##gff-version 3
P22300	UniProtKB	Signal peptide	1	39	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22300	UniProtKB	Chain	40	475	.	.	.	ID=PRO_0000000476;Note=Gamma-aminobutyric acid receptor subunit gamma-2	
P22300	UniProtKB	Topological domain	40	273	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P22300	UniProtKB	Transmembrane	274	296	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P22300	UniProtKB	Transmembrane	300	322	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P22300	UniProtKB	Transmembrane	334	356	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P22300	UniProtKB	Topological domain	357	451	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P22300	UniProtKB	Transmembrane	452	475	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P22300	UniProtKB	Modified residue	382	382	.	.	.	Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P22300	UniProtKB	Glycosylation	52	52	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22300	UniProtKB	Glycosylation	129	129	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22300	UniProtKB	Glycosylation	247	247	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P22300	UniProtKB	Disulfide bond	190	204	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P22300	UniProtKB	Alternative sequence	377	384	.	.	.	ID=VSP_000090;Note=In isoform 2S. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:1702226;Dbxref=PMID:1702226	
P22300	UniProtKB	Natural variant	230	230	.	.	.	Note=S->G