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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR002130",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0003755",
"name": "peptidyl-prolyl cis-trans isomerase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0000413",
"name": "protein peptidyl-prolyl isomerization",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"profile": {
"PS50072": "Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain profile"
},
"pfam": {
"PF00160": "Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD"
},
"prints": {
"PR00153": "CSAPPISMRASE"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR002130",
"name": "Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain",
"type": "Domain",
"children": [
{
"accession": "IPR035538",
"name": "PPIL4-like, cyclophilin domain",
"type": "Domain",
"children": []
}
]
},
"name": {
"name": "Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain",
"short": "Cyclophilin-type_PPIase_dom"
},
"description": [
{
"text": "<p>Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity ([ec:5.2.1.8]), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [[cite:PUB00017852], [cite:PUB00000320]]. They also have protein chaperone-like functions [[cite:PUB00021063]] and are the major high-affinity binding proteins for the immunosuppressive drug cyclosporin A (CSA) in vertebrates [[cite:PUB00017852]].</p>\r\n\r\n<p>Cyclophilins are found in all prokaryotes and eukaryotes, and have been structurally conserved throughout evolution, implying their importance in cellular function [[cite:PUB00056846]]. They share a common 109 amino acid cyclophilin-like domain (CLD) and additional domains unique to each member of the family. The CLD domain contains the PPIase activity, while the unique domains are important for selection of protein substrates and subcellular compartmentalisation [[cite:PUB00056847]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This entry represents the core β-barrel cyclophilin-like domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00021063": {
"PMID": 15998457,
"ISBN": null,
"volume": "6",
"issue": "7",
"year": 2005,
"title": "The cyclophilins.",
"URL": null,
"raw_pages": "226",
"medline_journal": "Genome Biol",
"ISO_journal": "Genome Biol.",
"authors": [
"Wang P",
"Heitman J."
],
"DOI_URL": "http://dx.doi.org/10.1186/gb-2005-6-7-226"
},
"PUB00000320": {
"PMID": 2186809,
"ISBN": null,
"volume": "29",
"issue": "9",
"year": 1990,
"title": "The mechanism of protein folding. Implications of in vitro refolding models for de novo protein folding and translocation in the cell.",
"URL": null,
"raw_pages": "2205-12",
"medline_journal": "Biochemistry",
"ISO_journal": "Biochemistry",
"authors": [
"Fischer G",
"Schmid FX."
],
"DOI_URL": "http://dx.doi.org/10.1021/bi00461a001"
},
"PUB00017852": {
"PMID": 14731520,
"ISBN": null,
"volume": "2",
"issue": "9",
"year": 1992,
"title": "Cyclophilins: a new family of proteins involved in intracellular folding.",
"URL": null,
"raw_pages": "272-6",
"medline_journal": "Trends Cell Biol",
"ISO_journal": "Trends Cell Biol.",
"authors": [
"Stamnes MA",
"Rutherford SL",
"Zuker CS."
],
"DOI_URL": "http://dx.doi.org/10.1016/0962-8924(92)90200-7"
},
"PUB00056846": {
"PMID": 21309470,
"ISBN": null,
"volume": "38",
"issue": "5",
"year": 2010,
"title": "An overview of cyclophilins in human cancers.",
"URL": null,
"raw_pages": "1561-74",
"medline_journal": "J Int Med Res",
"ISO_journal": "J. Int. Med. Res.",
"authors": [
"Lee J",
"Kim SS."
],
"DOI_URL": null
},
"PUB00056847": {
"PMID": 21295323,
"ISBN": null,
"volume": "411",
"issue": "2",
"year": 2011,
"title": "Emerging picture of host chaperone and cyclophilin roles in RNA virus replication.",
"URL": null,
"raw_pages": "374-82",
"medline_journal": "Virology",
"ISO_journal": "Virology",
"authors": [
"Nagy PD",
"Wang RY",
"Pogany J",
"Hafren A",
"Makinen K."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.virol.2010.12.061"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029000",
"name": "Cyclophilin-like domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 1553,
"interactions": 1,
"matches": 132919,
"pathways": 96,
"proteins": 132603,
"proteomes": 20459,
"sets": 0,
"structural_models": {
"alphafold": 109251,
"bfvd": 4
},
"structures": 484,
"taxa": 40512
},
"entry_annotations": {
"alignment:seed": 55,
"alignment:full": 71714
},
"cross_references": {
"prositedoc": {
"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC00154",
"url": "http://prosite.expasy.org/PDOC00154"
}
]
},
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "5.2.1.8",
"url": "https://enzyme.expasy.org/EC/5.2.1.8"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1lop",
"name": "CYCLOPHILIN A COMPLEXED WITH SUCCINYL-ALA-PRO-ALA-P-NITROANILIDE"
}
}
}
