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{
"metadata": {
"accession": "IPR022969",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"hamap": {
"MF_01115": "Putative ion-transport protein YfeO [yfeO]"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR001807",
"name": "Chloride channel",
"type": "Family",
"children": [
{
"accession": "IPR002242",
"name": "Chloride channel ClC-0",
"type": "Family",
"children": []
},
{
"accession": "IPR002243",
"name": "Chloride channel ClC-1",
"type": "Family",
"children": []
},
{
"accession": "IPR002244",
"name": "Chloride channel ClC-2",
"type": "Family",
"children": []
},
{
"accession": "IPR002245",
"name": "H(+)/Cl(-) exchange transporter 3",
"type": "Family",
"children": []
},
{
"accession": "IPR002246",
"name": "Chloride channel ClC-4",
"type": "Family",
"children": []
},
{
"accession": "IPR002247",
"name": "Chloride channel ClC-5",
"type": "Family",
"children": []
},
{
"accession": "IPR002248",
"name": "Chloride channel ClC-6",
"type": "Family",
"children": []
},
{
"accession": "IPR002249",
"name": "H(+)/Cl(-) exchange transporter 7",
"type": "Family",
"children": []
},
{
"accession": "IPR002250",
"name": "Chloride channel ClC-K",
"type": "Family",
"children": []
},
{
"accession": "IPR002251",
"name": "Chloride channel ClC-plant",
"type": "Family",
"children": []
},
{
"accession": "IPR022969",
"name": "Chloride channel YfeO",
"type": "Family",
"children": []
},
{
"accession": "IPR023790",
"name": "Chloride channel, voltage-gated, ClcB",
"type": "Family",
"children": []
},
{
"accession": "IPR023861",
"name": "Chloride channel, ClcA",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Chloride channel YfeO",
"short": "Chloride_channel_YfeO"
},
"description": [
{
"text": "<p>Chloride channels (CLCs) constitute an evolutionarily well-conserved family of voltage-gated channels that are structurally unrelated to the other known voltage-gated channels. They are found in organisms ranging from bacteria to yeasts and plants, and also to animals. Their functions in higher animals likely include the regulation of cell volume, control of electrical excitability and trans-epithelial transport [[cite:PUB00000734]]. Some members are plasma membrane Cl channels, while others are Cl/H exchangers [[cite:PUB00155406]].</p>\n\n<p>The first member of the family (CLC-0) was expression-cloned from the electric organ of Torpedo marmorata [[cite:PUB00004085]], and subsequently nine CLC-like proteins have been cloned from mammals. They are thought to function as multimers of two or more identical or homologous subunits, and they have varying tissue distributions and functional properties. To date, CLC-0, CLC-1, CLC-2, CLC-4 and CLC-5 have been demonstrated to form functional Cl-channels; whether the remaining isoforms do so is either contested or unproven. One possible explanation for the difficulty in expressing activatable Cl-channels is that some of the isoforms may function as Cl-channels of intracellular compartments, rather than of the plasma membrane. However, they are all thought to have a similar transmembrane (TM) topology, initial hydropathy analysis suggesting 13 hydrophobic stretches long enough to form putative TM domains [[cite:PUB00004085]]. Recently, the postulated TM topology has been revised, and it now seems likely that the CLCs have 10 (or possibly 12) TM domains, with both N-and C-termini residing in the cytoplasm [[cite:PUB00004913]].</p>\n\n<p>A number of human disease-causing mutations have been identified in the genes encoding CLCs. Mutations in CLCN1, the gene encoding CLC-1, the major skeletal muscle Cl-channel, lead to both recessively and dominantly-inherited forms of muscle stiffness or myotonia [[cite:PUB00001999]]. Similarly, mutations in CLCN5, which encodes CLC-5, a renal Cl-channel, lead to several forms of inherited kidney stone disease [[cite:PUB00004230]]. These mutations have been demonstrated to reduce or abolish CLC function.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This entry represents chloride channel proteins found in bacteria.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00004230": {
"PMID": 8559248,
"ISBN": null,
"volume": "379",
"issue": "6564",
"year": 1996,
"title": "A common molecular basis for three inherited kidney stone diseases.",
"URL": null,
"raw_pages": "445-9",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Lloyd SE",
"Pearce SH",
"Fisher SE",
"Steinmeyer K",
"Schwappach B",
"Scheinman SJ",
"Harding B",
"Bolino A",
"Devoto M",
"Goodyer P",
"Rigden SP",
"Wrong O",
"Jentsch TJ",
"Craig IW",
"Thakker RV."
],
"DOI_URL": "http://dx.doi.org/10.1038/379445a0"
},
"PUB00004085": {
"PMID": 2174129,
"ISBN": null,
"volume": "348",
"issue": "6301",
"year": 1990,
"title": "Primary structure of Torpedo marmorata chloride channel isolated by expression cloning in Xenopus oocytes.",
"URL": null,
"raw_pages": "510-4",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Jentsch TJ",
"Steinmeyer K",
"Schwarz G."
],
"DOI_URL": "http://dx.doi.org/10.1038/348510a0"
},
"PUB00000734": {
"PMID": 9046241,
"ISBN": null,
"volume": "19",
"issue": "2",
"year": 1997,
"title": "Chloride channels: an emerging molecular picture.",
"URL": null,
"raw_pages": "117-26",
"medline_journal": "Bioessays",
"ISO_journal": "Bioessays",
"authors": [
"Jentsch TJ",
"Gunther W."
],
"DOI_URL": "http://dx.doi.org/10.1002/bies.950190206"
},
"PUB00001999": {
"PMID": 7581380,
"ISBN": null,
"volume": "4",
"issue": "8",
"year": 1995,
"title": "Myotonia levior is a chloride channel disorder.",
"URL": null,
"raw_pages": "1397-402",
"medline_journal": "Hum Mol Genet",
"ISO_journal": "Hum. Mol. Genet.",
"authors": [
"Lehmann-Horn F",
"Mailander V",
"Heine R",
"George AL."
],
"DOI_URL": "http://dx.doi.org/10.1093/hmg/4.8.1397"
},
"PUB00004913": {
"PMID": 9207144,
"ISBN": null,
"volume": "94",
"issue": "14",
"year": 1997,
"title": "Transmembrane topology of a CLC chloride channel.",
"URL": null,
"raw_pages": "7633-8",
"medline_journal": "Proc Natl Acad Sci U S A",
"ISO_journal": "Proc. Natl. Acad. Sci. U.S.A.",
"authors": [
"Schmidt-Rose T",
"Jentsch TJ."
],
"DOI_URL": "http://dx.doi.org/10.1073/pnas.94.14.7633"
},
"PUB00155406": {
"PMID": 29845874,
"ISBN": null,
"volume": "98",
"issue": "3",
"year": 2018,
"title": "CLC Chloride Channels and Transporters: Structure, Function, Physiology, and Disease.",
"URL": null,
"raw_pages": "1493-1590",
"medline_journal": "Physiol Rev",
"ISO_journal": "Physiol Rev",
"authors": [
"Jentsch TJ",
"Pusch M."
],
"DOI_URL": "https://doi.org/10.1152/physrev.00047.2017"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR014743",
"name": "Chloride channel, core",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 1047,
"pathways": 0,
"proteins": 1047,
"proteomes": 181,
"sets": 0,
"structural_models": {
"alphafold": 958,
"bfvd": 0
},
"structures": 0,
"taxa": 646
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
