##gff-version 3
Q96G97	UniProtKB	Chain	1	398	.	.	.	ID=PRO_0000191679;Note=Seipin	
Q96G97	UniProtKB	Topological domain	1	26	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q96G97	UniProtKB	Transmembrane	27	47	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q96G97	UniProtKB	Topological domain	48	242	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q96G97	UniProtKB	Transmembrane	243	263	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q96G97	UniProtKB	Topological domain	264	398	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q96G97	UniProtKB	Region	281	398	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q96G97	UniProtKB	Compositional bias	322	336	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q96G97	UniProtKB	Modified residue	289	289	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
Q96G97	UniProtKB	Modified residue	346	346	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5FVJ6	
Q96G97	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q5FVJ6	
Q96G97	UniProtKB	Modified residue	372	372	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
Q96G97	UniProtKB	Glycosylation	88	88	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14981520;Dbxref=PMID:14981520	
Q96G97	UniProtKB	Glycosylation	242	242	.	.	.	Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q96G97	UniProtKB	Alternative sequence	1	1	.	.	.	ID=VSP_044545;Note=In isoform 3. M->MSTEKVDQKEEAGEKEVCGDQIKGPDKEEEPPAAASHGQGWRPGGRAARNARPEPGARHPALPAM;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q96G97	UniProtKB	Alternative sequence	225	287	.	.	.	ID=VSP_051726;Note=In isoform 2. YLLYNFPMTCAFIGVASNFTFLSVIVLFSYMQWVWGGIWPRHRFSLQVNIRKRDNSRKEVQRR->LTSEKETIPGRKSNEGSLLISQGLKARRSQLRNQMLQRMVRALKIPQGQRVSCPRRRNQISSP;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q96G97	UniProtKB	Alternative sequence	288	398	.	.	.	ID=VSP_051727;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039	
Q96G97	UniProtKB	Natural variant	88	88	.	.	.	ID=VAR_022375;Note=In SPG17 and HMND13%3B does not affect protein subcellular location. N->S;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14981520,ECO:0000269|PubMed:17663003,ECO:0000269|PubMed:18585921;Dbxref=dbSNP:rs137852972,PMID:14981520,PMID:17663003,PMID:18585921	
Q96G97	UniProtKB	Natural variant	90	90	.	.	.	ID=VAR_022376;Note=In SPG17 and HMND13%3B also found in patients with hereditary motor and sensory neuropathy type 2%3B does not affect the function in lipid storage. S->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14981520,ECO:0000269|PubMed:17663003,ECO:0000269|PubMed:21533227,ECO:0000269|PubMed:24604904;Dbxref=dbSNP:rs137852973,PMID:14981520,PMID:17663003,PMID:21533227,PMID:24604904	
Q96G97	UniProtKB	Natural variant	212	212	.	.	.	ID=VAR_022377;Note=In CGL2%3B increases localization to nuclear envelope%3B no effect on its interaction with LDAF1%3B no rescue of aberrant lipid droplet formation in BSCL2-knockdown cells. A->P;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11479539,ECO:0000269|PubMed:27879284,ECO:0000269|PubMed:30901948;Dbxref=dbSNP:rs137852971,PMID:11479539,PMID:27879284,PMID:30901948	
Q96G97	UniProtKB	Mutagenesis	67	67	.	.	.	Note=Loss of oligomerization and function in lipid droplet formation%3B when associated with A-70%3B A-151%3B D-156%3B D-169 and A-175. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30293840;Dbxref=PMID:30293840	
Q96G97	UniProtKB	Mutagenesis	70	70	.	.	.	Note=Loss of oligomerization and function in lipid droplet formation%3B when associated with R-67%3B A-151%3B D-156%3B D-169 and A-175. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30293840;Dbxref=PMID:30293840	
Q96G97	UniProtKB	Mutagenesis	151	151	.	.	.	Note=Loss of oligomerization and function in lipid droplet biogenesis%3B when associated with R-67%3B A-70%3B D-156%3B D-169 and A-175. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30293840;Dbxref=PMID:30293840	
Q96G97	UniProtKB	Mutagenesis	156	156	.	.	.	Note=Loss of oligomerization and function in lipid droplet formation%3B when associated with R-67%3B A-70%3B A-151%3B D-169 and A-175. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30293840;Dbxref=PMID:30293840	
Q96G97	UniProtKB	Mutagenesis	169	169	.	.	.	Note=Loss of oligomerization and function in lipid droplet formation%3B when associated with R-67%3B A-70%3B A-151%3B D-156 and A-175. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30293840;Dbxref=PMID:30293840	
Q96G97	UniProtKB	Mutagenesis	175	175	.	.	.	Note=Loss of oligomerization and function in lipid droplet formation%3B when associated with R-67%3B A-70%3B A-151%3B D-156 and D-169. Q->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30293840;Dbxref=PMID:30293840