##gff-version 3 Q9HBA0 UniProtKB Chain 1 871 . . . ID=PRO_0000215347;Note=Transient receptor potential cation channel subfamily V member 4 Q9HBA0 UniProtKB Topological domain 1 469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Transmembrane 470 490 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Topological domain 491 507 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Transmembrane 508 534 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Topological domain 535 547 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Transmembrane 548 568 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Topological domain 569 572 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Transmembrane 573 593 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Topological domain 594 608 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Transmembrane 609 636 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Topological domain 637 665 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Intramembrane 666 685 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Topological domain 686 693 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Transmembrane 694 722 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Topological domain 723 871 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Repeat 237 266 . . . Note=ANK 1 Q9HBA0 UniProtKB Repeat 284 313 . . . Note=ANK 2 Q9HBA0 UniProtKB Repeat 369 398 . . . Note=ANK 3 Q9HBA0 UniProtKB Region 1 68 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9HBA0 UniProtKB Region 812 831 . . . Note=Interaction with calmodulin and ITPR3;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12724311,ECO:0000269|PubMed:18826956;Dbxref=PMID:12724311,PMID:18826956 Q9HBA0 UniProtKB Region 849 871 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9HBA0 UniProtKB Motif 679 682 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9HBA0 UniProtKB Binding site 192 192 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22702953,ECO:0007744|PDB:4DX2;Dbxref=PMID:22702953 Q9HBA0 UniProtKB Binding site 197 197 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22702953,ECO:0007744|PDB:4DX2;Dbxref=PMID:22702953 Q9HBA0 UniProtKB Binding site 201 201 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22702953,ECO:0007744|PDB:4DX2;Dbxref=PMID:22702953 Q9HBA0 UniProtKB Binding site 236 239 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22702953,ECO:0007744|PDB:4DX2;Dbxref=PMID:22702953 Q9HBA0 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:22702953,ECO:0007744|PDB:4DX2;Dbxref=PMID:22702953 Q9HBA0 UniProtKB Binding site 249 251 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A1D5PXA5 Q9HBA0 UniProtKB Binding site 296 299 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A1D5PXA5 Q9HBA0 UniProtKB Binding site 344 344 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A1D5PXA5 Q9HBA0 UniProtKB Binding site 682 682 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9R186 Q9HBA0 UniProtKB Modified residue 110 110 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPK8 Q9HBA0 UniProtKB Modified residue 253 253 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPK8 Q9HBA0 UniProtKB Modified residue 805 805 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPK8 Q9HBA0 UniProtKB Modified residue 824 824 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9EPK8 Q9HBA0 UniProtKB Alternative sequence 28 61 . . . ID=VSP_026614;Note=In isoform 5. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16293632;Dbxref=PMID:16293632 Q9HBA0 UniProtKB Alternative sequence 239 285 . . . ID=VSP_026615;Note=In isoform 4 and isoform 6. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16293632;Dbxref=PMID:16293632 Q9HBA0 UniProtKB Alternative sequence 385 444 . . . ID=VSP_013436;Note=In isoform 2 and isoform 6. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:16293632,ECO:0000303|Ref.6;Dbxref=PMID:16293632 Q9HBA0 UniProtKB Alternative sequence 844 871 . . . ID=VSP_013437;Note=In isoform 3. PLDSMGNPRCDGHQQGYPRKWRTDDAPL->RHLCRVRRKR;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12692122;Dbxref=PMID:12692122 Q9HBA0 UniProtKB Natural variant 19 19 . . . ID=VAR_052391;Note=Associated with lower sodium concentrations in serum%3B shows diminished response to hypotonic stress relative to wild-type. P->S;Dbxref=dbSNP:rs3742030 Q9HBA0 UniProtKB Natural variant 89 89 . . . ID=VAR_064517;Note=In MTD%3B lethal form. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20425821;Dbxref=dbSNP:rs397514473,PMID:20425821 Q9HBA0 UniProtKB Natural variant 97 97 . . . ID=VAR_067989;Note=In HMND8%3B decreased calcium channel activity. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22526352;Dbxref=dbSNP:rs876661124,PMID:22526352 Q9HBA0 UniProtKB Natural variant 183 183 . . . ID=VAR_064518;Note=Found in a patient with spondyloepiphyseal dysplasia Maroteaux type%3B decreased protein stability%3B increased ATP-binding. