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Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
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{
"metadata": {
"accession": "IPR010600",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0004867",
"name": "serine-type endopeptidase inhibitor activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0030212",
"name": "hyaluronan metabolic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF06668": "Inter-alpha-trypsin inhibitor heavy chain C-terminus"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR010600",
"name": "Inter-alpha-trypsin inhibitor heavy chain, C-terminal",
"type": "Domain",
"children": []
},
"name": {
"name": "Inter-alpha-trypsin inhibitor heavy chain, C-terminal",
"short": "ITI_HC_C"
},
"description": [
{
"text": "<p>This entry represents the C-terminal region of inter-alpha-trypsin inhibitor heavy chains. Inter-alpha-trypsin inhibitors are glycoproteins with a high inhibitory activity against trypsin, built up from different combinations of four polypeptides: bikunin and the three heavy chains that belong to this family (HC1, HC2, HC3). The heavy chains do not have any protease inhibitory properties but have the capacity to interact<i>in vitro</i>and<i>in vivo</i>with hyaluronic acid, which promotes the stability of the extra-cellular matrix. This domain is associated with the VWA domain [interpro:IPR002035].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": null,
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 67,
"interactions": 0,
"matches": 5605,
"pathways": 10,
"proteins": 5512,
"proteomes": 789,
"sets": 0,
"structural_models": {
"alphafold": 5058,
"bfvd": 0
},
"structures": 2,
"taxa": 2586
},
"entry_annotations": {
"alignment:seed": 50,
"alignment:full": 4228
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}