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{
"metadata": {
"accession": "IPR003967",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0005249",
"name": "voltage-gated potassium channel activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006813",
"name": "potassium ion transport",
"category": {
"code": "P",
"name": "biological_process"
}
},
{
"identifier": "GO:0016020",
"name": "membrane",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"prints": {
"PR01470": "ERGCHANNEL"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR003938",
"name": "Potassium channel, voltage-dependent, EAG/ELK/ERG-like",
"type": "Family",
"children": [
{
"accession": "IPR045319",
"name": "Potassium channel KAT/AKT",
"type": "Family",
"children": []
},
{
"accession": "IPR050818",
"name": "Potassium channel, voltage-dependent, EAG/ELK/ERG-like, animal-type",
"type": "Family",
"children": [
{
"accession": "IPR003949",
"name": "Potassium channel, voltage-dependent, EAG",
"type": "Family",
"children": []
},
{
"accession": "IPR003950",
"name": "Potassium channel, voltage-dependent, ELK",
"type": "Family",
"children": []
},
{
"accession": "IPR003967",
"name": "Potassium channel, voltage-dependent, ERG",
"type": "Family",
"children": []
}
]
}
]
},
"name": {
"name": "Potassium channel, voltage-dependent, ERG",
"short": "K_chnl_volt-dep_ERG"
},
"description": [
{
"text": "<p>Potassium channels are the most diverse group of the ion channel family [[cite:PUB00001055], [cite:PUB00001622]]. They are important in shaping the action potential, and in neuronal excitability and plasticity [[cite:PUB00004020]]. The potassium channel family is composed of several functionally distinct isoforms, which can be broadly separated into 2 groups [[cite:PUB00006577]]: the practically non-inactivating 'delayed' group and the rapidly inactivating 'transient' group.</p>\r\n<p>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<SUP>+</SUP>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 [[cite:PUB00004011]]. In eukaryotic cells, K<SUP>+</SUP>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 [[cite:PUB00002771]]. In prokaryotic cells, they play a role in the maintenance of ionic homeostasis [[cite:PUB00009378]].</p>\r\n<p>All K<SUP>+</SUP>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 has been termed the K<SUP>+</SUP>selectivity sequence. In families that contain one P-domain, four subunits assemble to form a selective pathway for K<SUP>+</SUP>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<SUP>+</SUP>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<SUP>+</SUP>channels; and three types of calcium (Ca)-activated K<SUP>+</SUP>channels (BK, IK and SK) [[cite:PUB00009378]]. The 2TM domain family comprises inward-rectifying K<SUP>+</SUP>channels. In addition, there are K<SUP>+</SUP>channel alpha-subunits that possess two P-domains. These are usually highly regulated K<SUP>+</SUP>selective leak channels.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>The first EAG K+ channel was identified in Drosophila melanogaster (Fruit fly), following a screening 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 elegans appears to lack the ELK type [[cite:PUB00007312]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>The human ether-a-go-go-related gene (HERG), cloned from hippocampus, shares 49% amino acid identity with EAG. It is also found in the heart, where it helps to control K+ efflux [[cite:PUB00008904]]. Mutations in HERG result in the disruption of the repolarising current and the disease LQT2 syndrome, an inherited disorder of cardiac repolarisation that predisposes affected individuals to life-threatening arrhythmias [[cite:PUB00008906]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This entry also includes the nematode homologue Potassium voltage-gated channel unc-103 from Caenorhabditis elegans which is involved in the movements of the male's copulatory spicules before and during male mating behaviour [[cite:PUB00155000]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00007312": {
"PMID": 10798390,
"ISBN": null,
"volume": "26",
"issue": "1",
"year": 2000,
"title": "Ion channels and synaptic organization: analysis of the Drosophila genome.",
"URL": null,
"raw_pages": "35-43",
"medline_journal": "Neuron",
"ISO_journal": "Neuron",
"authors": [
"Littleton JT",
"Ganetzky B."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0896-6273(00)81135-6"
},
"PUB00009378": {
"PMID": 11178249,
"ISBN": null,
"volume": "1",
"issue": "4",
"year": 2000,
"title": "An overview of the potassium channel family.",
"URL": null,
"raw_pages": "REVIEWS0004",
"medline_journal": "Genome Biol",
"ISO_journal": "Genome Biol.",
"authors": [
"Miller C."
