Protein Domain : IPR003938

Type:  Family Name:  Potassium channel, voltage-dependent, EAG/ELK/ERG
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 broadly separated 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 acid changes 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 or other second messengers []. In eukaryotic cells, K+channels are 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 []. Short Name:  K_chnl_volt-dep_EAG/ELK/ERG
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5 Child Features

DB identifier Type Name
IPR003967 Family Potassium channel, voltage-dependent, ERG
IPR003949 Family Potassium channel, voltage-dependent, EAG
IPR003950 Family Potassium channel, voltage-dependent, ELK
IPR030173 Family Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
IPR030169 Family Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1

6 Contains

DB identifier Type Name
IPR018490 Domain Cyclic nucleotide-binding-like
IPR000595 Domain Cyclic nucleotide-binding domain
IPR014710 Domain RmlC-like jelly roll fold
IPR005821 Domain Ion transport domain
IPR021789 Domain KHA domain
IPR013621 Domain Ion transport N-terminal

1 Cross References

Identifier
PR01463

0 Found In

3 GO Annotations

GO Term Gene Name
GO:0005249 IPR003938
GO:0006813 IPR003938
GO:0016020 IPR003938

3 Ontology Annotations

GO Term Gene Name
GO:0005249 IPR003938
GO:0006813 IPR003938
GO:0016020 IPR003938

0 Parent Features

3256 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
113786 D8SCK7 PAC:15418666 Selaginella moellendorffii 726  
evm.model.supercontig_116.82 PAC:16406343 Carica papaya 791  
evm.model.supercontig_124.35 PAC:16407192 Carica papaya 545  
evm.model.supercontig_3.357 PAC:16416654 Carica papaya 825  
evm.model.supercontig_334.1 PAC:16417780 Carica papaya 877  
evm.model.supercontig_65.6 PAC:16424470 Carica papaya 716  
evm.model.supercontig_91.38 PAC:16428492 Carica papaya 806  
evm.model.supercontig_92.107 PAC:16428564 Carica papaya 702  
29693.m002020 B9S124 PAC:16805990 Ricinus communis 813  
29794.m003476 B9RS77 PAC:16808835 Ricinus communis 629  
29807.m000501 B9STQ4 PAC:16809344 Ricinus communis 901  
29912.m005585 B9RK12 PAC:16813460 Ricinus communis 886  
30147.m013975 B9RB50 PAC:16819990 Ricinus communis 680  
28613.m000143 B9T5D2 PAC:16801255 Ricinus communis 814  
29222.m000395 B9SU64 PAC:16802498 Ricinus communis 845  
Cucsa.386020.1 A0A0A0KGF9 PAC:16982671 Cucumis sativus 700  
Cucsa.063430.1 A0A0A0LWC8 PAC:16954985 Cucumis sativus 873  
Cucsa.090180.4 PAC:16957261 Cucumis sativus 698  
Cucsa.090180.1 A0A0A0LJ35 PAC:16957258 Cucumis sativus 731  
Cucsa.090180.6 PAC:16957263 Cucumis sativus 696  
Cucsa.090180.5 PAC:16957262 Cucumis sativus 696  
Cucsa.090180.7 PAC:16957264 Cucumis sativus 668  
Cucsa.090180.2 PAC:16957259 Cucumis sativus 719  
Cucsa.090180.3 PAC:16957260 Cucumis sativus 719  
Cucsa.124380.1 PAC:16961703 Cucumis sativus 594  
Cucsa.033010.1 PAC:16952515 Cucumis sativus 636  
Cucsa.034670.1 A0A0A0KRM4 PAC:16952628 Cucumis sativus 828  
Cucsa.063730.1 PAC:16955000 Cucumis sativus 823  
Cucsa.212380.1 PAC:16969330 Cucumis sativus 699  
Cucsa.310500.1 PAC:16976537 Cucumis sativus 817  

8 Publications

First Author Title Year Journal Volume Pages PubMed ID
            1772658
            1879548
            1373731
            2448635
            2451788
            2555158
            11178249
            10798390