##gff-version 3 E9PZQ0 UniProtKB Chain 1 5035 . . . ID=PRO_0000415566;Note=Ryanodine receptor 1 E9PZQ0 UniProtKB Topological domain 1 4556 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Transmembrane 4557 4577 . . . Note=Helical%3B Name%3D1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Topological domain 4578 4638 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Transmembrane 4639 4659 . . . Note=Helical%3B Name%3D2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Topological domain 4660 4777 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Transmembrane 4778 4800 . . . Note=Helical%3B Name%3D3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Topological domain 4801 4801 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Transmembrane 4802 4818 . . . Note=Helical%3B Name%3D4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Topological domain 4819 4833 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Transmembrane 4834 4854 . . . Note=Helical%3B Name%3D5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Topological domain 4855 4877 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Intramembrane 4878 4897 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Topological domain 4898 4917 . . . Note=Lumenal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Transmembrane 4918 4938 . . . Note=Helical%3B Name%3D6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Topological domain 4939 5035 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Domain 99 154 . . . Note=MIR 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 E9PZQ0 UniProtKB Domain 161 206 . . . Note=MIR 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 E9PZQ0 UniProtKB Domain 212 266 . . . Note=MIR 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 E9PZQ0 UniProtKB Domain 272 329 . . . Note=MIR 4;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 E9PZQ0 UniProtKB Domain 337 394 . . . Note=MIR 5;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00131 E9PZQ0 UniProtKB Domain 583 799 . . . Note=B30.2/SPRY 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548 E9PZQ0 UniProtKB Repeat 843 956 . . . Note=1 E9PZQ0 UniProtKB Repeat 957 1070 . . . Note=2 E9PZQ0 UniProtKB Domain 1015 1210 . . . Note=B30.2/SPRY 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548 E9PZQ0 UniProtKB Repeat 1346 1361 . . . Note=3%3B truncated E9PZQ0 UniProtKB Domain 1359 1572 . . . Note=B30.2/SPRY 3;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548 E9PZQ0 UniProtKB Repeat 1374 1389 . . . Note=4%3B truncated E9PZQ0 UniProtKB Repeat 2727 2846 . . . Note=5 E9PZQ0 UniProtKB Repeat 2847 2960 . . . Note=6 E9PZQ0 UniProtKB Domain 4078 4106 . . . Note=EF-hand;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00448 E9PZQ0 UniProtKB Region 671 682 . . . Note=Interaction with FKBP1A;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Region 843 2960 . . . Note=6 X approximate repeats E9PZQ0 UniProtKB Region 1309 1387 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Region 1873 1928 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Region 2391 2414 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Region 2828 2859 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Region 3479 3502 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Region 3615 3644 . . . Note=Interaction with CALM;Ontology_term=ECO:0000250;evidence=ECO:0000250 E9PZQ0 UniProtKB Region 4255 4283 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Region 4378 4531 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Region 4586 4618 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Motif 4892 4898 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Compositional bias 1372 1387 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Compositional bias 1874 1923 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Compositional bias 2828 2844 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Compositional bias 4257 4274 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Compositional bias 4402 4418 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Compositional bias 4482 4496 . . . Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Compositional bias 4497 4513 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Compositional bias 4514 4528 . . . Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite E9PZQ0 UniProtKB Binding site 3896 3896 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Binding site 3970 3970 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Binding site 4214 4218 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Binding site 4714 4714 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Binding site 4952 4957 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Binding site 4977 4983 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Binding site 4999 4999 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Modified residue 1339 1339 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:F1LMY4 E9PZQ0 UniProtKB Modified residue 2346 2346 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:F1LMY4 E9PZQ0 UniProtKB Modified residue 2844 2844 . . . Note=Phosphoserine%3B by PKA and PKG;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:18268335,ECO:0000269|PubMed:21156754,ECO:0007744|PubMed:21183079;Dbxref=PMID:18268335,PMID:21156754,PMID:21183079 E9PZQ0 UniProtKB Modified residue 3636 3636 . . . Note=S-nitrosocysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11716 E9PZQ0 UniProtKB Modified residue 4464 4464 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:F1LMY4 E9PZQ0 UniProtKB Modified residue 4468 4468 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:F1LMY4 E9PZQ0 UniProtKB Modified residue 4861 4861 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21817 E9PZQ0 UniProtKB Modified residue 4864 4864 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P21817 E9PZQ0 UniProtKB Mutagenesis 165 165 . . . Note=Increased channel activity%2C leading to permanently increased cytoplasmic Ca(2+) levels. Increased activation by calcium%2C and increased ryanodine binding. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21156754;Dbxref=PMID:21156754 E9PZQ0 UniProtKB Mutagenesis 4895 4895 . . . Note=Causes paralysis and perinatal death in homozygous mice%2C apparently due to asphyxia. Mutant mice have greatly reduced and amorphous skeletal muscle. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18003898;Dbxref=PMID:18003898 E9PZQ0 UniProtKB Sequence conflict 616 616 . . . Note=R->C;Ontology_term=ECO:0000305;evidence=ECO:0000305 E9PZQ0 UniProtKB Sequence conflict 1380 1380 . . . Note=A->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 E9PZQ0 UniProtKB Sequence conflict 3484 3484 . . . Note=D->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 E9PZQ0 UniProtKB Sequence conflict 4766 4766 . . . Note=I->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 E9PZQ0 UniProtKB Sequence conflict 4821 4821 . . . Note=L->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 E9PZQ0 UniProtKB Sequence conflict 4888 4888 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305