##gff-version 3
Q92819	UniProtKB	Chain	1	552	.	.	.	ID=PRO_0000197173;Note=Hyaluronan synthase 2	
Q92819	UniProtKB	Topological domain	1	11	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Transmembrane	12	32	.	.	.	Note=Helical%3B Name%3D1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Topological domain	33	45	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Transmembrane	46	66	.	.	.	Note=Helical%3B Name%3D2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Topological domain	67	374	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Transmembrane	375	395	.	.	.	Note=Helical%3B Name%3D3;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Topological domain	396	402	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Transmembrane	403	423	.	.	.	Note=Helical%3B Name%3D4;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Topological domain	424	429	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Transmembrane	430	450	.	.	.	Note=Helical%3B Name%3D5;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Topological domain	451	475	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Transmembrane	476	496	.	.	.	Note=Helical%3B Name%3D6;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Topological domain	497	510	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Transmembrane	511	531	.	.	.	Note=Helical%3B Name%3D7;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Topological domain	532	552	.	.	.	Note=Extracellular;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q92819	UniProtKB	Modified residue	110	110	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21228273;Dbxref=PMID:21228273	
Q92819	UniProtKB	Modified residue	328	328	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32993960;Dbxref=PMID:32993960	
Q92819	UniProtKB	Glycosylation	221	221	.	.	.	Note=O-linked (GlcNAc) serine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22887999;Dbxref=PMID:22887999	
Q92819	UniProtKB	Cross-link	190	190	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20507985;Dbxref=PMID:20507985	
Q92819	UniProtKB	Mutagenesis	110	110	.	.	.	Note=Completely abolishes hyaluronan synthase activity. Not detected in cytoplasmic vesicles nor at cell membrane. Inability to travel from ER to Golgi. Unresponsive to AMPK-mediated inactivation. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21228273,ECO:0000269|PubMed:30394292;Dbxref=PMID:21228273,PMID:30394292	
Q92819	UniProtKB	Mutagenesis	190	190	.	.	.	Note=Completely abolishes hyaluronan synthase activity. Cumulates at plasma membrane. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20507985,ECO:0000269|PubMed:30394292;Dbxref=PMID:20507985,PMID:30394292	
Q92819	UniProtKB	Mutagenesis	221	221	.	.	.	Note=Prevents O-GlcNAcylation. Increases protein stability. Reduces hyaluronan synthase activity. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:22887999,ECO:0000269|PubMed:30394292;Dbxref=PMID:22887999,PMID:30394292	
Q92819	UniProtKB	Mutagenesis	221	221	.	.	.	Note=Increases protein degradation. Abolishes hyaluronan synthase activity. Does not affect subcellular location. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30394292;Dbxref=PMID:30394292	
Q92819	UniProtKB	Mutagenesis	221	221	.	.	.	Note=Increases protein degradation. Abolishes hyaluronan synthase activity. Does not affect subcellular location. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30394292;Dbxref=PMID:30394292	
Q92819	UniProtKB	Mutagenesis	328	328	.	.	.	Note=Abolishes hyaluronan synthase activity. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32993960;Dbxref=PMID:32993960