##gff-version 3 Q8TD43 UniProtKB Chain 1 1214 . . . ID=PRO_0000259529;Note=Transient receptor potential cation channel subfamily M member 4 Q8TD43 UniProtKB Topological domain 1 782 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Transmembrane 783 803 . . . Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Topological domain 804 814 . . . Note=Extracellular;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Transmembrane 815 835 . . . Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Topological domain 836 863 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Transmembrane 864 884 . . . Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Topological domain 885 886 . . . Note=Extracellular;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Transmembrane 887 910 . . . Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Topological domain 911 930 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Transmembrane 931 951 . . . Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Topological domain 952 963 . . . Note=Extracellular;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Intramembrane 964 984 . . . Note=Pore-forming;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Topological domain 985 1019 . . . Note=Extracellular;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Transmembrane 1020 1040 . . . Note=Helical;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Topological domain 1041 1214 . . . Note=Cytoplasmic;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:29211723,ECO:0000269|PubMed:29217581;Dbxref=PMID:29211723,PMID:29217581 Q8TD43 UniProtKB Region 1076 1176 . . . Note=Calmodulin-binding Q8TD43 UniProtKB Region 1136 1141 . . . Note=Mediates modulation by decavanadate and PIP2-binding;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16424899;Dbxref=PMID:16424899 Q8TD43 UniProtKB Coiled coil 1134 1187 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q8TD43 UniProtKB Motif 975 977 . . . Note=Selectivity filter;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29211723;Dbxref=PMID:29211723 Q8TD43 UniProtKB Binding site 171 171 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7TN37 Q8TD43 UniProtKB Binding site 421 421 . . . Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7TN37 Q8TD43 UniProtKB Binding site 448 448 . . . Note=In other chain;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q7TN37 Q8TD43 UniProtKB Binding site 828 828 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:29217581,ECO:0007744|PDB:6BQV;Dbxref=PMID:29217581 Q8TD43 UniProtKB Binding site 831 831 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:29217581,ECO:0007744|PDB:6BQV;Dbxref=PMID:29217581 Q8TD43 UniProtKB Binding site 865 865 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:29217581,ECO:0007744|PDB:6BQV;Dbxref=PMID:29217581 Q8TD43 UniProtKB Binding site 868 868 . . . Ontology_term=ECO:0000305,ECO:0007744;evidence=ECO:0000305|PubMed:29217581,ECO:0007744|PDB:6BQV;Dbxref=PMID:29217581 Q8TD43 UniProtKB Modified residue 1145 1145 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Modified residue 1152 1152 . . . Note=Phosphoserine%3B by PKC;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Glycosylation 992 992 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29217581;Dbxref=PMID:29217581 Q8TD43 UniProtKB Disulfide bond 993 1011 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:29217581,ECO:0007744|PDB:6BQR;Dbxref=PMID:29217581 Q8TD43 UniProtKB Alternative sequence 1 174 . . . ID=VSP_021442;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:11535825,ECO:0000303|PubMed:12842017;Dbxref=PMID:11535825,PMID:12842017 Q8TD43 UniProtKB Alternative sequence 738 882 . . . ID=VSP_021443;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12842017;Dbxref=PMID:12842017 Q8TD43 UniProtKB Natural variant 7 7 . . . ID=VAR_064042;Note=In PFHB1B%3B attenuated desumoylation of TRPM4 resulting in constitutive sumoylation of the channel leading to impaired endocytosis and elevated channel density at the cell surface. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19726882;Dbxref=dbSNP:rs267607142,PMID:19726882 Q8TD43 UniProtKB Natural variant 101 101 . . . ID=VAR_066761;Note=A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs113984787,PMID:21887725 Q8TD43 UniProtKB Natural variant 103 103 . . . ID=VAR_066762;Note=Y->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs144781529,PMID:21887725 Q8TD43 UniProtKB Natural variant 131 131 . . . ID=VAR_066763;Note=In PFHB1B%3B incomplete right bundle-branch block. Q->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs172146854,PMID:21887725 Q8TD43 UniProtKB Natural variant 164 164 . . . ID=VAR_066764;Note=In PFHB1B. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20562447;Dbxref=dbSNP:rs387907216,PMID:20562447 Q8TD43 UniProtKB Natural variant 252 252 . . . ID=VAR_066765;Note=R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs146564314,PMID:21887725 Q8TD43 UniProtKB Natural variant 293 293 . . . ID=VAR_066766;Note=In PFHB1B%3B right bundle-branch block. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs172147855,PMID:21887725 Q8TD43 UniProtKB Natural variant 432 432 . . . ID=VAR_066767;Note=In PFHB1B%3B atrioventricular block. A->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20562447,ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs201907325,PMID:20562447,PMID:21887725 Q8TD43 UniProtKB Natural variant 487 498 . . . ID=VAR_066768;Note=Missing Q8TD43 UniProtKB Natural variant 561 561 . . . ID=VAR_066769;Note=D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs56355369,PMID:21887725 Q8TD43 UniProtKB Natural variant 582 582 . . . ID=VAR_066770;Note=In PFHB1B%3B atrioventricular block. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs172149856,PMID:21887725 Q8TD43 UniProtKB Natural variant 790 790 . . . ID=VAR_066771;Note=In PFHB1B%3B atrioventricular block. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs172150857,PMID:21887725 Q8TD43 UniProtKB Natural variant 844 844 . . . ID=VAR_066772;Note=In PFHB1B%3B right bundle-branch block. G->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:20562447,ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs200038418,PMID:20562447,PMID:21887725 Q8TD43 UniProtKB Natural variant 854 854 . . . ID=VAR_066773;Note=Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs172155862,PMID:21887725 Q8TD43 UniProtKB Natural variant 914 914 . . . ID=VAR_066774;Note=In PFHB1B%3B atrioventricular block. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs172151858,PMID:21887725 Q8TD43 UniProtKB Natural variant 970 970 . . . ID=VAR_066775;Note=In PFHB1B%3B incomplete right bundle-branch block. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs172152859,PMID:21887725 Q8TD43 UniProtKB Natural variant 1033 1033 . . . ID=VAR_083166;Note=In EKVP6%3B increased calcium activated cation channel activity%3B increased keratinocytes proliferation and differentiation%3B no effect on localization at cell membrane. I->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30528822;Dbxref=dbSNP:rs1278993777,PMID:30528822 Q8TD43 UniProtKB Natural variant 1040 1040 . . . ID=VAR_083167;Note=In EKVP6%3B increased calcium activated cation channel activity%3B increased keratinocytes proliferation and differentiation%3B no effect on localization at cell membrane. I->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:30528822;Dbxref=dbSNP:rs1369949906,PMID:30528822 Q8TD43 UniProtKB Natural variant 1204 1204 . . . ID=VAR_066776;Note=P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21887725;Dbxref=dbSNP:rs150391806,PMID:21887725 Q8TD43 UniProtKB Mutagenesis 275 275 . . . Note=Abolishes ability to restore sensitivity to Ca(2+) after desensitization. L->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Mutagenesis 278 278 . . . Note=No effect. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Mutagenesis 279 279 . . . Note=No effect. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Mutagenesis 324 324 . . . Note=No effect. