"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"
"PF08397"	"{'subfamilies': 0, 'domain_architectures': 96, 'interactions': 0, 'matches': 13143, 'pathways': 0, 'proteins': 12516, 'proteomes': 1320, 'sets': 1, 'structural_models': {'alphafold': 11009, 'bfvd': 0}, 'structures': 6, 'taxa': 4466}"	"{}"	"[{'text': '<p>The N-terminal predicted helical stretch of the insulin receptor tyrosine kinase substrate p53 (IRSp53) is an evolutionary conserved F-actin bundling domain involved in filopodium formation. The domain has been named IMD after the IRSp53 and missing in metastasis (MIM) proteins in which it occurs. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent [[cite:PUB00020898]].</p>', 'llm': False, 'checked': False, 'updated': False}]"	""	""	""	"IPR013606"	False	False	False	"{'PUB00020898': {'PMID': 14752106, 'ISBN': None, 'volume': '279', 'issue': '15', 'year': 2004, 'title': 'A novel actin bundling/filopodium-forming domain conserved in insulin receptor tyrosine kinase substrate p53 and missing in metastasis protein.', 'URL': None, 'raw_pages': '14929-36', 'medline_journal': 'J Biol Chem', 'ISO_journal': 'J. Biol. Chem.', 'authors': ['Yamagishi A', 'Masuda M', 'Ohki T', 'Onishi H', 'Mochizuki N.'], 'DOI_URL': 'http://dx.doi.org/10.1074/jbc.M309408200'}}"	""	"{'name': 'IRSp53/MIM homology domain', 'short': 'IMD'}"	""	"{'accession': '2d1l', 'name': 'Structure of F-actin binding domain IMD of MIM (Missing In Metastasis)'}"	"{'accession': 'CL0145', 'name': 'Golgi-transport'}"	"pfam"	"family"	"[{'title': 'IMD_domain', 'extract': '<p>In molecular biology, the <b>IMD domain</b> is a BAR-like domain of approximately 250 amino acids found at the N-terminus in the insulin receptor tyrosine kinase substrate p53 (IRSp53/BAIAP2) and in the evolutionarily related IRSp53/MIM (MTSS1) family. In IRSp53, a ubiquitous regulator of the actin cytoskeleton, the IMD domain acts as conserved F-actin bundling domain involved in filopodium formation. Filopodium-inducing IMD activity is regulated by Cdc42 and Rac1 and is SH3-independent. The IRSp53/MIM family is a novel F-actin bundling protein family that includes invertebrate relatives:</p><ul><li>Vertebrate MIM (MTSS1), an actin-binding scaffold protein that may be involved in cancer metastasis.</li>\n<li>Vertebrate ABBA-1 (MTSS1L), a MIM-related protein.</li>\n<li>Vertebrate brain-specific angiogenesis inhibitor 1-associated protein 2 or insulin receptor tyrosine kinase substrate p53 (IRSp53), a multifunctional adaptor protein that links Rac1 with a Wiskott–Aldrich syndrome family verprolin-homologous protein 2 (WAVE2/WASF2) to induce lamellipodia or Cdc42 with Mena to induce filopodia.</li>\n<li>Vertebrate brain-specific angiogenesis inhibitor 1-associated protein 2-like proteins 1 and 2.</li>\n<li><i>Drosophila melanogaster</i> CG32082-PA.</li>\n<li><i>Caenorhabditis elegans</i> M04F3.5 protein.</li></ul>', 'thumbnail': None}]"