##gff-version 3
P51667	UniProtKB	Initiator methionine	1	1	.	.	.	Note=Removed;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20668449;Dbxref=PMID:20668449	
P51667	UniProtKB	Chain	2	166	.	.	.	ID=PRO_0000198728;Note=Myosin regulatory light chain 2%2C ventricular/cardiac muscle isoform	
P51667	UniProtKB	Domain	24	59	.	.	.	Note=EF-hand 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
P51667	UniProtKB	Domain	94	129	.	.	.	Note=EF-hand 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
P51667	UniProtKB	Domain	130	165	.	.	.	Note=EF-hand 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
P51667	UniProtKB	Binding site	37	37	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
P51667	UniProtKB	Binding site	39	39	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
P51667	UniProtKB	Binding site	41	41	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
P51667	UniProtKB	Binding site	48	48	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448	
P51667	UniProtKB	Modified residue	2	2	.	.	.	Note=N%2CN%2CN-trimethylalanine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20668449;Dbxref=PMID:20668449	
P51667	UniProtKB	Modified residue	14	14	.	.	.	Note=Phosphoserine%3B by MLCK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20445002,ECO:0000269|PubMed:22426213,ECO:0007744|PubMed:21183079;Dbxref=PMID:20445002,PMID:21183079,PMID:22426213	
P51667	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine%3B by MLCK;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:20445002,ECO:0000269|PubMed:22426213,ECO:0007744|PubMed:21183079;Dbxref=PMID:20445002,PMID:21183079,PMID:22426213	
P51667	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22426213,ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079,PMID:22426213	
P51667	UniProtKB	Modified residue	52	52	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P08733	
P51667	UniProtKB	Mutagenesis	14	14	.	.	.	Note=Loss of cardiac myofibril assembly%3B when associated with A-15 and A-19. Loss of phosphorylation%3B when associated with A-15 and A-19. Loss of calcium sensitivity of force development%3B when associated with A-15 and A-19. Phosphorylation at Ser-19%3B when associated with A-15. Significant decrease in phosphorylation by MLCK%3B when associated with A-15. Adult lethality associated with early defects in cardiac twitch relaxation and torsion leading to dilated cardiomyopathy%2C heart failure and premature death%3B when associated with A-15.Significant acceleration of twitch relaxation in absence of changes in calcium transients%3B when associated with A-15. Absence of transmural phosphorylation gradient leading to alteration of torsion%3B when associated with A-14. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10409661,ECO:0000269|PubMed:22426213;Dbxref=PMID:10409661,PMID:22426213	
P51667	UniProtKB	Mutagenesis	15	15	.	.	.	Note=Loss of cardiac myofibril assembly%3B when associated with A-14 and A-19. Loss of phosphorylation%3B when associated with A-14 and A-19. Loss of calcium sensitivity of force development%3B when associated with A-14 and A-19. Increase of phosphorylation. Phosphorylation at Ser-14 and at Ser-19. Phosphorylation at Ser-19%3B when associated with A-14. Significant decrease in phosphorylation by MLCK%3B when associated with A-14. Adult lethality associated with early defects in cardiac twitch relaxation and torsion leading to dilated cardiomyopathy%2C heart failure and premature death%3B when associated with A-14. Significant acceleration of twitch relaxation in absence of changes in calcium transients%3B when associated with A-14. Absence of transmural phosphorylation gradient leading to alteration of torsion%3B when associated with A-14. S->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10409661,ECO:0000269|PubMed:22426213;Dbxref=PMID:10409661,PMID:22426213	
P51667	UniProtKB	Mutagenesis	19	19	.	.	.	Note=Loss of cardiac myofibril assembly%3B when associated with A-14 and A-15. Loss of phosphorylation%3B when associated with A-14 and A-15. Loss of calcium sensitivity of force development%3B when associated with A-14 and A-15. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10409661;Dbxref=PMID:10409661	
P51667	UniProtKB	Sequence conflict	4	5	.	.	.	Note=KK->LF;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P51667	UniProtKB	Sequence conflict	14	14	.	.	.	Note=S->T;Ontology_term=ECO:0000305;evidence=ECO:0000305	
P51667	UniProtKB	Sequence conflict	128	128	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305