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Protein Page:
Villin (human)

Overview
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. Monomer. Homodimer; homodimerization is necessary for actin-bundling. Associates with F-actin; phosphorylation at tyrosines residues decreases the association with F-actin. Interacts (phosphorylated at C-terminus tyrosine phosphorylation sites) with PLCG1 (via the SH2 domains). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF). Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes. Belongs to the villin/gelsolin family. Note: This description may include information from UniProtKB.
Protein type: Actin-binding; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 2q35
Cellular Component: actin filament bundle; brush border; filopodium; filopodium tip; lamellipodium; microvillus; nucleoplasm; plasma membrane; ruffle
Molecular Function: actin filament binding; calcium ion binding; caspase inhibitor activity; identical protein 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; barbed-end actin filament capping; epidermal growth factor receptor signaling pathway; epithelial cell differentiation; positive regulation of actin filament bundle formation; positive regulation of actin filament depolymerization; positive regulation of cell migration; protein complex assembly; regulation of actin nucleation; regulation of cell shape; response to bacterium
Reference #:  P09327 (UniProtKB)
Alt. Names/Synonyms: D2S1471; VIL; VIL1; VILI; villin 1; Villin-1
Gene Symbols: VIL1
Molecular weight: 92,695 Da
Basal Isoelectric point: 5.99  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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Villin

Protein Structure Not Found.
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