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{
"metadata": {
"accession": "IPR025521",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF14365": "Neprosin activation peptide"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR025521",
"name": "Neprosin activation peptide",
"type": "Domain",
"children": []
},
"name": {
"name": "Neprosin activation peptide",
"short": "Neprosin_propep"
},
"description": [
{
"text": "<p>Pitcher plants are insectivorous and secrete a digestive fluid into the pitcher. This fluid contains a mixture of enzymes, including peptidases. One of these is neprosin, characterised by the pitcher plant Nepenthes ventrata. Neprosin is a glutamic endopeptidase that preferentially cleaves peptide bonds on the C-terminal side of proline residues [[cite:PUB00081922], [cite:PUB00151162], [cite:PUB00151161]]. In contrast to most proline-cleaving enzymes, it effectively degrades proteins of any size [[cite:PUB00151161]]. The peptidase is secreted and is presumed to possess an N-terminal activation peptide [[cite:PUB00081922]] which is represented in this entry.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00151162": {
"PMID": 35915115,
"ISBN": null,
"volume": "13",
"issue": "1",
"year": 2022,
"title": "Molecular and in vivo studies of a glutamate-class prolyl-endopeptidase for coeliac disease therapy.",
"URL": null,
"raw_pages": "4446",
"medline_journal": "Nat Commun",
"ISO_journal": "Nat Commun",
"authors": [
"Del Amo-Maestro L",
"Mendes SR",
"Rodriguez-Banqueri A",
"Garzon-Flores L",
"Girbal M",
"Rodriguez-Lagunas MJ",
"Guevara T",
"Franch A",
"Perez-Cano FJ",
"Eckhard U",
"Gomis-Ruth FX."
],
"DOI_URL": null
},
"PUB00151161": {
"PMID": 28404794,
"ISBN": null,
"volume": "16",
"issue": "6",
"year": 2017,
"title": "Neprosin, a Selective Prolyl Endoprotease for Bottom-up Proteomics and Histone Mapping.",
"URL": null,
"raw_pages": "1162-1171",
"medline_journal": "Mol Cell Proteomics",
"ISO_journal": "Mol Cell Proteomics",
"authors": [
"Schrader CU",
"Lee L",
"Rey M",
"Sarpe V",
"Man P",
"Sharma S",
"Zabrouskov V",
"Larsen B",
"Schriemer DC."
],
"DOI_URL": null
},
"PUB00081922": {
"PMID": 27481162,
"ISBN": null,
"volume": "6",
"issue": null,
"year": 2016,
"title": "Addressing proteolytic efficiency in enzymatic degradation therapy for celiac disease.",
"URL": null,
"raw_pages": "30980",
"medline_journal": "Sci Rep",
"ISO_journal": "Sci Rep",
"authors": [
"Rey M",
"Yang M",
"Lee L",
"Zhang Y",
"Sheff JG",
"Sensen CW",
"Mrazek H",
"Halada P",
"Man P",
"McCarville JL",
"Verdu EF",
"Schriemer DC."
],
"DOI_URL": "http://dx.doi.org/10.1038/srep30980"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 178,
"interactions": 0,
"matches": 9466,
"pathways": 0,
"proteins": 9197,
"proteomes": 363,
"sets": 0,
"structural_models": {
"alphafold": 7860,
"bfvd": 0
},
"structures": 3,
"taxa": 1086
},
"entry_annotations": {
"alignment:seed": 82,
"alignment:full": 5033
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}