##gff-version 3
Q5S006	UniProtKB	Chain	1	2527	.	.	.	ID=PRO_0000086239;Note=Leucine-rich repeat serine/threonine-protein kinase 2	
Q5S006	UniProtKB	Repeat	983	1004	.	.	.	Note=LRR 1	
Q5S006	UniProtKB	Repeat	1012	1033	.	.	.	Note=LRR 2	
Q5S006	UniProtKB	Repeat	1036	1057	.	.	.	Note=LRR 3	
Q5S006	UniProtKB	Repeat	1059	1080	.	.	.	Note=LRR 4	
Q5S006	UniProtKB	Repeat	1084	1105	.	.	.	Note=LRR 5	
Q5S006	UniProtKB	Repeat	1108	1129	.	.	.	Note=LRR 6	
Q5S006	UniProtKB	Repeat	1130	1151	.	.	.	Note=LRR 7	
Q5S006	UniProtKB	Repeat	1174	1195	.	.	.	Note=LRR 8	
Q5S006	UniProtKB	Repeat	1197	1218	.	.	.	Note=LRR 9	
Q5S006	UniProtKB	Repeat	1221	1242	.	.	.	Note=LRR 10	
Q5S006	UniProtKB	Repeat	1246	1267	.	.	.	Note=LRR 11	
Q5S006	UniProtKB	Repeat	1269	1291	.	.	.	Note=LRR 12	
Q5S006	UniProtKB	Domain	1328	1511	.	.	.	Note=Roc;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00758	
Q5S006	UniProtKB	Domain	1879	2146	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q5S006	UniProtKB	Repeat	2139	2183	.	.	.	Note=WD 1	
Q5S006	UniProtKB	Repeat	2188	2228	.	.	.	Note=WD 2	
Q5S006	UniProtKB	Repeat	2233	2276	.	.	.	Note=WD 3	
Q5S006	UniProtKB	Repeat	2281	2327	.	.	.	Note=WD 4	
Q5S006	UniProtKB	Repeat	2333	2377	.	.	.	Note=WD 5	
Q5S006	UniProtKB	Repeat	2402	2438	.	.	.	Note=WD 6	
Q5S006	UniProtKB	Repeat	2443	2497	.	.	.	Note=WD 7	
Q5S006	UniProtKB	Region	957	979	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5S006	UniProtKB	Coiled coil	9	33	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q5S006	UniProtKB	Compositional bias	958	979	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q5S006	UniProtKB	Active site	1994	1994	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
Q5S006	UniProtKB	Binding site	1341	1348	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00758	
Q5S006	UniProtKB	Binding site	1885	1893	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q5S006	UniProtKB	Binding site	1906	1906	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q5S006	UniProtKB	Binding site	2098	2121	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00758	
Q5S006	UniProtKB	Binding site	2295	2298	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00758	
Q5S006	UniProtKB	Modified residue	910	910	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5S007	
Q5S006	UniProtKB	Modified residue	935	935	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:26824392,ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079,PMID:26824392	
Q5S006	UniProtKB	Modified residue	955	955	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5S007	
Q5S006	UniProtKB	Modified residue	973	973	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5S007	
Q5S006	UniProtKB	Modified residue	1292	1292	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5S007	
Q5S006	UniProtKB	Modified residue	1444	1444	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5S007	
Q5S006	UniProtKB	Mutagenesis	1441	1441	.	.	.	Note=Impaired ability to recruit SEC61A and SEC31A to endoplasmic reticulum exit sites. Impaired ability to regulate ER to Golgi vesicle-mediated transport. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25201882;Dbxref=PMID:25201882	
Q5S006	UniProtKB	Mutagenesis	1441	1441	.	.	.	Note=Increases kinase activity. Reduces primary ciliogenesis. Causes fragmentation of the trans-Golgi network. R->G;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29125462,ECO:0000269|PubMed:29212815,ECO:0000269|PubMed:30398148;Dbxref=PMID:29125462,PMID:29212815,PMID:30398148	
Q5S006	UniProtKB	Mutagenesis	2016	2016	.	.	.	Note=Does not affect kinase activity and decreases sensitivity towards small molecule kinase inhibitors. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26824392;Dbxref=PMID:26824392	
Q5S006	UniProtKB	Mutagenesis	2019	2019	.	.	.	Note=Increases kinase activity. Causes loss of dopaminergic neurons in the substantia nigra of 20-month old mice due to increased phosphorylation of APP. Reduces primary ciliogenesis. G->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:26824392,ECO:0000269|PubMed:28720718,ECO:0000269|PubMed:29125462;Dbxref=PMID:26824392,PMID:28720718,PMID:29125462	
Q5S006	UniProtKB	Sequence conflict	343	343	.	.	.	Note=E->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q5S006	UniProtKB	Sequence conflict	777	777	.	.	.	Note=V->I;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q5S006	UniProtKB	Sequence conflict	863	863	.	.	.	Note=K->N;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q5S006	UniProtKB	Sequence conflict	925	925	.	.	.	Note=C->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q5S006	UniProtKB	Sequence conflict	1705	1707	.	.	.	Note=WSR->GQD;Ontology_term=ECO:0000305;evidence=ECO:0000305