InterPro : IPR003950

Name  Potassium channel, voltage-dependent, ELK Short Name  K_chnl_volt-dep_ELK
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 six transmembrane (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.The first EAG K+ channel was identified in Drosophila melanogaster(Fruit fly), following a screen for mutations giving rise to behavioural abnormalities. Disruption of the Eag gene caused an ether-induced, leg-shaking behaviour. Subsequent studies have revealed a conserved multi-gene family of EAG-like K+ channels, which are present in human and many other species. Based on the varying functional properties of the channels, the family has been divided into 3 subfamilies: EAG, ELK and ERG. Interestingly, Caenorhabditis elegansappears to lack the ELK type [].Little is known about the properties of channels of the ELK subfamily. However, when expressed in frog oocytes, they show properties between thoseof the EAG and ERG subtypes. Included in this family are Bec1 and Bec2,brain-specific genes found in the human telencephalon regions. It is thoughtthat they are involved in cellular excitability of restricted neurons in thehuman central nervous system. Phylogenetic analysis reveals that these genesconstitute a subfamily with Elk within the Eag family []. Recently, afurther Elk subfamily member has been identified in the mouse (Melk). On thebasis of sequence similarity, this indicates a distinct subclass within this family [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

8 Contains

Id Name Short Name Type
IPR005821 Ion transport domain Ion_trans_dom Domain
IPR018490 Cyclic nucleotide-binding-like cNMP-bd-like Domain
IPR000595 Cyclic nucleotide-binding domain cNMP-bd_dom Domain
IPR000014 PAS domain PAS Domain
IPR013655 PAS fold-3 PAS_fold_3 Domain
IPR014710 RmlC-like jelly roll fold RmlC-like_jellyroll Domain
IPR001610 PAC motif PAC Repeat
IPR000700 PAS-associated, C-terminal PAS-assoc_C Domain

0 Found In

1 Parent Features

Id Name Short Name Type
IPR003938 Potassium channel, voltage-dependent, EAG/ELK/ERG K_chnl_volt-dep_EAG/ELK/ERG Family

10 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
Littleton JT Ion channels and synaptic organization: analysis of the Drosophila genome. 2000 Neuron 26 35-43
Miyake A New ether-à-go-go K(+) channel family members localized in human telencephalon. 1999 J Biol Chem 274 25018-25
Trudeau MC Functional analysis of a mouse brain Elk-type K+ channel. 1999 J Neurosci 19 2906-18



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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)