##gff-version 3 P18507 UniProtKB Signal peptide 1 39 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 P18507 UniProtKB Chain 40 475 . . . ID=PRO_0000000477;Note=Gamma-aminobutyric acid receptor subunit gamma-2 P18507 UniProtKB Topological domain 40 273 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Transmembrane 274 296 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Transmembrane 300 322 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Transmembrane 334 356 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Topological domain 357 451 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Transmembrane 452 474 . . . Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Region 433 450 . . . Note=Interaction with GABARAP;Ontology_term=ECO:0000255;evidence=ECO:0000255 P18507 UniProtKB Glycosylation 52 52 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P18507 UniProtKB Glycosylation 129 129 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P18507 UniProtKB Glycosylation 247 247 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255 P18507 UniProtKB Disulfide bond 190 204 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P18507 UniProtKB Alternative sequence 211 211 . . . ID=VSP_061922;Note=In isoform 3. Y->WSRSIAQAGMCSGVISAHYSLRFWGSTDPPTLASRVAGISD;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Alternative sequence 377 384 . . . ID=VSP_061923;Note=In isoform 2. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Natural variant 79 79 . . . ID=VAR_065226;Note=Found in a patient with generalized tonic-clonic seizures. N->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20485450;Dbxref=dbSNP:rs112894280,PMID:20485450 P18507 UniProtKB Natural variant 82 82 . . . ID=VAR_014265;Note=In ECA2 and FEB8%3B abolishes in vitro sensitivity to diazepam. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11326275;Dbxref=dbSNP:rs121909673,PMID:11326275 P18507 UniProtKB Natural variant 83 83 . . . ID=VAR_071813;Note=Found in a patient with idiopathic generalized epilepsy%3B uncertain significance%3B the currents elicited by mutant receptors are indistinguishable from wild-type%3B no difference in sensitivity of the mutant receptors to the allosteric regulators zinc and benzodiazepine diazepam compared to wild-type. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21714819;Dbxref=dbSNP:rs587777365,PMID:21714819 P18507 UniProtKB Natural variant 106 106 . . . ID=VAR_082266;Note=In DEE74%3B does not affect protein abundance%3B decreases cell surface expression%3B decreases current amplitude in response to GABA%3B does not affect zinc sensitivity%3B accelerates activation and prolonges deactivation. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27864268;Dbxref=dbSNP:rs796052505,PMID:27864268 P18507 UniProtKB Natural variant 107 107 . . . ID=VAR_082267;Note=In DEE74%3B increases protein abundance%3B retained in the endoplasmic reticulum%3B decreases cell surface expression%3B decreases current amplitude in response to GABA%3B increases zinc sensitivity%3B accelerates activation and prolonges deactivation. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27864268;Dbxref=PMID:27864268 P18507 UniProtKB Natural variant 177 177 . . . ID=VAR_038602;Note=In FEB8. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16924025;Dbxref=dbSNP:rs267606837,PMID:16924025 P18507 UniProtKB Natural variant 274 274 . . . ID=VAR_078226;Note=Found in a patient with generalized epilepsy with myoclonic atonic seizures%2C cognitive impairment and behavioral disorder%3B likely pathogenic. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27864847;Dbxref=PMID:27864847 P18507 UniProtKB Natural variant 282 282 . . . ID=VAR_082268;Note=In DEE74%3B increases protein abundance%3B retained in the endoplasmic reticulum decreases%3B cell surface expression%3B decreases current amplitude in response to GABA%3B increases zinc sensitivity%3B accelerates activation and prolonges deactivation. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27864268;Dbxref=dbSNP:rs796052508,PMID:27864268 P18507 UniProtKB Natural variant 323 323 . . . ID=VAR_078620;Note=In GEFSP3 and DEE74%3B does not affect protein abundance%3B decreases cell surface expression%3B decreases current amplitude in response to GABA%3B increases zinc sensitivity%3B accelerates deactivation. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23708187,ECO:0000269|PubMed:27864268;Dbxref=dbSNP:rs397514737,PMID:23708187,PMID:27864268 P18507 UniProtKB Natural variant 323 323 . . . ID=VAR_082269;Note=In DEE74%3B does not affect protein abundance%3B decreases cell surface expression%3B decreases current amplitude in response to GABA%3B increases zinc sensitivity%3B accelerates deactivation. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27864268;Dbxref=dbSNP:rs796052510,PMID:27864268 P18507 UniProtKB Natural variant 328 328 . . . ID=VAR_014266;Note=In GEFSP3. K->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11326274;Dbxref=dbSNP:rs121909672,PMID:11326274 P18507 UniProtKB Natural variant 343 343 . . . ID=VAR_082270;Note=In DEE74%3B does not affect protein abundance%3B decreases cell surface expression%3B decreases current amplitude in response to GABA%3B does not affect zinc sensitivity%3B accelerates activation and prolonges deactivation. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27864268;Dbxref=dbSNP:rs796052511,dbSNP:rs1554100923,PMID:27864268 P18507 UniProtKB Natural variant 357 357 . . . ID=VAR_065163;Note=H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs17855003,PMID:15489334 P18507 UniProtKB Sequence conflict 120 120 . . . Note=T->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Sequence conflict 181 181 . . . Note=T->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Sequence conflict 392 393 . . . Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Sequence conflict 407 407 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Sequence conflict 446 447 . . . Note=IA->RI;Ontology_term=ECO:0000305;evidence=ECO:0000305 P18507 UniProtKB Helix 65 73 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Turn 74 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Turn 83 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 90 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Turn 106 109 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 110 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Helix 124 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 130 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6I53 P18507 UniProtKB Beta strand 134 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Helix 139 144 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 150 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 155 160 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 163 165 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 168 173 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 176 189 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Turn 195 198 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 201 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Turn 215 217 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 218 229 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 232 235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 238 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 257 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Helix 274 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Helix 292 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Helix 301 323 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Beta strand 324 326 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7QNE P18507 UniProtKB Helix 334 359 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T P18507 UniProtKB Helix 440 465 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6X3T