],
"DOI_URL": "http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=11178249&action=stream&blobtype=pdf"
},
"PUB00001622": {
"PMID": 1879548,
"ISBN": null,
"volume": "288",
"issue": "1-2",
"year": 1991,
"title": "Shaw-like rat brain potassium channel cDNA's with divergent 3' ends.",
"URL": null,
"raw_pages": "163-7",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Luneau C",
"Wiedmann R",
"Smith JS",
"Williams JB."
],
"DOI_URL": "http://dx.doi.org/10.1016/0014-5793(91)81026-5"
},
"PUB00006577": {
"PMID": 2555158,
"ISBN": null,
"volume": "8",
"issue": "11",
"year": 1989,
"title": "Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain.",
"URL": null,
"raw_pages": "3235-44",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Stuhmer W",
"Ruppersberg JP",
"Schroter KH",
"Sakmann B",
"Stocker M",
"Giese KP",
"Perschke A",
"Baumann A",
"Pongs O."
],
"DOI_URL": "http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2555158"
},
"PUB00002771": {
"PMID": 1373731,
"ISBN": null,
"volume": "267",
"issue": "12",
"year": 1992,
"title": "Cloning, functional expression, and regulation of two K+ channels in human T lymphocytes.",
"URL": null,
"raw_pages": "8650-7",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Attali B",
"Romey G",
"Honore E",
"Schmid-Alliana A",
"Mattei MG",
"Lesage F",
"Ricard P",
"Barhanin J",
"Lazdunski M."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/267/12/8650"
},
"PUB00008906": {
"PMID": 10187793,
"ISBN": null,
"volume": "274",
"issue": "15",
"year": 1999,
"title": "Long QT syndrome-associated mutations in the Per-Arnt-Sim (PAS) domain of HERG potassium channels accelerate channel deactivation.",
"URL": null,
"raw_pages": "10113-8",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Chen J",
"Zou A",
"Splawski I",
"Keating MT",
"Sanguinetti MC."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.274.15.10113"
},
"PUB00004020": {
"PMID": 2451788,
"ISBN": null,
"volume": "332",
"issue": "6167",
"year": 1988,
"title": "Cloning of a probable potassium channel gene from mouse brain.",
"URL": null,
"raw_pages": "837-9",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Tempel BL",
"Jan YN",
"Jan LY."
],
"DOI_URL": "http://dx.doi.org/10.1038/332837a0"
},
"PUB00004011": {
"PMID": 2448635,
"ISBN": null,
"volume": "331",
"issue": "6152",
"year": 1988,
"title": "Multiple potassium-channel components are produced by alternative splicing at the Shaker locus in Drosophila.",
"URL": null,
"raw_pages": "137-42",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Schwarz TL",
"Tempel BL",
"Papazian DM",
"Jan YN",
"Jan LY."
],
"DOI_URL": "http://dx.doi.org/10.1038/331137a0"
},
"PUB00008904": {
"PMID": 7604285,
"ISBN": null,
"volume": "269",
"issue": "5220",
"year": 1995,
"title": "HERG, a human inward rectifier in the voltage-gated potassium channel family.",
"URL": null,
"raw_pages": "92-5",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Trudeau MC",
"Warmke JW",
"Ganetzky B",
"Robertson GA."
],
"DOI_URL": "http://www.sciencemag.org/cgi/content/abstract/269/5220/92"
},
"PUB00001055": {
"PMID": 1772658,
"ISBN": null,
"volume": "3",
"issue": "4",
"year": 1991,
"title": "The molecular biology of K+ channels.",
"URL": null,
"raw_pages": "663-70",
"medline_journal": "Curr Opin Cell Biol",
"ISO_journal": "Curr. Opin. Cell Biol.",
"authors": [
"Perney TM",
"Kaczmarek LK."
],
"DOI_URL": "http://dx.doi.org/10.1016/0955-0674(91)90039-2"
},
"PUB00155000": {
"PMID": 12684455,
"ISBN": null,
"volume": "23",
"issue": "7",
"year": 2003,
"title": "Caenorhabditis elegans UNC-103 ERG-like potassium channel regulates contractile behaviors of sex muscles in males before and during mating.",
"URL": null,
"raw_pages": "2696-705",
"medline_journal": "J Neurosci",
"ISO_journal": "J Neurosci",
"authors": [
"Garcia LR",
"Sternberg PW."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR014710",
"name": "RmlC-like jelly roll fold",
"type": "homologous_superfamily"
},
{
"accession": "IPR018490",
"name": "Cyclic nucleotide-binding domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 25286,
"pathways": 10,
"proteins": 5432,
"proteomes": 1140,
"sets": 0,
"structural_models": {
"alphafold": 4537,
"bfvd": 0
},
"structures": 21,
"taxa": 3836
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
