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{
"metadata": {
"accession": "IPR000519",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd00111": "Trefoil"
},
"profile": {
"PS51448": "P-type Trefoil domain profile"
},
"pfam": {
"PF00088": "Trefoil (P-type) domain"
},
"smart": {
"SM00018": "P or trefoil or TFF domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR000519",
"name": "P-type trefoil domain",
"type": "Domain",
"children": []
},
"name": {
"name": "P-type trefoil domain",
"short": "P_trefoil_dom"
},
"description": [
{
"text": "<p>A cysteine-rich domain of approximately forty five amino-acid residues has been found in some extracellular eukaryotic proteins [[cite:PUB00001033], [cite:PUB00001707], [cite:PUB00005012], [cite:PUB00005400]]. It is known as either the 'P', 'trefoil' or 'TFF' domain, and contains six cysteines linked by three disulphide bonds with connectivity 1-5, 2-4, 3-6. This leads to a characteristic three leafed structure ('trefoil'). The P-type domain is clearly composed of three looplike regions. The central core of the domain consists of a short two-stranded antiparallel β-sheet, which is capped by an irregular loop and forms a central hairpin (loop 3). The β-sheet is preceded by a short α-helix, with majority of the remainder of the domain contained in two loops, which lie on either side of the central hairpin.</p>\n\n<p>This domain has been found in a variety of extracellular eukaryotic proteins [[cite:PUB00001033], [cite:PUB00005012], [cite:PUB00005400]], including:</p>\n\n<ul>\n<li>Protein pS2 (TFF1), a protein secreted by the stomach mucosa</li>\n<li>Spasmolytic polypeptide (SP) (TFF2), a protein of about 115 residues that inhibits gastrointestinal motility and gastric acid secretion</li>\n<li>Intestinal trefoil factor (ITF) (TFF3)</li>\n<li>Xenopus laevis stomach proteins xP1 and xP4</li>\n<li>Xenopus integumentary mucins A.1 (FIM-A.1 or preprospasmolysin) and C.1 (FIM-C.1), proteins which may be involved in defence against microbial infections by protecting the epithelia from the external environment</li>\n<li>Xenopus skin protein xp2 (or APEG)</li>\n<li>Zona pellucida sperm-binding protein B (ZP-B)</li>\n<li>Intestinal sucrase-isomaltase ([ec:3.2.1.48] / [ec:3.2.1.10]), a vertebrate membrane bound, multifunctional enzyme complex which hydrolyses sucrose, maltose and isomaltose</li>\n<li>Lysosomal alpha-glucosidase ([ec:3.2.1.20])</li>\n</ul>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00001707": {
"PMID": 9187350,
"ISBN": null,
"volume": "408",
"issue": "2",
"year": 1997,
"title": "Rolling in the clover: trefoil factor family (TFF)-domain peptides, cell migration and cancer.",
"URL": null,
"raw_pages": "121-3",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Wright NA",
"Hoffmann W",
"Otto WR",
"Rio MC",
"Thim L."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0014-5793(97)00424-9"
},
"PUB00005012": {
"PMID": 8518738,
"ISBN": null,
"volume": "2",
"issue": "4",
"year": 1993,
"title": "A trefoil domain in the major rabbit zona pellucida protein.",
"URL": null,
"raw_pages": "669-70",
"medline_journal": "Protein Sci",
"ISO_journal": "Protein Sci.",
"authors": [
"Bork P."
],
"DOI_URL": "http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=8518738"
},
"PUB00005400": {
"PMID": 8267796,
"ISBN": null,
"volume": "18",
"issue": "7",
"year": 1993,
"title": "The P-domain or trefoil motif: a role in renewal and pathology of mucous epithelia?",
"URL": null,
"raw_pages": "239-43",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Hoffmann W",
"Hauser F."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(93)90170-R"
},
"PUB00001033": {
"PMID": 7820556,
"ISBN": null,
"volume": "4",
"issue": "9",
"year": 1994,
"title": "Trefoil peptides. Coming up clover.",
"URL": null,
"raw_pages": "835-8",
"medline_journal": "Curr Biol",
"ISO_journal": "Curr. Biol.",
"authors": [
"Otto B",
"Wright N."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0960-9822(00)00186-X"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR044913",
"name": "P-type trefoil domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 561,
"interactions": 0,
"matches": 15487,
"pathways": 17,
"proteins": 11758,
"proteomes": 1369,
"sets": 0,
"structural_models": {
"alphafold": 8848,
"bfvd": 0
},
"structures": 45,
"taxa": 4810
},
"entry_annotations": {
"alignment:seed": 172,
"alignment:full": 10134
},
"cross_references": {
"prositedoc": {
"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC00024",
"url": "http://prosite.expasy.org/PDOC00024"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "2psp",
"name": "Porcine pancreatic spasmolytic polypeptide"
}
}
}
