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InterPro-Version: 104.0
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{
"metadata": {
"accession": "IPR023302",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0004252",
"name": "serine-type endopeptidase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF02897": "Prolyl oligopeptidase, N-terminal beta-propeller domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR023302",
"name": "Peptidase S9A, N-terminal domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Peptidase S9A, N-terminal domain",
"short": "Pept_S9A_N"
},
"description": [
{
"text": "<p>This entry represents the β-propeller domain found at the N-terminal of prolyl oligopeptidase from the MEROPS peptidase family S9A. The prolyl oligopeptidase family consist of a number of evolutionary related peptidases whose catalytic activity seems to be provided by a charge relay system similar to that of the trypsin family of serine proteases, but which evolved by independent convergent evolution. The N-terminal domain of prolyl oligopeptidases form an unusual 7-bladed β-propeller consisting of seven 4-stranded β-sheet motifs.</p>\r\n<p>Prolyl oligopeptidase is a large cytosolic enzyme involved in the maturation and degradation of peptide hormones and neuropeptides, which relate to the induction of amnesia. The enzyme contains a peptidase domain, where its catalytic triad (Ser554, His680, Asp641) is covered by the central tunnel of the N-terminal β-propeller domain. In this way, large structured peptides are excluded from the active site, thereby protecting larger peptides and proteins from proteolysis in the cytosol [[cite:PUB00020062]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00020062": {
"PMID": 9695945,
"ISBN": null,
"volume": "94",
"issue": "2",
"year": 1998,
"title": "Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis.",
"URL": null,
"raw_pages": "161-70",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Fulop V",
"Bocskei Z",
"Polgar L."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0092-8674(00)81416-6"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029058",
"name": "Alpha/Beta hydrolase fold",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 230,
"interactions": 0,
"matches": 43760,
"pathways": 1,
"proteins": 43020,
"proteomes": 6508,
"sets": 0,
"structural_models": {
"alphafold": 31686
},
"structures": 81,
"taxa": 25096
},
"entry_annotations": {
"alignment:seed": 30,
"alignment:full": 13364
},
"cross_references": {
"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": "3.4.14.-",
"url": "https://enzyme.expasy.org/EC/3.4.14.-"
},
{
"accession": "3.4.21.-",
"url": "https://enzyme.expasy.org/EC/3.4.21.-"
},
{
"accession": "3.4.21.26",
"url": "https://enzyme.expasy.org/EC/3.4.21.26"
},
{
"accession": "3.4.21.83",
"url": "https://enzyme.expasy.org/EC/3.4.21.83"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "7ne5",
"name": "catalytically non active S532A mutant of oligopeptidase B from S. proteomaculans with modified hinge region"
}
}
}