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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: Motility/polarity/chemotaxis; Actin binding protein Cellular Component: ruffle; filopodium tip; microvillus; lamellipodium; cytoplasm; actin filament bundle; filopodium Molecular Function: actin filament binding; identical protein binding; protein binding; phosphatidylinositol-4,5-bisphosphate binding; protein homodimerization activity; caspase inhibitor activity; calcium ion binding Biological Process: epidermal growth factor receptor signaling pathway; regulation of cell shape; actin filament severing; actin filament depolymerization; response to bacterium; actin filament polymerization; actin filament capping; regulation of actin nucleation; positive regulation of actin filament bundle formation; protein complex assembly; positive regulation of cell migration 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®

Select Structure to View Below villin 1UNC - A=793-827 (human) 3FG7 - A/B=360-720 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1UNC 3FG7  |  Phospho3D  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  Ensembl Protein

	Sites Implicated In
cell motility, altered: Y286‑p cytoskeletal reorganization: Y46‑p, Y60‑p, Y64‑p, Y81‑p, Y256‑p, Y286‑p intracellular localization: Y60‑p, Y81‑p, Y256‑p molecular association, regulation: Y60‑p, Y81‑p, Y256‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		T2-p	______MtKLsAQVK
0	1		S5-p	___MtKLsAQVKGSL
0	1		T15-p	VKGSLNItTPGLQIW
0	1		S39	VPSSTFGSFFDGDCy
2	1		Y46-p	SFFDGDCyIILAIHK
3	0		Y60-p	KTASSLSyDIHyWIG
1	0		Y64-p	SLSyDIHyWIGQDSS
3	0		Y81-p	EQGAAAIyTTQMDDF
0	1		K119-a	KQGLVIRkGGVASGM
0	3		Y134-p	KHVETNSyDVQRLLH
0	2		T206-p	DQERGGRtyVGVVDG
0	2		Y207-p	QERGGRtyVGVVDGE
0	2		K237-u	LGKRRELkAAVPDTV
0	1		K250	TVVEPALKAALKLyH
2	0		Y256-p	LKAALKLyHVSDSEG
0	1		N264	HVSDSEGNLVVREVA
0	1		S281	PLTQDLLSHEDCyIL
1	0		Y286-p	LLSHEDCyILDQGGL
0	1		K320	SHALNFIKAKQyPPS
1	0		Y324-p	NFIKAKQyPPSTQVE
0	1		T350	QQLFQKWTASNRTsG
0	1		S356-p	WTASNRTsGLGKTHT
1	0		Y461-p	DEITASAyQAVILDQ
0	1		T506	YQGGTSRTNNLETGP
0	3		K529-u	GTGANNTkAFEVPAR
1	0		Y555-p	LKTQSCCyLWCGKGC
1	0		Y604-p	ALGGKAPyANTKRLQ
0	1		K672	HANEEEKKAAATTAQ
0	1		Y681-p	AATTAQEyLKTHPSG
0	1		K683	TTAQEyLKTHPSGRD
1	0		Y725-p	KWSNTKSyEDLkAEL
0	1		K729-a	TKSyEDLkAELGNSR
0	1		S735	LkAELGNSRDWSQIT
0	1		P776	LEQLVNKPVEELPEG

	mouse
T2	______MTKLNAQVK
N5	___MTKLNAQVKGSL
T15	VKGSLNITTPGIQIW
S39-p	VPSSTFGsFFDGDCy
Y46-p	sFFDGDCyVVLAIHK
Y60	KTSSTLSYDIHYWIG
Y64	TLSYDIHYWIGQDSS
Y81	EQGAAAIYTTQMDDY
K119	KQGLVIRKGGVASGM
C134	KHVETNSCDVQRLLH
T206	DQERGGRTYVGVVDG
Y207	QERGGRTYVGVVDGE
K237-u	LGPRKELkAAISDSV
K250-u	SVVEPAAkAALKLYH
Y256	AkAALKLYHVSDSEG
K264-u	HVSDSEGkLVVREVA
K281-u	PLTQDLLkHEDCYIL
Y286	LLkHEDCYILDQGGL
K320-u	SQALNFIkAKQYPPS
Y324	NFIkAKQYPPSTQVE
T350-p	QQLFQKWtVPNRTSG
S356	WtVPNRTSGLGKTHT
Y461	DEIAASAYQAVLLDQ
K506-u	YQGGTSRkNNLEPVP
K529-u	GTNADNTkAFEVTAR
Y555	LKTPSCCYLWCGKGC
Y604	ALGGKAPYANTKRLQ
K672-u	HANEEEKkAAATTVQ
Y681	AATTVQEYLkTHPGN
K683-u	TTVQEYLkTHPGNRD
Y725	KWSNTKSYDDLKAEL
K729	TKSYDDLKAELGNsG
S735-p	LKAELGNsGDWSQIA
S776-p	LEQLVNKsVEDLPEG

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