##gff-version 3
P09327	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:2846586;Dbxref=PMID:2846586	
P09327	UniProtKB	Chain	2	827	.	.	.	ID=PRO_0000218727;Note=Villin-1	
P09327	UniProtKB	Repeat	27	76	.	.	.	Note=Gelsolin-like 1	
P09327	UniProtKB	Repeat	148	188	.	.	.	Note=Gelsolin-like 2	
P09327	UniProtKB	Repeat	265	309	.	.	.	Note=Gelsolin-like 3	
P09327	UniProtKB	Repeat	407	457	.	.	.	Note=Gelsolin-like 4	
P09327	UniProtKB	Repeat	528	568	.	.	.	Note=Gelsolin-like 5	
P09327	UniProtKB	Repeat	631	672	.	.	.	Note=Gelsolin-like 6	
P09327	UniProtKB	Domain	761	827	.	.	.	Note=HP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00595	
P09327	UniProtKB	Region	2	734	.	.	.	Note=Core	
P09327	UniProtKB	Region	2	126	.	.	.	Note=Necessary for homodimerization	
P09327	UniProtKB	Region	112	119	.	.	.	Note=LPA/PIP2-binding site 1	
P09327	UniProtKB	Region	138	146	.	.	.	Note=LPA/PIP2-binding site 2	
P09327	UniProtKB	Region	735	827	.	.	.	Note=Headpiece	
P09327	UniProtKB	Region	816	824	.	.	.	Note=LPA/PIP2-binding site 3	
P09327	UniProtKB	Modified residue	366	366	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
P09327	UniProtKB	Modified residue	735	735	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q62468	
P09327	UniProtKB	Alternative sequence	368	421	.	.	.	ID=VSP_054436;Note=In isoform 2. AKVEQVKFDATSMHVKPQVAAQQKMVDDGSGEVQVWRIENLELVPVDSKWLGHF->GEGQAGAVREPGSRSWARRATWSTTHPPSLTCIFNEDFYAGSGLVLADGDVDKL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
P09327	UniProtKB	Alternative sequence	422	827	.	.	.	ID=VSP_054437;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334	
P09327	UniProtKB	Natural variant	254	254	.	.	.	ID=VAR_054502;Note=K->R;Dbxref=dbSNP:rs35305540	
P09327	UniProtKB	Mutagenesis	25	25	.	.	.	Note=Inhibits activities regarding actin capping%2C actin severing and actin bundling. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15272027;Dbxref=PMID:15272027	
P09327	UniProtKB	Mutagenesis	44	44	.	.	.	Note=Inhibits activities regarding actin capping and actin severing. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15272027;Dbxref=PMID:15272027	
P09327	UniProtKB	Mutagenesis	46	46	.	.	.	Note=Reduces activities regarding actin capping and actin severing. Does not reduce lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-60%3B F-81%3B F-256%3B F-286%3B F-324%3B F-461%3B F-555%3B F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1%3B when associated with F-60%3B F-81 and F-256. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12269817,ECO:0000269|PubMed:15342783,ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:12269817,PMID:15342783,PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	60	60	.	.	.	Note=Reduces activities regarding actin capping and actin severing%2C lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-81%3B F-256%3B F-286%3B F-324%3B F-461%3B F-555%3B F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1%3B when associated with F-46%3B F-81 and F-256. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12269817,ECO:0000269|PubMed:15342783,ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:12269817,PMID:15342783,PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	61	61	.	.	.	Note=Inhibits actin-severing activity. Does not inhibit actin-nucleation and actin-capping activities. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15272027,ECO:0000269|PubMed:17182858;Dbxref=PMID:15272027,PMID:17182858	
P09327	UniProtKB	Mutagenesis	74	74	.	.	.	Note=Inhibits activities regarding actin capping and actin severing. E->L;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15272027,ECO:0000269|PubMed:17182858;Dbxref=PMID:15272027,PMID:17182858	
P09327	UniProtKB	Mutagenesis	81	81	.	.	.	Note=Reduces activities regarding actin nucleating and actin severing%2C lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-60%3B F-256%3B F-286%3B F-324%3B F-461%3B F-555%3B F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1%3B when associated with F-46%3B F-60 and F-256. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12269817,ECO:0000269|PubMed:15342783,ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:12269817,PMID:15342783,PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	86	91	.	.	.	Note=Inhibits actin-severing activity and motility of the S.flexneri%2C does not inhibit activities regarding actin nucleation%2C actin capping and actin bundling%2C lamellipodium or ruffle localization and cell morphology%3B when associated with 125-A--S-129. DDFLKG->NTLLKE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182858;Dbxref=PMID:17182858	
P09327	UniProtKB	Mutagenesis	86	86	.	.	.	Note=Inhibits actin-severing activity. Does not inhibit actin-capping activity. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15272027;Dbxref=PMID:15272027	
P09327	UniProtKB	Mutagenesis	93	93	.	.	.	Note=Inhibits actin-severing activity. Does not inhibit actin-capping activity. A->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15272027;Dbxref=PMID:15272027	
P09327	UniProtKB	Mutagenesis	125	129	.	.	.	Note=Inhibits actin-severing activity and motility of the S.flexneri%2C does not inhibit activities regarding actin nucleation%2C actin capping and actin bundling%2C lamellipodium or ruffle localization and cell morphology%3B when associated with 86-N--E-91. GMKHV->AMHKTS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17182858;Dbxref=PMID:17182858	
