##gff-version 3 Q9NZV8 UniProtKB Chain 1 630 . . . ID=PRO_0000054064;Note=A-type voltage-gated potassium channel KCND2 Q9NZV8 UniProtKB Topological domain 1 184 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:34552243;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Transmembrane 185 206 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Topological domain 207 226 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:34552243;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Transmembrane 227 249 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Topological domain 250 256 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:34552243;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Transmembrane 257 281 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Topological domain 282 287 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:34552243;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Transmembrane 288 307 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Topological domain 308 321 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:34552243;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Transmembrane 322 345 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Topological domain 346 357 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:34552243;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Intramembrane 358 369 . . . Note=Helical%3B Name%3DPore helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q9NZV8 UniProtKB Intramembrane 370 377 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q9NZV8 UniProtKB Topological domain 378 380 . . . Note=Extracellular;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:34552243;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Transmembrane 381 403 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Topological domain 404 630 . . . Note=Cytoplasmic;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:34552243;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Region 2 20 . . . Note=Interaction with KCNIP1%2C KCNIP2%2C and other family members;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Region 71 90 . . . Note=Interaction with KCNIP1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Region 308 321 . . . Note=S4-S5 linker;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q9NZV8 UniProtKB Region 474 630 . . . Note=Important for normal channel activation and inactivation%2C for interaction with KCNIP2%2C and probably other family members as well;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:Q63881,ECO:0000305|PubMed:16934482;Dbxref=PMID:16934482 Q9NZV8 UniProtKB Region 474 489 . . . Note=Required for dendritic targeting;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Region 600 630 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9NZV8 UniProtKB Motif 370 375 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q9NZV8 UniProtKB Motif 627 630 . . . Note=PDZ-binding;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Binding site 105 105 . . . Note=In chain A;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Binding site 111 111 . . . Note=In chain B;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Binding site 132 132 . . . Note=In chain A;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Binding site 133 133 . . . Note=In chain A;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:34552243,ECO:0007744|PDB:7F0J;Dbxref=PMID:34552243 Q9NZV8 UniProtKB Binding site 370 370 . . . Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:35597238,ECO:0007744|PDB:7UK5,ECO:0007744|PDB:7UKD,ECO:0007744|PDB:7UKE,ECO:0007744|PDB:7UKF;Dbxref=PMID:35597238 Q9NZV8 UniProtKB Binding site 371 371 . . . Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:35597238,ECO:0007744|PDB:7UKC,ECO:0007744|PDB:7UKG;Dbxref=PMID:35597238 Q9NZV8 UniProtKB Binding site 372 372 . . . Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:35597238,ECO:0007744|PDB:7UK5,ECO:0007744|PDB:7UKC,ECO:0007744|PDB:7UKD,ECO:0007744|PDB:7UKE,ECO:0007744|PDB:7UKF,ECO:0007744|PDB:7UKG;Dbxref=PMID:35597238 Q9NZV8 UniProtKB Binding site 373 373 . . . Ontology_term=ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|PubMed:35597238,ECO:0007744|PDB:7UK5,ECO:0007744|PDB:7UKD,ECO:0007744|PDB:7UKE,ECO:0007744|PDB:7UKF;Dbxref=PMID:35597238 Q9NZV8 UniProtKB Modified residue 38 38 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Modified residue 438 438 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Modified residue 548 548 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Modified residue 552 552 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0V2 Q9NZV8 UniProtKB Modified residue 572 572 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0V2 Q9NZV8 UniProtKB Modified residue 575 575 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0V2 Q9NZV8 UniProtKB Modified residue 602 602 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Modified residue 607 607 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63881 Q9NZV8 UniProtKB Modified residue 616 616 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9Z0V2 Q9NZV8 UniProtKB Natural variant 404 404 . . . ID=VAR_072076;Note=Found in a family with atypical autism and severe epilepsy%3B likely pathogenic%3B disrupts potassium current inactivation. V->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24501278;Dbxref=dbSNP:rs587777631,PMID:24501278 Q9NZV8 UniProtKB Mutagenesis 309 309 . . . Note=Increases peak current amplitude and causes a negative shift in the voltage-dependence of activation. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 311 311 . . . Note=No effect on peak current amplitude%2C but causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 312 312 . . . Note=Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 313 313 . . . Note=Causes a positive shift in the voltage-dependence of activation. May decrease the affinity for the closed-inactivated state of the channel. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 314 314 . . . Note=Loss of channel activity. G->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 315 315 . . . Note=Increases peak current amplitude but has a minor effect on the voltage-dependence of activation. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 316 316 . . . Note=Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 317 317 . . . Note=Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 318 318 . . . Note=Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 319 319 . . . Note=May impair protein folding. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 320 320 . . . Note=Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 320 320 . . . Note=Increases peak current amplitude and slows the onset of inactivation at low voltage%2C but has no effect on the voltage-dependence of activation. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 322 322 . . . Note=Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 323 323 . . . Note=Slightly increases peak current amplitude and causes a negative shift in the voltage-dependence of activation. May decrease the affinity for the closed-inactivated state of the channel. E->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 324 324 . . . Note=May impair protein folding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 327 327 . . . Note=Loss of channel activity. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 328 328 . . . Note=May impair protein folding. L->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 329 329 . . . Note=Loss of channel activity. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 397 397 . . . Note=May impair protein folding. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 398 398 . . . Note=Loss of channel activity. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 399 399 . . . Note=May impair protein folding. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 401 401 . . . Note=May impair protein folding. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 402 404 . . . Note=Increases pak current amplitude and causes a positive shift in the voltage-dependence of activation and steady-state inactivation. May increase the affinity for the closed-inactivated state of the channel. VPV->IPI;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 403 403 . . . Note=Loss of channel activity. P->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 405 405 . . . Note=Loss of channel activity. I->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 406 406 . . . Note=Loss of channel activity. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 407 407 . . . Note=Increases peak current amplitude but has no effect on the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 408 408 . . . Note=Decreases peak current amplitude and causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel. N->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 409 409 . . . Note=May impair protein folding. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19171772;Dbxref=PMID:19171772 Q9NZV8 UniProtKB Mutagenesis 601 604 . . . Note=Abolishes interaction with FLNC. PTPP->ATAA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11102480;Dbxref=PMID:11102480 Q9NZV8 UniProtKB Sequence conflict 450 450 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NZV8 UniProtKB Sequence conflict 464 464 . . . Note=Q->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NZV8 UniProtKB Sequence conflict 550 550 . . . Note=Q->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NZV8 UniProtKB Sequence conflict 553 553 . . . Note=I->V;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9NZV8 UniProtKB Helix 9 15 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 16 18 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Turn 19 22 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 28 31 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 36 38 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Beta strand 43 47 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Beta strand 50 54 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 56 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Turn 66 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 70 75 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Turn 78 81 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 89 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Beta strand 108 110 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7F0J Q9NZV8 UniProtKB Helix 112 121 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 126 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 131 152 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 155 157 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7F0J Q9NZV8 UniProtKB Helix 167 176 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Turn 178 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 182 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Beta strand 207 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Beta strand 216 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 221 224 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 226 249 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 254 258 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 261 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 280 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Beta strand 283 285 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 288 295 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 296 305 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 308 319 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 321 346 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Beta strand 349 351 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7F0J Q9NZV8 UniProtKB Helix 357 368 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Beta strand 374 376 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 381 399 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 402 423 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKG Q9NZV8 UniProtKB Helix 426 450 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH Q9NZV8 UniProtKB Helix 473 489 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7UKH