Protein Details: Potassium voltage-gated channel subfamily KQT member 1

Protein ID

ICDB_Pro_0686

Protein Name

Potassium voltage-gated channel subfamily KQT member 1

Gene Name

kcnq1; kvlqt1

Organism

Xenopus laevis (African clawed frog)

Length

652 amino acids

AlphaFoldDB

AF-P70057-F1-model_v4.pdb

Function

Potassium channel that plays an important role in a number of tissues; including heart; inner ear; stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity). When associated with KCNE3; forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). When associated with KCNE2; forms a heterooligomer complex leading to currents with an apparently instantaneous activation; a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4; inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5; this complex only conducts current upon strong and continued depolarization (By similarity)

Sequence

MSSEQPAWTFGLFTPDQNKQAPLEMNENAINSLYEAIPLPQDGSSNGQRQEDRQANSFELKRETLVATDPPRPTINLDPRVSIYSGRRPLLSRTNIQGRVYNFLERPTGWKCFVYHFTVFLIVLICLIFSVLSTIQQYNNLATETLFWMEIVLVVFFGAEYVVRLWSAGCRSKYVGVWGRLRFARKPISVIDLIVVVASVIVLCVGSNGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAIDSSGEYQFGSYADALWWGVVTVTTIGYGDKVPQTWIGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTAWRCYAAENPDSATWKIYIRKQSRNHHLMSPSPKPKKSAMVKKKKIRTERDEGSTDKMLNIPHITYDHVADDRKNDGYSVESYENTVRKPFGFLDPSTGPFIRTSSFTDDLDMEGDTLLTPITHISELKEHHRAAIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSLGKPSLFLSVSDKVKDKGINTIGSRLNRVEDKVTQMDHKLNLITDMLHHLLTNQQGSQSIRTPHRSNSLNSENHPSRNTLPTYEQLNVPRMTQDNIS

PDB Structures

Ligand Binding

1. DICL_CP

2. DICL_Pep

Binding Site

Disease

Location

DOI ID

10.1159/000129628; 10.1038/384080a0

RefSeq

NP_001116347.1; XP_018111889.1

Feature