##gff-version 3 Q9EPK8 UniProtKB Chain 1 871 . . . ID=PRO_0000215348;Note=Transient receptor potential cation channel subfamily V member 4 Q9EPK8 UniProtKB Topological domain 1 469 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Transmembrane 470 490 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Topological domain 491 507 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Transmembrane 508 534 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Topological domain 535 547 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Transmembrane 548 568 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Topological domain 569 572 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Transmembrane 573 593 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Topological domain 594 608 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Transmembrane 609 636 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Topological domain 637 665 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Intramembrane 666 685 . . . Note=Pore-forming;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Topological domain 686 693 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Transmembrane 694 722 . . . Note=Helical;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Topological domain 723 871 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O35433 Q9EPK8 UniProtKB Repeat 237 266 . . . Note=ANK 1 Q9EPK8 UniProtKB Repeat 284 313 . . . Note=ANK 2 Q9EPK8 UniProtKB Repeat 369 398 . . . Note=ANK 3 Q9EPK8 UniProtKB Region 1 68 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9EPK8 UniProtKB Region 110 143 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9EPK8 UniProtKB Region 812 831 . . . Note=Interaction with calmodulin and ITPR3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HBA0 Q9EPK8 UniProtKB Region 850 871 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9EPK8 UniProtKB Motif 679 682 . . . Note=Selectivity filter;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12093812;Dbxref=PMID:12093812 Q9EPK8 UniProtKB Compositional bias 112 131 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9EPK8 UniProtKB Binding site 192 192 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HBA0 Q9EPK8 UniProtKB Binding site 197 197 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HBA0 Q9EPK8 UniProtKB Binding site 201 201 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HBA0 Q9EPK8 UniProtKB Binding site 236 239 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HBA0 Q9EPK8 UniProtKB Binding site 248 248 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9HBA0 Q9EPK8 UniProtKB Binding site 249 251 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A1D5PXA5 Q9EPK8 UniProtKB Binding site 296 299 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A1D5PXA5 Q9EPK8 UniProtKB Binding site 344 344 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:A0A1D5PXA5 Q9EPK8 UniProtKB Binding site 682 682 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9R186 Q9EPK8 UniProtKB Modified residue 110 110 . . . Note=Phosphotyrosine%3B by SRC-type Tyr-kinases;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19033444;Dbxref=PMID:19033444 Q9EPK8 UniProtKB Modified residue 253 253 . . . Note=Phosphotyrosine%3B by LYN;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:12538589;Dbxref=PMID:12538589 Q9EPK8 UniProtKB Modified residue 805 805 . . . Note=Phosphotyrosine%3B by SRC-type Tyr-kinases;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19033444;Dbxref=PMID:19033444 Q9EPK8 UniProtKB Modified residue 824 824 . . . Note=Phosphoserine%3B by PKC and PKA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20043876;Dbxref=PMID:20043876 Q9EPK8 UniProtKB Glycosylation 651 651 . . . Note=N-linked (GlcNAc...) asparagine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:16368742;Dbxref=PMID:16368742 Q9EPK8 UniProtKB Mutagenesis 110 110 . . . Note=Increases protein abundance at plasma membrane. Greatly reduces channel activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19033444;Dbxref=PMID:19033444 Q9EPK8 UniProtKB Mutagenesis 142 143 . . . Note=Strongly reduced interaction with PACSIN3. PP->AL;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16627472;Dbxref=PMID:16627472 Q9EPK8 UniProtKB Mutagenesis 253 253 . . . Note=Results are conflicting as to whether hypotonicity-dependent channel activity is abolished. Y->F;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12538589,ECO:0000269|PubMed:14691263;Dbxref=PMID:12538589,PMID:14691263 Q9EPK8 UniProtKB Mutagenesis 556 556 . . . Note=Reduces channel activation by 4-alpha-PDD and heat but not hypo-osmotic cell swelling. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14691263;Dbxref=PMID:14691263 Q9EPK8 UniProtKB Mutagenesis 556 556 . . . Note=No changes in channel activation by 4-alpha-PDD or heat. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14691263;Dbxref=PMID:14691263 Q9EPK8 UniProtKB Mutagenesis 557 557 . . . Note=No changes in channel activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14691263;Dbxref=PMID:14691263 Q9EPK8 UniProtKB Mutagenesis 651 651 . . . Note=Loss of a probable N-glycosylation site. Increased expression at the cell membrane%2C leading to increased ion currents. N->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16368742;Dbxref=PMID:16368742 Q9EPK8 UniProtKB Mutagenesis 672 672 . . . Note=Greatly reduces Ca(2+) permeation and channel rectification%3B when associated with A-682. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12093812;Dbxref=PMID:12093812 Q9EPK8 UniProtKB Mutagenesis 675 675 . . . Note=No effect on channel pore properties. K->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12093812;Dbxref=PMID:12093812 Q9EPK8 UniProtKB Mutagenesis 680 680 . . . Note=Impairs Ca(2+) permeation. M->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12093812;Dbxref=PMID:12093812 Q9EPK8 UniProtKB Mutagenesis 682 682 . . . Note=Greatly reduces Ca(2+) permeation and channel rectification%3B when associated with A-672. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12093812;Dbxref=PMID:12093812 Q9EPK8 UniProtKB Mutagenesis 805 805 . . . Note=No changes in channel activity. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19033444;Dbxref=PMID:19033444 Q9EPK8 UniProtKB Mutagenesis 824 824 . . . Note=Loss of phosphorylation but no significant effect on channel activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20043876;Dbxref=PMID:20043876 Q9EPK8 UniProtKB Mutagenesis 824 824 . . . Note=Phosphomimetic mutant which enhances channel function. S->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20043876;Dbxref=PMID:20043876 Q9EPK8 UniProtKB Sequence conflict 45 45 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9EPK8 UniProtKB Sequence conflict 90 90 . . . Note=L->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9EPK8 UniProtKB Sequence conflict 137 137 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9EPK8 UniProtKB Sequence conflict 210 211 . . . Note=IP->LQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9EPK8 UniProtKB Sequence conflict 477 477 . . . Note=S->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9EPK8 UniProtKB Sequence conflict 784 784 . . . Note=N->S;Ontology_term=ECO:0000305;evidence=ECO:0000305