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Mutagenesis 325 325 . . . Note=Abolishes ability to restore sensitivity to Ca(2+) after desensitization. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Mutagenesis 327 327 . . . Note=No effect. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Mutagenesis 977 977 . . . Note=Alters the monovalent cation permeability sequence and results in a pore with moderate Ca(2+) permeability. Q->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15845551;Dbxref=PMID:15845551 Q8TD43 UniProtKB Mutagenesis 981 986 . . . Note=Induces a functional channel that combines the gating hallmarks of TRPM4 (activation by Ca(2+)) with TRPV6-like sensitivity to block by extracellular Ca(2+) and Mg(2+) as well as Ca(2+) permeation. EDMDVA->TIIDGP;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15845551;Dbxref=PMID:15845551 Q8TD43 UniProtKB Mutagenesis 981 981 . . . Note=Results in a channel with normal permeability properties but with a reduced sensitivity to block by intracellular spermine. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15845551;Dbxref=PMID:15845551 Q8TD43 UniProtKB Mutagenesis 982 982 . . . Note=Results in a functional channel that exhibits extremely fast desensitization%2C possibly indicating destabilization of the pore. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15845551;Dbxref=PMID:15845551 Q8TD43 UniProtKB Mutagenesis 984 984 . . . Note=Results in a non-functional channel with a dominant negative phenotype. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15845551;Dbxref=PMID:15845551 Q8TD43 UniProtKB Mutagenesis 1059 1059 . . . Note=Does not affect PIP2-binding. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16424899;Dbxref=PMID:16424899 Q8TD43 UniProtKB Mutagenesis 1072 1072 . . . Note=Does not affect PIP2-binding. R->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16424899;Dbxref=PMID:16424899 Q8TD43 UniProtKB Mutagenesis 1136 1141 . . . Note=Results in a channel with very rapid desensitization and highly reduced sensitivity to PIP2. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16424899;Dbxref=PMID:16424899 Q8TD43 UniProtKB Mutagenesis 1145 1145 . . . Note=Decreases the sensitivity to Ca(2+). S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Mutagenesis 1152 1152 . . . Note=Decreases the sensitivity to Ca(2+). S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590641;Dbxref=PMID:15590641 Q8TD43 UniProtKB Sequence conflict 1149 1149 . . . Note=K->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8TD43 UniProtKB Sequence conflict 1207 1207 . . . Note=P->L;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8TD43 UniProtKB Sequence conflict 1210 1210 . . . Note=P->H;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8TD43 UniProtKB Sequence conflict 1214 1214 . . . Note=D->E;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q8TD43 UniProtKB Beta strand 88 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 100 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 108 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 118 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 126 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 132 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 142 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 152 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 158 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 162 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 177 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 185 187 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 191 193 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 202 205 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 230 235 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 238 240 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQR Q8TD43 UniProtKB Helix 245 259 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 260 263 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 268 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 273 277 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 282 293 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 298 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 308 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 319 326 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQR Q8TD43 UniProtKB Helix 331 338 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 344 357 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 359 364 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 370 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 373 385 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 395 397 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 398 402 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 406 414 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 415 417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 422 434 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 438 446 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 451 454 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 457 465 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 469 473 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 474 480 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 504 509 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 560 568 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 572 578 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 579 581 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 585 601 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 608 633 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 635 642 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 648 651 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 654 660 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 664 667 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 670 680 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 681 683 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 690 697 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 700 704 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 705 708 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 768 776 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 779 803 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 807 809 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 812 829 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 830 834 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 852 859 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 863 883 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 888 909 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 914 916 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 917 920 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 921 926 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 927 951 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 959 965 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 968 972 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 973 975 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 980 983 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 985 987 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 995 998 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Beta strand 1005 1008 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 1017 1030 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 1031 1033 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 1034 1070 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Turn 1080 1086 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 1087 1093 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 1115 1141 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 1144 1166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV Q8TD43 UniProtKB Helix 1168 1174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6BQV