##gff-version 3
Q0GNC1	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q27J81	
Q0GNC1	UniProtKB	Chain	2	1273	.	.	.	ID=PRO_0000259890;Note=Inverted formin-2	
Q0GNC1	UniProtKB	Domain	2	330	.	.	.	Note=GBD/FH3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00579	
Q0GNC1	UniProtKB	Domain	421	564	.	.	.	Note=FH1	
Q0GNC1	UniProtKB	Domain	589	979	.	.	.	Note=FH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00774	
Q0GNC1	UniProtKB	Domain	1007	1022	.	.	.	Note=WH2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00406	
Q0GNC1	UniProtKB	Region	1	30	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Region	346	387	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Region	427	559	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Region	960	999	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Region	1021	1273	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Coiled coil	907	984	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q0GNC1	UniProtKB	Compositional bias	1	22	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Compositional bias	356	387	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Compositional bias	1044	1063	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Compositional bias	1136	1151	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Compositional bias	1209	1237	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Compositional bias	1249	1267	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q0GNC1	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q27J81	
Q0GNC1	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q27J81	
Q0GNC1	UniProtKB	Modified residue	1172	1172	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19144319;Dbxref=PMID:19144319	
Q0GNC1	UniProtKB	Modified residue	1174	1174	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19144319;Dbxref=PMID:19144319	
Q0GNC1	UniProtKB	Modified residue	1203	1203	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q0GNC1	UniProtKB	Modified residue	1216	1216	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q27J81	
Q0GNC1	UniProtKB	Modified residue	1218	1218	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q27J81	
Q0GNC1	UniProtKB	Modified residue	1223	1223	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q0GNC1	UniProtKB	Modified residue	1230	1230	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q0GNC1	UniProtKB	Alternative sequence	1256	1273	.	.	.	ID=VSP_021560;Note=In isoform 2. EFVPDSDDIKAKRLCVIQ->GLRSRPKAK;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
Q0GNC1	UniProtKB	Mutagenesis	1009	1009	.	.	.	Note=Strongly inhibits depolymerization%3B when associated with A-1010 and A-1019. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16818491;Dbxref=PMID:16818491	
Q0GNC1	UniProtKB	Mutagenesis	1010	1010	.	.	.	Note=Strongly inhibits depolymerization%3B when associated with A-1009 and A-1019. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16818491;Dbxref=PMID:16818491	
Q0GNC1	UniProtKB	Mutagenesis	1019	1019	.	.	.	Note=Strongly inhibits depolymerization%3B when associated with A-1009 and A-1010. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16818491;Dbxref=PMID:16818491	
Q0GNC1	UniProtKB	Sequence conflict	1038	1038	.	.	.	Note=T->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
Q0GNC1	UniProtKB	Sequence conflict	1167	1167	.	.	.	Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305