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20503319,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs387906324,PMID:20503319,PMID:22702953 Q9HBA0 UniProtKB Natural variant 197 197 . . . ID=VAR_064519;Note=In MTD%3B lethal form%3B decreased protein stability%3B reduced ATP-binding. K->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20425821,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs387906903,PMID:20425821,PMID:22702953 Q9HBA0 UniProtKB Natural variant 199 199 . . . ID=VAR_064520;Note=In MTD%3B decreased protein stability. L->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20577006,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs515726167,PMID:20577006,PMID:22702953 Q9HBA0 UniProtKB Natural variant 232 232 . . . ID=VAR_067990;Note=In HMND8 and CMT2C%3B does not affect channel localization to plasma membrane%3B results in increased agonist-induced channel activity and increased basal intracellular calcium concentration%3B decreases ATP-binding%3B no effect on protein stability%3B decreases binding to membranes enriched in phosphatidylinositol-2%2C4-bisphosphate%3B causes increased cell death. R->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21288981,ECO:0000269|PubMed:22526352,ECO:0000269|PubMed:22702953,ECO:0000269|PubMed:25256292;Dbxref=dbSNP:rs387906904,PMID:21288981,PMID:22526352,PMID:22702953,PMID:25256292 Q9HBA0 UniProtKB Natural variant 269 269 . . . ID=VAR_063528;Note=In CMT2C%3B increased agonist-induced channel activity%3B causes increased cell death%3B no effect on protein stability and ATP-binding. R->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20037586,ECO:0000269|PubMed:21288981,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs267607146,PMID:20037586,PMID:21288981,PMID:22702953 Q9HBA0 UniProtKB Natural variant 269 269 . . . ID=VAR_063529;Note=In HMND8 and CMT2C%3B increased agonist-induced channel activity and increased basal intracellular calcium concentration%3B slightly decreased protein stability and ATP-binding%3B decreases binding to membranes enriched in phosphatidylinositol-2%2C4-bisphosphate%3B causes increased cell death. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20037586,ECO:0000269|PubMed:20037587,ECO:0000269|PubMed:20037588,ECO:0000269|PubMed:21288981,ECO:0000269|PubMed:22702953,ECO:0000269|PubMed:25256292;Dbxref=dbSNP:rs267607144,PMID:20037586,PMID:20037587,PMID:20037588,PMID:21288981,PMID:22702953,PMID:25256292 Q9HBA0 UniProtKB Natural variant 270 270 . . . ID=VAR_068498;Note=In FDAB%3B poorly expressed on the cell surface%3B mutant channels show a significantly reduced response to agonists. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21964574;Dbxref=dbSNP:rs387907220,PMID:21964574 Q9HBA0 UniProtKB Natural variant 271 271 . . . ID=VAR_068499;Note=In FDAB%3B poorly expressed on the cell surface%3B mutant channels show a significantly reduced response to agonists. R->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21964574;Dbxref=dbSNP:rs387907219,PMID:21964574 Q9HBA0 UniProtKB Natural variant 273 273 . . . ID=VAR_068500;Note=In FDAB%3B poorly expressed on the cell surface%3B mutant channels show a significantly reduced response to agonists. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21964574;Dbxref=dbSNP:rs515726170,PMID:21964574 Q9HBA0 UniProtKB Natural variant 278 278 . . . ID=VAR_064521;Note=In SMDK%3B slightly increased ATP-binding%3B slightly decreased protein stability. E->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20577006,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs267607148,PMID:20577006,PMID:22702953 Q9HBA0 UniProtKB Natural variant 295 295 . . . ID=VAR_064522;Note=In MTD%3B impairs protein folding or stability. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20577006,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs515726171,PMID:20577006,PMID:22702953 Q9HBA0 UniProtKB Natural variant 315 315 . . . ID=VAR_063541;Note=In CMT2C%3B increased basal and agonist-induced channel activity%2C decreased protein stability%3B decreased ATP-binding%3B decreases binding to membranes enriched in phosphatidylinositol-2%2C4-bisphosphate%3B causes increased cell death. R->W;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20037588,ECO:0000269|PubMed:21115951,ECO:0000269|PubMed:22702953,ECO:0000269|PubMed:25256292;Dbxref=dbSNP:rs267607143,PMID:20037588,PMID:21115951,PMID:22702953,PMID:25256292 Q9HBA0 UniProtKB Natural variant 316 316 . . . ID=VAR_063530;Note=In CMT2C and SPSMA%3B decreased protein stability%3B decreased ATP-binding. R->C;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20037587,ECO:0000269|PubMed:20037588;Dbxref=dbSNP:rs267607145,PMID:20037587,PMID:20037588 Q9HBA0 UniProtKB Natural variant 316 316 . . . ID=VAR_067991;Note=In CMT2C%3B does not affect channel localization to plasma membrane%3B results in increased agonist-induced channel activity and increased basal intracellular calcium concentration%3B decreases protein