##gff-version 3 Q8K4J6 UniProtKB Chain 1 964 . . . ID=PRO_0000126626;Note=Myocardin-related transcription factor A Q8K4J6 UniProtKB Repeat 15 40 . . . Note=RPEL 1 Q8K4J6 UniProtKB Repeat 59 84 . . . Note=RPEL 2 Q8K4J6 UniProtKB Repeat 103 128 . . . Note=RPEL 3 Q8K4J6 UniProtKB Domain 385 419 . . . Note=SAP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00186 Q8K4J6 UniProtKB Region 1 291 . . . Note=Mediates interaction with SCAI and ACTB;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19350017;Dbxref=PMID:19350017 Q8K4J6 UniProtKB Region 41 58 . . . Note=Intervening spacer sequence 1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19008859;Dbxref=PMID:19008859 Q8K4J6 UniProtKB Region 85 102 . . . Note=Intervening spacer sequence 2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19008859;Dbxref=PMID:19008859 Q8K4J6 UniProtKB Region 145 292 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Region 328 371 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Region 484 508 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Region 638 673 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Region 706 779 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Region 796 849 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Coiled coil 552 600 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8K4J6 UniProtKB Compositional bias 145 198 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Compositional bias 340 371 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Compositional bias 722 749 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Compositional bias 764 779 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Compositional bias 816 843 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K4J6 UniProtKB Modified residue 41 41 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 159 159 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 191 191 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 349 349 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 351 351 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 352 352 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 355 355 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 358 358 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 360 360 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 371 371 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q969V6 Q8K4J6 UniProtKB Modified residue 423 423 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 484 484 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 485 485 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 487 487 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 488 488 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 492 492 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 494 494 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 496 496 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 520 520 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 530 530 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 544 544 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 548 548 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 605 605 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 606 606 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 651 651 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 687 687 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 718 718 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 724 724 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 728 728 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 810 810 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 822 822 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 826 826 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 840 840 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 842 842 . . . Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Modified residue 892 892 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27304076;Dbxref=PMID:27304076 Q8K4J6 UniProtKB Alternative sequence 1 35 . . . ID=VSP_007652;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:12397177,ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:16141072;Dbxref=PMID:12397177,PMID:15489334,PMID:16141072 Q8K4J6 UniProtKB Mutagenesis 24 24 . . . Note=In 123-1A: Reduced interaction with G-actin%2C leading to a constitutively active SRF-MRTFA complex%3B when associated with A-68 and A-112. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17588931;Dbxref=PMID:17588931 Q8K4J6 UniProtKB Mutagenesis 45 45 . . . Note=Induces a nuclear accumulation in unstimulated cells. F->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 48 48 . . . Note=Induces a nuclear accumulation in unstimulated cells. Q->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 52 52 . . . Note=Induces a nuclear accumulation in unstimulated cells. L->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 54 54 . . . Note=Impaired interaction with G-actin%2C leading to nuclear accumulation in unstimulated cells. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 56 56 . . . Note=Impaired interaction with G-actin%2C leading to nuclear accumulation in unstimulated cells. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 68 68 . . . Note=In 123-1A: Reduced interaction with G-actin%2C leading to a constitutively active SRF-MRTFA complex%3B when associated with A-24 and A-112. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17588931;Dbxref=PMID:17588931 Q8K4J6 UniProtKB Mutagenesis 89 89 . . . Note=Does not induce a nuclear accumulation in unstimulated cells. L->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 92 92 . . . Note=Does not induce a nuclear accumulation in unstimulated cells. K->A%2CD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 96 96 . . . Note=Induces a nuclear accumulation in unstimulated cells. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 96 96 . . . Note=Induces a nuclear decrease in unstimulated cells. L->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 98 98 . . . Note=Impaired interaction with G-actin%2C leading to cytoplasmic accumulation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 100 100 . . . Note=Impaired interaction with G-actin%2C leading to cytoplasmic accumulation. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21673315;Dbxref=PMID:21673315 Q8K4J6 UniProtKB Mutagenesis 112 112 . . . Note=In 123-1A: Reduced interaction with G-actin%2C leading to a constitutively active SRF-MRTFA complex%3B when associated with A-24 and A-68. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17588931;Dbxref=PMID:17588931 Q8K4J6 UniProtKB Sequence conflict 53 53 . . . Note=E->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8K4J6 UniProtKB Sequence conflict 724 724 . . . Note=S->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8K4J6 UniProtKB Sequence conflict 728 728 . . . Note=S->F;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8K4J6 UniProtKB Helix 15 23 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2V51 Q8K4J6 UniProtKB Helix 27 32 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2V51 Q8K4J6 UniProtKB Beta strand 39 41 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YJE Q8K4J6 UniProtKB Helix 59 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2V52 Q8K4J6 UniProtKB Helix 71 76 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2V52 Q8K4J6 UniProtKB Helix 87 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YJF Q8K4J6 UniProtKB Helix 115 120 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2YJF