"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"IPR003128"	"{'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}"	"{'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'}]}}"	"[{'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}]"	""	"[{'identifier': 'GO:0003779', 'name': 'actin binding', 'category': {'code': 'F', 'name': 'molecular_function'}}, {'identifier': 'GO:0007010', 'name': 'cytoskeleton organization', 'category': {'code': 'P', 'name': 'biological_process'}}]"	"{'accession': 'IPR003128', 'name': 'Villin headpiece', 'type': 'Domain', 'children': []}"	""	False	False	False	"{'PUB00007540': {'PMID': 11977079, 'ISBN': None, 'volume': '52', 'issue': '1', 'year': 2002, 'title': 'Villin-type headpiece domains show a wide range of F-actin-binding affinities.', 'URL': None, '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': None, 'volume': '320', 'issue': '4', 'year': 2002, 'title': 'Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein.', 'URL': None, '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'}}"	"{'profile': {'PS51089': 'Headpiece (HP) domain profile'}, 'smart': {'SM00153': 'Villin headpiece domain'}, 'pfam': {'PF02209': 'Villin headpiece domain'}}"	"{'name': 'Villin headpiece', 'short': 'Villin_headpiece'}"	"[{'accession': 'IPR036886', 'name': 'Villin headpiece domain superfamily', 'type': 'homologous_superfamily'}]"	"{'accession': '1wy3', 'name': 'Chicken villin subdomain HP-35, K65(NLE), N68H, pH7.0'}"	""	"interpro"	"domain"	""