{"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"}}}