##gff-version 3
P48168	UniProtKB	Signal peptide	1	22	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250	
P48168	UniProtKB	Chain	23	496	.	.	.	ID=PRO_0000000424;Note=Glycine receptor subunit beta	
P48168	UniProtKB	Topological domain	23	268	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Transmembrane	269	290	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Topological domain	291	295	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Transmembrane	296	316	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Topological domain	317	327	.	.	.	Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Transmembrane	328	348	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Topological domain	349	474	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Transmembrane	475	495	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Region	32	53	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P48168	UniProtKB	Compositional bias	37	53	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P48168	UniProtKB	Binding site	247	253	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O93430	
P48168	UniProtKB	Site	307	307	.	.	.	Note=Important for obstruction of the ion pore in the closed conformation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Modified residue	391	391	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P20781	
P48168	UniProtKB	Glycosylation	54	54	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P48168	UniProtKB	Glycosylation	242	242	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P48168	UniProtKB	Disulfide bond	183	197	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Disulfide bond	243	255	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P23415	
P48168	UniProtKB	Natural variant	74	83	.	.	.	Note=In spastic 1. NFKGIPVDVV->TTMLDIQPMI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7946325;Dbxref=PMID:7946325	
P48168	UniProtKB	Natural variant	84	496	.	.	.	Note=In spastic 1. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7946325;Dbxref=PMID:7946325	
P48168	UniProtKB	Natural variant	143	151	.	.	.	Note=In spastic 2. LFFANEKSA->VSMSWIYNR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7946325;Dbxref=PMID:7946325	
P48168	UniProtKB	Natural variant	152	496	.	.	.	Note=In spastic 2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7946325;Dbxref=PMID:7946325	
P48168	UniProtKB	Sequence conflict	365	365	.	.	.	Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305