProtKB Disulfide bond 265 302 . . . . O75899 UniProtKB Natural variant 163 163 . . . ID=VAR_049280;Note=L->P;Dbxref=dbSNP:rs35449008 O75899 UniProtKB Natural variant 567 567 . . . ID=VAR_079029;Note=In NDPLHS%3B increased basal signaling activity and only weak stimulation by GABA agonist%3B when injected into Xenopus tadpoles%2C causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals%3B no effect on cell surface expression. A->T;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26740508,ECO:0000269|PubMed:28856709,ECO:0000269|PubMed:29369404;Dbxref=dbSNP:rs922847767,PMID:26740508,PMID:28856709,PMID:29369404 O75899 UniProtKB Natural variant 628 628 . . . ID=VAR_010148;Note=Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10328880;Dbxref=PMID:10328880 O75899 UniProtKB Natural variant 693 693 . . . ID=VAR_080569;Note=In DEE59%3B uncertain significance. G->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29100083;Dbxref=dbSNP:rs1554689320,PMID:29100083 O75899 UniProtKB Natural variant 695 695 . . . ID=VAR_080570;Note=In DEE59%3B full signaling activity in the absence of GABA agonist%3B when injected into Xenopus tadpoles%2C causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals%3B no effect on cell surface expression. S->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28856709,ECO:0000269|PubMed:29369404;Dbxref=dbSNP:rs1554689319,PMID:28856709,PMID:29369404 O75899 UniProtKB Natural variant 705 705 . . . ID=VAR_080571;Note=In DEE59%3B increased basal signaling activity and no stimulation by GABA agonist%3B when injected into Xenopus tadpoles%2C causes abnormal swimming patterns and increased frequencies of seizure-like behavior compared to wild-type-injected animals%3B no effect on cell surface expression. I->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:28856709,ECO:0000269|PubMed:29369404;Dbxref=dbSNP:rs1554689315,PMID:28856709,PMID:29369404 O75899 UniProtKB Natural variant 707 707 . . . ID=VAR_080572;Note=In NDPLHS%3B increased basal signaling activity and only weak stimulation by GABA agonist%3B no effect on cell surface expression. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29369404;Dbxref=dbSNP:rs1554689313,PMID:29369404 O75899 UniProtKB Natural variant 869 869 . . . ID=VAR_010149;Note=T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10328880;Dbxref=dbSNP:rs10985765,PMID:10328880 O75899 UniProtKB Mutagenesis 118 118 . . . Note=Impairs interaction with GABBR1. Decreases signaling via G-proteins. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22660477;Dbxref=PMID:22660477 O75899 UniProtKB Sequence conflict 6 6 . . . Note=S->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 O75899 UniProtKB Sequence conflict 12 12 . . . Note=P->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 O75899 UniProtKB Sequence conflict 424 424 . . . Note=G->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 O75899 UniProtKB Sequence conflict 797 797 . . . Note=R->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 O75899 UniProtKB Beta strand 55 62 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 66 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MQE O75899 UniProtKB Helix 71 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Turn 91 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 98 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 110 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 128 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 136 145 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 146 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 152 157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 161 164 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Turn 166 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 172 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 179 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 182 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 197 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 206 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Turn 220 223 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 225 234 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 237 245 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 250 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 257 269 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 274 276 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6WIV O75899 UniProtKB Beta strand 278 283 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Turn 287 290 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 304 311 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 315 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 335 345 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Turn 346 348 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MR7 O75899 UniProtKB Helix 355 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 378 387 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Helix 393 404 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 407 410 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 413 418 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 421 423 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 425 431 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 436 443 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Turn 444 447 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 448 451 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Turn 453 455 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 459 462 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4MS4 O75899 UniProtKB Beta strand 470 474 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7Q O75899 UniProtKB Helix 479 505 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Turn 506 508 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Helix 510 513 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Helix 517 538 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Beta strand 541 544 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Helix 546 550 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Helix 553 583 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Turn 596 598 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Helix 599 618 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Beta strand 622 627 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Beta strand 638 641 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Beta strand 644 649 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Helix 653 677 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Turn 680 682 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7Q O75899 UniProtKB Turn 684 686 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7Q O75899 UniProtKB Helix 690 712 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Turn 713 715 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7EB2 O75899 UniProtKB Helix 717 740 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Helix 742 748 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7C7S O75899 UniProtKB Helix 780 816 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4PAS O75899 UniProtKB Helix 885 890 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6M8R O75899 UniProtKB Helix 899 902 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6OCP O75899 UniProtKB Beta strand 908 911 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6M8R