##gff-version 3
Q08873	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
Q08873	UniProtKB	Chain	2	200	.	.	.	ID=PRO_0000204795;Note=Transgelin	
Q08873	UniProtKB	Domain	26	136	.	.	.	Note=Calponin-homology (CH);Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00044	
Q08873	UniProtKB	Region	144	168	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q08873	UniProtKB	Region	151	164	.	.	.	Note=Interaction with SH3 domain of ABP1	
Q08873	UniProtKB	Modified residue	2	2	.	.	.	Note=N-acetylserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
Q08873	UniProtKB	Modified residue	11	11	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17330950,ECO:0007744|PubMed:19779198;Dbxref=PMID:17330950,PMID:19779198	
Q08873	UniProtKB	Mutagenesis	185	185	.	.	.	Note=Greatly reduces actin-binding and actin-bundling activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857851;Dbxref=PMID:12857851	
Q08873	UniProtKB	Mutagenesis	185	185	.	.	.	Note=Moderately reduces actin-binding and actin-bundling activity. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12857851;Dbxref=PMID:12857851