InterPro : IPR005827

Name  Potassium channel, voltage dependent, KCNQ1 Short Name  K_chnl_volt-dep_KCQN1
Type  Family Description  Potassium channels are the most diverse group of the ion channel family[, ]. They are important in shaping the action potential, and in neuronal excitability and plasticity []. The potassium channel family iscomposed of several functionally distinct isoforms, which can be broadlyseparated into 2 groups []: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.These are all highly similar proteins, with only small amino acidchanges causing the diversity of the voltage-dependent gating mechanism,channel conductance and toxin binding properties. Each type of K+channel is activated by different signals and conditions depending on their type of regulation: some open in response to depolarisation of the plasma membrane; others in response to hyperpolarisation or an increase in intracellular calcium concentration; some can be regulated by binding of a transmitter, together with intracellular kinases; while others are regulated by GTP-binding proteins orother second messengers []. In eukaryotic cells, K+channelsare involved in neural signalling and generation of the cardiac rhythm, act as effectors in signal transduction pathways involving G protein-coupled receptors (GPCRs) and may have a role in target cell lysis by cytotoxic T-lymphocytes []. In prokaryotic cells, they play a role in themaintenance of ionic homeostasis [].All K+channels discovered so far possess a core of alpha subunits, each comprising either one or two copies of a highly conserved pore loop domain (P-domain). The P-domain contains the sequence (T/SxxTxGxG), which hasbeen termed the K+selectivity sequence.In families that contain one P-domain, four subunits assemble to form a selective pathway for K+across the membrane.However, it remains unclear how the 2 P-domain subunits assemble to form a selective pore. The functional diversity of these families can arise through homo- or hetero-associations of alpha subunits or association with auxiliary cytoplasmic beta subunits. K+channel subunits containing one pore domain can be assigned into one of two superfamilies: those that possess sixtransmembrane (TM) domains and those that possess only two TM domains.The six TM domain superfamily can be further subdivided into conserved gene families: the voltage-gated (Kv) channels; the KCNQ channels (originally known as KvLQT channels); the EAG-like K+channels; and three types of calcium (Ca)-activated K+channels (BK, IK and SK)[]. The 2TM domain family comprises inward-rectifying K+channels. In addition, there are K+channel alpha-subunits that possess two P-domains. These are usually highly regulated K+selective leak channels.KCNQ channels (also known as KQT-like channels) differ from other voltage-gated 6 TM helix channels, chiefly in that they possess no tetramerisation domain. Consequently, they rely on interaction with accessory subunits, or form heterotetramers with other members of the family []. Currently, 5 members of the KCNQ family are known. These have been found to be widely distributed within the body, having been shown to be expressed in the heart, brain, pancreas, lung, placenta and ear. They were initially cloned as a result of a search for proteins involved in cardiac arhythmia. Subsequently, mutations in other KCNQ family members have been shown to be responsible for some forms of hereditary deafness []and benign familial neonatal epilepsy [].KCNQ1 was the first member of the KCNQ channel family to be isolated, and has been found to be the most common cause of the disease `long QT syndrome' a cardiac arhythmia resulting in a prolonged QT interval. In exceptional cases, this can lead to sudden death, triggered by extreme stress []. KCNQ1 is expressed in the stria vascularis of the inner ear, and may be the cause of hereditary deafness [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

2 Contains

Id Name Short Name Type
IPR005821 Ion transport domain Ion_trans_dom Domain
IPR013821 Potassium channel, voltage dependent, KCNQ, C-terminal K_chnl_volt-dep_KCNQ_C Domain

0 Found In

1 Parent Features

Id Name Short Name Type
IPR003937 Potassium channel, voltage dependent, KCNQ K_chnl_volt-dep_KCNQ Family

12 Publications

First Author Title Year Journal Volume Pages
Perney TM The molecular biology of K+ channels. 1991 Curr Opin Cell Biol 3 663-70
Luneau C Shaw-like rat brain potassium channel cDNA's with divergent 3' ends. 1991 FEBS Lett 288 163-7
Attali B Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes. 1992 J Biol Chem 267 8650-7
Schwarz TL Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila. 1988 Nature 331 137-42
Tempel BL Cloning of a probable potassium channel gene from mouse brain. 1988 Nature 332 837-9
Stühmer W Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain. 1989 EMBO J 8 3235-44
Miller C An overview of the potassium channel family. 2000 Genome Biol 1 REVIEWS0004
Sanguinetti MC Maximal function of minimal K+ channel subunits. 2000 Trends Pharmacol Sci 21 199-201
Wang Q Positional cloning of a novel potassium channel gene: KVLQT1 mutations cause cardiac arrhythmias. 1996 Nat Genet 12 17-23
Biervert C A potassium channel mutation in neonatal human epilepsy. 1998 Science 279 403-6
Sanguinetti MC Coassembly of K(V)LQT1 and minK (IsK) proteins to form cardiac I(Ks) potassium channel. 1996 Nature 384 80-3
Neyroud N A novel mutation in the potassium channel gene KVLQT1 causes the Jervell and Lange-Nielsen cardioauditory syndrome. 1997 Nat Genet 15 186-9



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Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)