stability%3B causes increased cell death. R->H;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:21288981,ECO:0000269|PubMed:25256292;Dbxref=dbSNP:rs387906905,PMID:21288981,PMID:25256292 Q9HBA0 UniProtKB Natural variant 331 331 . . . ID=VAR_062331;Note=In MTD%3B decreased protein stability%3B no effect on ATP-binding. I->F;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19232556,ECO:0000269|PubMed:20425821,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs121912636,PMID:19232556,PMID:20425821,PMID:22702953 Q9HBA0 UniProtKB Natural variant 331 331 . . . ID=VAR_064523;Note=In MTD%3B no effect on protein stability%3B no effect on ATP-binding. I->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20577006,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs515726172,PMID:20577006,PMID:22702953 Q9HBA0 UniProtKB Natural variant 333 336 . . . ID=VAR_067992;Note=In SMDK. Missing Q9HBA0 UniProtKB Natural variant 333 333 . . . ID=VAR_062332;Note=In SMDK%3B decreased protein stability%3B no effect on ATP-binding. D->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19232556,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs121912634,PMID:19232556,PMID:22702953 Q9HBA0 UniProtKB Natural variant 342 342 . . . ID=VAR_064524;Note=In MTD%3B decreased protein stability%3B decreased ATP-binding. V->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20577006,ECO:0000269|PubMed:22702953;Dbxref=dbSNP:rs515726152,PMID:20577006,PMID:22702953 Q9HBA0 UniProtKB Natural variant 471 471 . . . ID=VAR_064525;Note=In MTD%3B lethal form. Missing;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20425821,ECO:0000269|PubMed:20577006;Dbxref=PMID:20425821,PMID:20577006 Q9HBA0 UniProtKB Natural variant 542 542 . . . ID=VAR_067993;Note=In CMT2C. S->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21115951;Dbxref=dbSNP:rs387906902,PMID:21115951 Q9HBA0 UniProtKB Natural variant 592 592 . . . ID=VAR_064526;Note=In MTD. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs515726158,PMID:20577006 Q9HBA0 UniProtKB Natural variant 594 594 . . . ID=VAR_062333;Note=In SMDK and PSTD. R->H;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19232556,ECO:0000269|PubMed:20503319,ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs77975504,PMID:19232556,PMID:20503319,PMID:20577006 Q9HBA0 UniProtKB Natural variant 596 596 . . . ID=VAR_064527;Note=In SMDK. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs515726159,PMID:20577006 Q9HBA0 UniProtKB Natural variant 600 600 . . . ID=VAR_064528;Note=In SMDK. G->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs515726160,PMID:20577006 Q9HBA0 UniProtKB Natural variant 602 602 . . . ID=VAR_064529;Note=Found in a patient with spondyloepiphyseal dysplasia Maroteaux type. Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20503319;Dbxref=dbSNP:rs267607150,PMID:20503319 Q9HBA0 UniProtKB Natural variant 604 604 . . . ID=VAR_064530;Note=In MTD%3B lethal form. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20425821;Dbxref=dbSNP:rs515726161,PMID:20425821 Q9HBA0 UniProtKB Natural variant 616 616 . . . ID=VAR_054805;Note=In BCYM3%3B results in a gain of function and a constitutive activation of the channel. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18587396;Dbxref=dbSNP:rs121912632,PMID:18587396 Q9HBA0 UniProtKB Natural variant 617 617 . . . ID=VAR_064531;Note=In MTD. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20425821;Dbxref=dbSNP:rs515726162,PMID:20425821 Q9HBA0 UniProtKB Natural variant 618 618 . . . ID=VAR_064532;Note=In MTD. L->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20425821,ECO:0000269|Ref.6;Dbxref=dbSNP:rs515726163,PMID:20425821 Q9HBA0 UniProtKB Natural variant 620 620 . . . ID=VAR_054806;Note=In BCYM3%3B results in a gain of function and a constitutive activation of the channel. V->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18587396;Dbxref=dbSNP:rs121912633,PMID:18587396 Q9HBA0 UniProtKB Natural variant 625 625 . . . ID=VAR_064533;Note=In SMDK. M->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs515726164,PMID:20577006 Q9HBA0 UniProtKB Natural variant 709 709 . . . ID=VAR_064534;Note=In SMDK. L->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs116571438,PMID:20577006 Q9HBA0 UniProtKB Natural variant 716 716 . . . ID=VAR_062334;Note=In SMDK. A->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19232556;Dbxref=dbSNP:rs121912635,PMID:19232556 Q9HBA0 UniProtKB Natural variant 775 775 . . . ID=VAR_064535;Note=In MTD. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=PMID:20577006 Q9HBA0 UniProtKB Natural variant 777 777 . . . ID=VAR_064536;Note=In SMDK. C->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs515726165,PMID:20577006 Q9HBA0 UniProtKB Natural variant 797 797 . . . ID=VAR_064537;Note=In MTD and SMDK%3B also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20425821,ECO:0000269|PubMed:20503319,ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs267607149,PMID:20425821,PMID:20503319,PMID:20577006 Q9HBA0 UniProtKB Natural variant 799 799 . . . ID=VAR_064538;Note=In MTD. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs267607147,PMID:20577006 Q9HBA0 UniProtKB Natural variant 799 799 . . . ID=VAR_062335;Note=In MTD%3B also found in a patient with spondyloepiphyseal dysplasia Maroteaux type. P->L;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19232556,ECO:0000269|PubMed:20425821,ECO:0000269|PubMed:20503319,ECO:0000269|PubMed:20577006,ECO:0000269|PubMed:26249260;Dbxref=dbSNP:rs121912637,PMID:19232556,PMID:20425821,PMID:20503319,PMID:20577006,PMID:26249260 Q9HBA0 UniProtKB Natural variant 799 799 . . . ID=VAR_064539;Note=In MTD. P->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs121912637,PMID:20577006 Q9HBA0 UniProtKB Natural variant 799 799 . . . ID=VAR_064540;Note=In MTD. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20577006;Dbxref=dbSNP:rs267607147,PMID:20577006 Q9HBA0 UniProtKB Mutagenesis 231 231 . . . Note=Decreased ATP-binding. F->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22702953;Dbxref=PMID:22702953 Q9HBA0 UniProtKB Mutagenesis 251 251 . . . Note=No effect on channel activity. No effect on interaction with membranes enriched in phosphatidylinositol-2%2C4-bisphosphate. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25256292;Dbxref=PMID:25256292 Q9HBA0 UniProtKB Mutagenesis 296 296 . . . Note=Loss of interaction with membranes enriched in phosphatidylinositol-2%2C4-bisphosphate%3B when associated with P-299. N->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25256292;Dbxref=PMID:25256292 Q9HBA0 UniProtKB Mutagenesis 299 299 . . . Note=Strongly decreased interaction with membranes enriched in phosphatidylinositol-2%2C4-bisphosphate. Loss of interaction with membranes enriched in phosphatidylinositol-2%2C4-bisphosphate%3B when associated with D-296. H->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25256292;Dbxref=PMID:25256292 Q9HBA0 UniProtKB Mutagenesis 344 344 . . . Note=No effect on channel activity. No effect on interaction with membranes enriched in phosphatidylinositol-2%2C4-bisphosphate. K->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25256292;Dbxref=PMID:25256292 Q9HBA0 UniProtKB Mutagenesis 680 680 . . . Note=Loss of Ca(2+) influx. Loss of DDX3X translocation to the nucleus. M->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29899501;Dbxref=PMID:29899501 Q9HBA0 UniProtKB Mutagenesis 816 821 . . . Note=Loss of calmodulin binding%3B when associated with A-828. RLRRDR->ELEEDE Q9HBA0 UniProtKB Mutagenesis 821 824 . . . Note=Loss of calmodulin binding. RWSS->AASA Q9HBA0 UniProtKB Mutagenesis 822 822 . . . Note=Loss of Ca(2+) dependent current potentiation. W->A Q9HBA0 UniProtKB Mutagenesis 828 828 . . . Note=Loss of calmodulin binding%3B when associated with 816-ELEEDE-821. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12724311;Dbxref=PMID:12724311 Q9HBA0 UniProtKB Sequence conflict 385 385 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9HBA0 UniProtKB Sequence conflict 452 452 . . . Note=V->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9HBA0 UniProtKB Sequence conflict 781 781 . . . Note=D->N;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9HBA0 UniProtKB Sequence conflict 820 820 . . . Note=D->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9HBA0 UniProtKB Sequence conflict 861 861 . . . Note=P->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9HBA0 UniProtKB Sequence conflict 867 867 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9HBA0 UniProtKB Helix 151 159 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 164 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 169 175 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 183 185 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Beta strand 188 190 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 194 200 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 209 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 223 228 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Beta strand 234 239 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 241 247 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 251 260 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 271 273 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX2 Q9HBA0 UniProtKB Turn 276 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 288 294 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 298 306 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 324 331 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 336 356 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Beta strand 357 360 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 362 364 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX2 Q9HBA0 UniProtKB Helix 373 379 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1 Q9HBA0 UniProtKB Helix 383 395 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4DX1