HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "IPR003128",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0003779",
"name": "actin binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0007010",
"name": "cytoskeleton organization",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"profile": {
"PS51089": "Headpiece (HP) domain profile"
},
"smart": {
"SM00153": "Villin headpiece domain"
},
"pfam": {
"PF02209": "Villin headpiece domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR003128",
"name": "Villin headpiece",
"type": "Domain",
"children": []
},
"name": {
"name": "Villin headpiece",
"short": "Villin_headpiece"
},
"description": [
{
"text": "<p>Villin is an F-actin bundling protein involved in the maintenance of the microvilli of the absorptive epithelia. The villin-type \"headpiece\" domain is a modular motif found at the extreme C terminus of larger \"core\" domains in over 25 cytoskeletal proteins in plants and animals, often in assocation with the Gelsolin repeat. Although the headpiece is classified as an F-actin-binding domain, it has been shown that not all headpiece domains are intrinsically F-actin-binding motifs, surface charge distribution may be an important element for F-actin recognition [[cite:PUB00007540]]. An autonomously folding, 35 residue, thermostable subdomain (HP36) of the full-length 76 amino acid residue villin headpiece, is the smallest known example of a cooperatively folded domain of a naturally occurring protein. The structure of HP36, as determined by NMR spectroscopy, consists of three short helices surrounding a tightly packed hydrophobic core [[cite:PUB00007541]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00007540": {
"PMID": 11977079,
"ISBN": null,
"volume": "52",
"issue": "1",
"year": 2002,
"title": "Villin-type headpiece domains show a wide range of F-actin-binding affinities.",
"URL": null,
"raw_pages": "9-21",
"medline_journal": "Cell Motil Cytoskeleton",
"ISO_journal": "Cell Motil. Cytoskeleton",
"authors": [
"Vardar D",
"Chishti AH",
"Frank BS",
"Luna EJ",
"Noegel AA",
"Oh SW",
"Schleicher M",
"McKnight CJ."
],
"DOI_URL": "http://dx.doi.org/10.1002/cm.10027"
},
"PUB00007541": {
"PMID": 12095260,
"ISBN": null,
"volume": "320",
"issue": "4",
"year": 2002,
"title": "Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein.",
"URL": null,
"raw_pages": "841-54",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Vugmeyster L",
"Trott O",
"McKnight CJ",
"Raleigh DP",
"Palmer AG 3rd."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0022-2836(02)00537-5"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036886",
"name": "Villin headpiece domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 256,
"interactions": 0,
"matches": 21490,
"pathways": 8,
"proteins": 21487,
"proteomes": 1776,
"sets": 0,
"structural_models": {
"alphafold": 15560,
"bfvd": 0
},
"structures": 57,
"taxa": 6050
},
"entry_annotations": {
"alignment:seed": 170,
"alignment:full": 14392
},
"cross_references": {
"prositedoc": {
"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC51089",
"url": "http://prosite.expasy.org/PDOC51089"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "1wy3",
"name": "Chicken villin subdomain HP-35, K65(NLE), N68H, pH7.0"
}
}
}
