Villin-1 (Protein name
), VILI_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Predicted Eptitope
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Vaild Sequence
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Gene name:
VIL1(VIL);
Protein name:
Villin-1;
Alternative:
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
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).
Function:
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.
Subcellular Location:
Cytoplasm
cytoskeleton
Cell projection
lamellipodium
Cell projection
ruffle
Cell projection
microvillus
Cell projection
filopodium tip
Cell projection
filopodium
Relocalized in the tip of cellular protrusions and filipodial extensions upon infection with S.flexneri in primary intestinal epithelial cells (IEC) and in the tail-like structures forming the actin comets of S.flexneri. Redistributed to the leading edge of hepatocyte growth factor (HGF)-induced lamellipodia (By similarity). Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);PROTEIN SEQUENCE OF 2-13
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 718-827 (ISOFORM 1);TISSUE SPECIFICITY
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Cited for: FUNCTION;ASSOCIATION WITH F-ACTIN;PHOSPHORYLATION
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Cited for: PHOSPHORYLATION BY SRC;PHOSPHORYLATION AT TYROSINE RESIDUES;MUTAGENESIS OF TYR-46; TYR-60; TYR-81 AND TYR-256
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Cited for: POSSIBLE INVOLVEMENT IN BILIARY ATRESIA;TISSUE SPECIFICITY
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Cited for: FUNCTION;INTERACTION WITH PHOSPHATIDYLINOSITOL;MUTAGENESIS OF ARG-138; LYS-145; ARG-146; LYS-822 AND LYS-824
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Cited for: FUNCTION;CALCIUM-BINDING;MUTAGENESIS OF GLU-25; ASP-44; ASP-61; GLU-74; ASP-86 AND ALA-93
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Cited for: FUNCTION;MUTAGENESIS OF TYR-46; TYR-60; TYR-81 AND TYR-256;SUBCELLULAR LOCATION
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Cited for: FUNCTION;INTERACTION WITH PLCG1;PHOSPHORYLATION AT TYROSINE RESIDUES;MUTAGENESIS OF TYR-46; TYR-60; TYR-81; TYR-256; TYR-286; TYR-324; TYR-461; TYR-555; TYR-604 AND TYR-725;SUBCELLULAR LOCATION
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Cited for: FUNCTION;INTERACTION WITH PLCG1;PHOSPHORYLATION AT TYROSINE RESIDUES;MUTAGENESIS OF TYR-46; TYR-60; TYR-81; TYR-256; TYR-286; TYR-324; TYR-461; TYR-555; TYR-604 AND TYR-725;SUBCELLULAR LOCATION
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Cited for: FUNCTION;MUTAGENESIS OF ASP-61; GLU-74; 86-ASP--GLY-91 AND 125-GLY--VAL-129;SUBCELLULAR LOCATION
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Cited for: FUNCTION;MUTAGENESIS OF TYR-46; TYR-60; TYR-81; TYR-256; TYR-286; TYR-324; TYR-461; TYR-555; TYR-604 AND TYR-725;SUBCELLULAR LOCATION
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Cited for: FUNCTION;INTERACTION WITH LYSOPHOSPHATIDIC ACID;ASSOCIATION WITH F-ACTIN;SUBCELLULAR LOCATION
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: STRUCTURE BY NMR OF 793-827;ASSOCIATION WITH F-ACTIN;MUTAGENESIS OF TRP-815
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Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 360-720
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Vaild Sequence:
