##gff-version 3
P70460	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50552	
P70460	UniProtKB	Chain	2	375	.	.	.	ID=PRO_0000065768;Note=Vasodilator-stimulated phosphoprotein	
P70460	UniProtKB	Domain	2	113	.	.	.	Note=WH1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00410	
P70460	UniProtKB	Repeat	340	354	.	.	.	Note=1	
P70460	UniProtKB	Repeat	355	369	.	.	.	Note=2	
P70460	UniProtKB	Region	111	340	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P70460	UniProtKB	Region	221	373	.	.	.	Note=EVH2	
P70460	UniProtKB	Region	221	241	.	.	.	Note=EVH2 block A	
P70460	UniProtKB	Region	257	274	.	.	.	Note=EVH2 block B	
P70460	UniProtKB	Region	338	372	.	.	.	Note=EVH2 block C	
P70460	UniProtKB	Region	339	368	.	.	.	Note=2 X 15 AA tandem repeats of L-[EQ]-[KR] [MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-E	
P70460	UniProtKB	Coiled coil	337	367	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
P70460	UniProtKB	Motif	230	233	.	.	.	Note=KLKR	
P70460	UniProtKB	Compositional bias	159	186	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P70460	UniProtKB	Compositional bias	265	290	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P70460	UniProtKB	Compositional bias	310	333	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
P70460	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50552	
P70460	UniProtKB	Modified residue	39	39	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50552	
P70460	UniProtKB	Modified residue	46	46	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50552	
P70460	UniProtKB	Modified residue	153	153	.	.	.	Note=Phosphoserine%3B by PKA%2C PKC%2C PKG/PRKG1 and ROCK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882740;Dbxref=PMID:10882740	
P70460	UniProtKB	Modified residue	235	235	.	.	.	Note=Phosphoserine%3B by PKA and PKG;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10882740,ECO:0007744|PubMed:21183079;Dbxref=PMID:10882740,PMID:21183079	
P70460	UniProtKB	Modified residue	274	274	.	.	.	Note=Phosphothreonine%3B by PKA%2C PKG/PRKG1 and AMPK;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50552	
P70460	UniProtKB	Modified residue	279	279	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50552	
P70460	UniProtKB	Modified residue	309	309	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50552	
P70460	UniProtKB	Modified residue	311	311	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50552	
P70460	UniProtKB	Modified residue	317	317	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P70460	UniProtKB	Modified residue	318	318	.	.	.	Note=Phosphoserine%3B by AMPK;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21945940;Dbxref=PMID:21945940	
P70460	UniProtKB	Modified residue	320	320	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
P70460	UniProtKB	Natural variant	209	209	.	.	.	Note=A->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16141072,ECO:0000269|PubMed:8812448;Dbxref=PMID:16141072,PMID:8812448	
P70460	UniProtKB	Mutagenesis	153	153	.	.	.	Note=Reduces actin polymerization to a lesser extent than wild-type. Greater effect on actin polymerization%3B when associated with D-235 and E-274. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882740;Dbxref=PMID:10882740	
P70460	UniProtKB	Mutagenesis	232	233	.	.	.	Note=Reduced binding to monomeric actin. No VASP-induced actin polymerization. RK->GE%2CEE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12372613;Dbxref=PMID:12372613	
P70460	UniProtKB	Mutagenesis	235	235	.	.	.	Note=Reduces actin polymerization to a lesser extent than wild-type. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882740;Dbxref=PMID:10882740	
P70460	UniProtKB	Mutagenesis	274	274	.	.	.	Note=Reduces actin polymerization to a lesser extent than wild-type. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10882740;Dbxref=PMID:10882740	
P70460	UniProtKB	Sequence conflict	106	115	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P70460	UniProtKB	Sequence conflict	237	237	.	.	.	Note=Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P70460	UniProtKB	Sequence conflict	337	337	.	.	.	Note=S->Y;Ontology_term=ECO:0000305;evidence=ECO:0000305