P09327	UniProtKB	Mutagenesis	138	138	.	.	.	Note=Reduces binding to PIP2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14594952;Dbxref=PMID:14594952	
P09327	UniProtKB	Mutagenesis	145	145	.	.	.	Note=Does not reduce binding to PIP2. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14594952;Dbxref=PMID:14594952	
P09327	UniProtKB	Mutagenesis	146	146	.	.	.	Note=Does not reduce binding to PIP2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14594952;Dbxref=PMID:14594952	
P09327	UniProtKB	Mutagenesis	256	256	.	.	.	Note=Reduces activities regarding actin nucleation and actin severing%2C lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-60%3B F-81%3B F-286%3B F-324%3B F-461%3B F-555%3B F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1%3B when associated with F-46%3B F-60 and F-81. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12269817,ECO:0000269|PubMed:15342783,ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:12269817,PMID:15342783,PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	286	286	.	.	.	Note=Reduces actin-severing activity and interaction with PLCG1. Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-60%3B F-81%3B F-256%3B F-324%3B F-461%3B F-555%3B F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization%3B when associated with F-324%3B F-461%3B F-555%3B F-604 and F-725. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	324	324	.	.	.	Note=Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-60%3B F-81%3B F-256%3B F-286%3B F-461%3B F-555%3B F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization%3B when associated with F-286%3B F-461%3B F-555%3B F-604 and F-725. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	461	461	.	.	.	Note=Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-60%3B F-81%3B F-256%3B F-286%3B F-324%3B F-555%3B F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization%3B when associated with F-286%3B F-324%3B F-555%3B F-604 and F-725. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	467	467	.	.	.	Note=Reduces the Ca(2+)-dependent actin-severing activity. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15084600;Dbxref=PMID:15084600	
P09327	UniProtKB	Mutagenesis	555	555	.	.	.	Note=Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-60%3B F-81%3B F-256%3B F-286%3B F-324%3B F-461%3B F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization%3B when associated with F-286%3B F-324%3B F-461%3B F-604 and F-725. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	604	604	.	.	.	Note=Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-60%3B F-81%3B F-256%3B F-286%3B F-324%3B F-461%3B F-555 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization%3B when associated with F-286%3B F-324%3B F-461%3B F-555 and F-725. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	715	715	.	.	.	Note=Reduces the Ca(2+)-dependent actin-severing activity. D->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15084600;Dbxref=PMID:15084600	
P09327	UniProtKB	Mutagenesis	725	725	.	.	.	Note=Complete loss of phosphorylation and interaction with PLCG1%2C does not reduce lamellipodium or ruffle localization%2C inhibits cell migration%3B when associated with F-46%3B F-60%3B F-81%3B F-256%3B F-286%3B F-324%3B F-461%3B F-555 and F-604. Inhibits interaction with PLCG1 and lamellipodia localization%3B when associated with F-286%3B F-324%3B F-461%3B F-555 and F-604. Y->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16921170,ECO:0000269|PubMed:17229814,ECO:0000269|PubMed:18054784;Dbxref=PMID:16921170,PMID:17229814,PMID:18054784	
P09327	UniProtKB	Mutagenesis	815	815	.	.	.	Note=Reduces interaction with F-actin. W->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15096633;Dbxref=PMID:15096633	
P09327	UniProtKB	Mutagenesis	822	822	.	.	.	Note=Does not reduce binding to PIP2. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14594952;Dbxref=PMID:14594952	
P09327	UniProtKB	Mutagenesis	824	824	.	.	.	Note=Does not reduce binding to PIP2. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14594952;Dbxref=PMID:14594952	
P09327	UniProtKB	Sequence conflict	146	146	.	.	.	Note=R->K;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P09327	UniProtKB	Sequence conflict	732	732	.	.	.	Note=L->S;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P09327	UniProtKB	Sequence conflict	735	735	.	.	.	Note=S->L;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P09327	UniProtKB	Beta strand	620	625	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Beta strand	632	635	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Helix	641	643	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Beta strand	648	653	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Beta strand	658	662	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Helix	668	684	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Beta strand	685	688	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Beta strand	695	699	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Helix	705	708	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3FG7	
P09327	UniProtKB	Helix	795	800	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNC	
P09327	UniProtKB	Helix	806	811	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNC	
P09327	UniProtKB	Helix	814	823	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNC