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{
"metadata": {
"accession": "PF01992",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "pfam",
"member_databases": null,
"integrated": "IPR002843",
"hierarchy": null,
"name": {
"name": "ATP synthase (C/AC39) subunit",
"short": "vATP-synt_AC39"
},
"description": [
{
"text": "<p>This family includes the AC39 subunit from vacuolar ATP synthase [swissprot:P32366] [[cite:PUB00005711]], and the C subunit from archaebacterial ATP synthase [[cite:PUB00002959]]. The family also includes subunit C from the Sodium transporting ATP synthase from Enterococcus hirae [swissprot:P43456] [[cite:PUB00005718]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": [
{
"title": "V-ATPase",
"extract": "<p><b>Vacuolar-type ATPase</b> (<b>V-ATPase</b>) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.</p>",
"thumbnail": null
}
],
"literature": {
"PUB00005718": {
"PMID": 8157629,
"ISBN": null,
"volume": "269",
"issue": "15",
"year": 1994,
"title": "Sequencing and characterization of the ntp gene cluster for vacuolar-type Na(+)-translocating ATPase of Enterococcus hirae.",
"URL": null,
"raw_pages": "11037-44",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Takase K",
"Kakinuma S",
"Yamato I",
"Konishi K",
"Igarashi K",
"Kakinuma Y."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/269/15/11037"
},
"PUB00002959": {
"PMID": 8702544,
"ISBN": null,
"volume": "271",
"issue": "31",
"year": 1996,
"title": "Subunit structure and organization of the genes of the A1A0 ATPase from the Archaeon Methanosarcina mazei Go1.",
"URL": null,
"raw_pages": "18843-52",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Wilms R",
"Freiberg C",
"Wegerle E",
"Meier I",
"Mayer F",
"Muller V."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.271.31.18843"
},
"PUB00005711": {
"PMID": 8509410,
"ISBN": null,
"volume": "268",
"issue": "17",
"year": 1993,
"title": "The Saccharomyces cerevisiae VMA6 gene encodes the 36-kDa subunit of the vacuolar H(+)-ATPase membrane sector.",
"URL": null,
"raw_pages": "12749-57",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Bauerle C",
"Ho MN",
"Lindorfer MA",
"Stevens TH."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/268/17/12749"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 76,
"interactions": 0,
"matches": 9768,
"pathways": 0,
"proteins": 9571,
"proteomes": 5033,
"sets": 0,
"structural_models": {
"alphafold": 8588,
"bfvd": 0
},
"structures": 95,
"taxa": 13624
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 217,
"alignment:full": 5562
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1v9m",
"name": "Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus"
}
}
}
