Villin Epithelial cell-specific Ca(2+)-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination. Belongs to the villin/gelsolin family. Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes (at protein level). 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Actin-binding; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 1 C3|1 38.54 cM
Cellular Component:  actin filament bundle; brush border; cell projection; cytoplasm; cytoskeleton; filopodium; filopodium tip; lamellipodium; microvillus; plasma membrane; ruffle
Molecular Function:  actin binding; actin filament binding; calcium ion binding; cysteine-type endopeptidase inhibitor activity involved in apoptotic process; identical protein binding; lysophosphatidic acid binding; metal ion binding; phosphatidylinositol-4,5-bisphosphate binding; protein binding; protein homodimerization activity
Biological Process:  actin filament capping; actin filament depolymerization; actin filament polymerization; actin filament severing; actin nucleation; apoptotic process; barbed-end actin filament capping; cellular response to epidermal growth factor stimulus; cellular response to hepatocyte growth factor stimulus; cytoplasmic actin-based contraction involved in cell motility; cytoskeleton organization; epidermal growth factor receptor signaling pathway; intestinal D-glucose absorption; positive regulation of actin filament bundle assembly; positive regulation of actin filament depolymerization; positive regulation of cell migration; positive regulation of epithelial cell migration; positive regulation of lamellipodium morphogenesis; positive regulation of multicellular organism growth; positive regulation of protein localization to plasma membrane; regulation of actin nucleation; regulation of cell shape; regulation of lamellipodium morphogenesis; regulation of microvillus length; regulation of wound healing; response to bacterium; terminal web assembly
Reference #:  Q62468 (UniProtKB)
Alt. Names/Synonyms: MGC143974; OTTMUSP00000024309; Vil; Vil1; VILI; Villin; villin 1; Villin-1
Gene Symbols: Vil1
Molecular weight: 92,775 Da
Basal Isoelectric point: 5.72  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Villin

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene