##gff-version 3 P09493 UniProtKB Chain 1 284 . . . ID=PRO_0000205620;Note=Tropomyosin alpha-1 chain P09493 UniProtKB Region 1 38 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P09493 UniProtKB Region 116 136 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P09493 UniProtKB Coiled coil 1 284 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250 P09493 UniProtKB Modified residue 1 1 . . . Note=N-acetylmethionine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:3548719;Dbxref=PMID:3548719 P09493 UniProtKB Modified residue 45 45 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04692 P09493 UniProtKB Modified residue 174 174 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P09493 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P58771 P09493 UniProtKB Modified residue 206 206 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P58771 P09493 UniProtKB Modified residue 252 252 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P58771 P09493 UniProtKB Modified residue 261 261 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P04692 P09493 UniProtKB Modified residue 271 271 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P58771 P09493 UniProtKB Modified residue 283 283 . . . Note=Phosphoserine%3B by DAPK1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17895359;Dbxref=PMID:17895359 P09493 UniProtKB Alternative sequence 1 80 . . . ID=VSP_006576;Note=In isoform 2. MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD->MCRLRIFLRTASSEHLHERKLRET;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:3138425;Dbxref=PMID:3138425 P09493 UniProtKB Alternative sequence 1 80 . . . ID=VSP_017498;Note=In isoform 5. MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD->MAGSSSLEAVRRKIRSLQEQADAAEERAGTLQRELDHERKLRET;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P09493 UniProtKB Alternative sequence 41 80 . . . ID=VSP_036064;Note=In isoform 6 and isoform 7. DELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATD->EDIAAKEKLLRVSEDERDRVLEELHKAEDSLLAAEEAAAK;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15249230,ECO:0000303|PubMed:17974005;Dbxref=PMID:15249230,PMID:17974005 P09493 UniProtKB Alternative sequence 41 53 . . . ID=VSP_047297;Note=In isoform 8. DELVSLQKKLKGT->EDIAAKEKLLRVS;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09493 UniProtKB Alternative sequence 57 80 . . . ID=VSP_047298;Note=In isoform 8. LDKYSEALKDAQEKLELAEKKATD->RDRVLEELHKAEDSLLAAEEAAAK;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09493 UniProtKB Alternative sequence 189 212 . . . ID=VSP_006578;Note=In isoform 2. KCAELEEELKTVTNNLKSLEAQAE->QVRQLEEQLRIMDSDLESINAAED;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:3138425;Dbxref=PMID:3138425 P09493 UniProtKB Alternative sequence 189 212 . . . ID=VSP_006577;Note=In isoform 3 and isoform 4. KCAELEEELKTVTNNLKSLEAQAE->QVRQLEEQLRIMDQTLKALMAAED;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:3336357,ECO:0000303|PubMed:3336363;Dbxref=PMID:15489334,PMID:3336357,PMID:3336363 P09493 UniProtKB Alternative sequence 189 192 . . . ID=VSP_047299;Note=In isoform 8 and isoform 10. KCAE->QVRQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09493 UniProtKB Alternative sequence 196 212 . . . ID=VSP_047300;Note=In isoform 8 and isoform 10. ELKTVTNNLKSLEAQAE->QLRIMDQTLKALMAAED;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09493 UniProtKB Alternative sequence 258 284 . . . ID=VSP_006579;Note=In isoform 2%2C isoform 3%2C isoform 7%2C isoform 8 and isoform 9. DELYAQKLKYKAISEELDHALNDMTSI->EKVAHAKEENLSMHQMLDQTLLELNNM;Ontology_term=ECO:0000303,ECO:0000303,ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:17974005,ECO:0000303|PubMed:3138425,ECO:0000303|PubMed:3336357,ECO:0000303|PubMed:3336363;Dbxref=PMID:17974005,PMID:3138425,PMID:3336357,PMID:3336363 P09493 UniProtKB Alternative sequence 259 284 . . . ID=VSP_017499;Note=In isoform 5. ELYAQKLKYKAISEELDHALNDMTSI->QLYQQLEQNRRLTNELKLALNED;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P09493 UniProtKB Alternative sequence 284 284 . . . ID=VSP_047301;Note=In isoform 10. I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09493 UniProtKB Natural variant 40 40 . . . ID=VAR_043986;Note=In CMD1Y. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11273725;Dbxref=dbSNP:rs104894501,PMID:11273725 P09493 UniProtKB Natural variant 54 54 . . . ID=VAR_043987;Note=In CMD1Y. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11273725;Dbxref=dbSNP:rs104894505,PMID:11273725 P09493 UniProtKB Natural variant 63 63 . . . ID=VAR_013135;Note=In CMH3. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:8523464;Dbxref=dbSNP:rs199476306,PMID:8523464 P09493 UniProtKB Natural variant 175 175 . . . ID=VAR_007601;Note=In CMH3%3B no change in homodimerization%3B no change in homodimer thermal stability%3B decreased actin binding%3B recessive effect in the homodimer%3B increased calcium-dependent regulation of myosin binding to actin filaments%3B dominant effect in the homodimer. D->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23170982,ECO:0000269|PubMed:7898523,ECO:0000269|PubMed:8205619,ECO:0000269|PubMed:8523464,ECO:0000269|PubMed:9822100;Dbxref=dbSNP:rs104894503,PMID:23170982,PMID:7898523,PMID:8205619,PMID:8523464,PMID:9822100 P09493 UniProtKB Natural variant 180 180 . . . ID=VAR_007602;Note=In CMH3%3B no change in homodimerization%3B decreased in hom odimer thermal stability%3B decreased in actin binding%3B increased calcium-dependent regulation of myosin binding to actin filaments%3B dominant effect in the homodimer. E->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:23170982,ECO:0000269|PubMed:8205619;Dbxref=dbSNP:rs104894502,PMID:23170982,PMID:8205619 P09493 UniProtKB Natural variant 180 180 . . . ID=VAR_029452;Note=In CMH3. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12974739;Dbxref=dbSNP:rs104894502,PMID:12974739 P09493 UniProtKB Natural variant 192 192 . . . ID=VAR_070121;Note=In LVNC9. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21551322;Dbxref=dbSNP:rs199476315,PMID:21551322 P09493 UniProtKB Natural variant 248 248 . . . ID=VAR_070122;Note=In LVNC9. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21551322;Dbxref=dbSNP:rs199476319,PMID:21551322 P09493 UniProtKB Mutagenesis 15 15 . . . Note=Impairs interaction with LMOD2 and TMOD1. K->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26873245;Dbxref=PMID:26873245 P09493 UniProtKB Mutagenesis 283 283 . . . Note=Loss of phosphorylation and decreased formation of actin stress fibers. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17895359;Dbxref=PMID:17895359 P09493 UniProtKB Mutagenesis 283 283 . . . Note=Increased formation of actin stress fibers. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17895359;Dbxref=PMID:17895359 P09493 UniProtKB Sequence conflict 109 109 . . . Note=A->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09493 UniProtKB Sequence conflict 203 203 . . . Note=N->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P09493 UniProtKB Helix 1 28 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5KHT P09493 UniProtKB Helix 46 209 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8EFH P09493 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P09493 UniProtKB Modified residue 213 213 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09493 UniProtKB Modified residue 213 213 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09493 UniProtKB Modified residue 51 51 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P09493 UniProtKB Modified residue 213 213 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861 P09493 UniProtKB Modified residue 213 213 . . . Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861