##gff-version 3
P29465	UniProtKB	Chain	1	1165	.	.	.	ID=PRO_0000193729;Note=Chitin synthase 3	
P29465	UniProtKB	Topological domain	1	170	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Transmembrane	171	191	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29465	UniProtKB	Topological domain	192	340	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Transmembrane	341	354	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Topological domain	355	452	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Transmembrane	453	473	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29465	UniProtKB	Topological domain	474	891	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Transmembrane	892	910	.	.	.	Note=Helical;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Topological domain	911	1029	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Transmembrane	1030	1050	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29465	UniProtKB	Topological domain	1051	1055	.	.	.	Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Transmembrane	1056	1076	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
P29465	UniProtKB	Topological domain	1077	1165	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:28346351;Dbxref=PMID:28346351	
P29465	UniProtKB	Region	19	53	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P29465	UniProtKB	Region	74	97	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P29465	UniProtKB	Modified residue	537	537	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17330950;Dbxref=PMID:17330950	
P29465	UniProtKB	Modified residue	538	538	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:17330950;Dbxref=PMID:17330950	
P29465	UniProtKB	Glycosylation	303	303	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
P29465	UniProtKB	Glycosylation	332	332	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00498	
P29465	UniProtKB	Cross-link	136	136	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12872131;Dbxref=PMID:12872131	
P29465	UniProtKB	Mutagenesis	991	991	.	.	.	Note=Reduces catalytic activity by 67%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
P29465	UniProtKB	Mutagenesis	993	993	.	.	.	Note=Reduces catalytic activity by 89%25. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
P29465	UniProtKB	Mutagenesis	994	994	.	.	.	Note=Completely abolishes catalytic activity. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
P29465	UniProtKB	Mutagenesis	995	995	.	.	.	Note=Reduces catalytic activity by 87%25. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
P29465	UniProtKB	Mutagenesis	999	999	.	.	.	Note=Reduces catalytic activity by 59%25. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760183;Dbxref=PMID:9760183	
P29465	UniProtKB	Sequence conflict	1163	1163	.	.	.	Note=F->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P29465	UniProtKB	Helix	13	23	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4WJW