Villin 1

Villin 1 is a protein that in humans is encoded by the VIL1 gene. <ref name="entrez {{cite web | title = Entrez Gene: Villin 1 | url = https://www.ncbi.nlm.nih.gov/gene/7429 | access-date = 2018-09-27 }}</ref>

VIL1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1UNC, 3FG7
Identifiers
Aliases	VIL1, D2S1471, VIL, villin 1
External IDs	OMIM: 193040; MGI: 98930; HomoloGene: 5169; GeneCards: VIL1; OMA:VIL1 - orthologs
Gene location (Human) Chr. Chromosome 2 (human) Band 2q35 Start 218,419,121 bp End 218,453,295 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 C3|1 38.54 cM Start 74,448,535 bp End 74,474,718 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa mucosa of ileum mucosa of transverse colon rectum duodenum mucosa of sigmoid colon buccal mucosa cell gallbladder secondary oocyte islet of Langerhans Top expressed in ileum intestinal villus epithelium of small intestine Ileal epithelium crypt of lieberkuhn of small intestine colon left colon duodenum jejunum Paneth cell More reference expression data BioGPS n/a
Gene ontology Molecular function lysophosphatidic acid binding calcium ion binding protein homodimerization activity cysteine-type endopeptidase inhibitor activity involved in apoptotic process actin filament binding protein binding identical protein binding actin binding phosphatidylinositol-4,5-bisphosphate binding Cellular component cytoplasm cell projection filopodium ruffle plasma membrane nucleoplasm microvillus filopodium tip brush border actin filament bundle extracellular exosome cytoskeleton lamellipodium Biological process negative regulation of cysteine-type endopeptidase activity involved in apoptotic process actin nucleation positive regulation of lamellipodium morphogenesis cytoplasmic actin-based contraction involved in cell motility epithelial cell differentiation epidermal growth factor receptor signaling pathway response to bacterium positive regulation of cell migration cellular response to hepatocyte growth factor stimulus actin filament depolymerization actin filament severing barbed-end actin filament capping positive regulation of epithelial cell migration regulation of lamellipodium morphogenesis terminal web assembly cellular response to epidermal growth factor stimulus actin filament polymerization regulation of wound healing cytoskeleton organization actin filament capping regulation of cell shape positive regulation of multicellular organism growth intestinal D-glucose absorption positive regulation of actin filament bundle assembly regulation of microvillus length regulation of actin nucleation positive regulation of actin filament depolymerization apoptotic process positive regulation of protein localization to plasma membrane protein-containing complex assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7429 22349 Ensembl ENSG00000127831 ENSMUSG00000026175 UniProt P09327 Q62468 RefSeq (mRNA) NM_007127 NM_009509 RefSeq (protein) NP_009058 NP_033535 Location (UCSC) Chr 2: 218.42 – 218.45 Mb Chr 1: 74.45 – 74.47 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a member of a family of calcium-regulated actin-binding proteins. This protein represents a dominant part of the brush border cytoskeleton which functions in the capping, severing, and bundling of actin filaments. Two mRNAs of 2.7 kb and 3.5 kb have been observed; they result from utilization of alternate poly-adenylation signals present in the terminal exon. [provided by RefSeq, Jul 2008].

Further reading

• Zhai L, Zhao P, Panebra A, Guerrerio AL, Khurana S (September 2001). "Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton". J. Biol. Chem. 276 (39): 36163–7. doi:10.1074/jbc.C100418200. PMID 11500485.
• Kumar N, Tomar A, Parrill AL, Khurana S (October 2004). "Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin". J. Biol. Chem. 279 (43): 45036–46. doi:10.1074/jbc.M405424200. PMID 15272027.
• Tomar A, Wang Y, Kumar N, George S, Ceacareanu B, Hassid A, Chapman KE, Aryal AM, Waters CM, Khurana S (November 2004). "Regulation of cell motility by tyrosine phosphorylated villin". Mol. Biol. Cell. 15 (11): 4807–17. doi:10.1091/mbc.e04-05-0431. PMC 524729. PMID 15342783.
• Rieder G, Tessier AJ, Qiao XT, Madison B, Gumucio DL, Merchant JL (February 2005). "Helicobacter-induced intestinal metaplasia in the stomach correlates with Elk-1 and serum response factor induction of villin". J. Biol. Chem. 280 (6): 4906–12. doi:10.1074/jbc.M413399200. PMID 15576363.
• Revenu C, Courtois M, Michelot A, Sykes C, Louvard D, Robine S (March 2007). "Villin severing activity enhances actin-based motility in vivo". Mol. Biol. Cell. 18 (3): 827–38. doi:10.1091/mbc.e06-05-0423. PMC 1805090. PMID 17182858.
• Khurana S, Tomar A, George SP, Wang Y, Siddiqui MR, Guo H, Tigyi G, Mathew S (February 2008). "Autotaxin and lysophosphatidic acid stimulate intestinal cell motility by redistribution of the actin modifying protein villin to the developing lamellipodia". Exp. Cell Res. 314 (3): 530–42. doi:10.1016/j.yexcr.2007.10.028. PMC 2680351. PMID 18054784.
• Khurana S, George SP (June 2008). "Regulation of cell structure and function by actin-binding proteins: villin's perspective". FEBS Lett. 582 (14): 2128–39. doi:10.1016/j.febslet.2008.02.040. PMC 2680319. PMID 18307996.
• Yamamichi N, Inada K, Furukawa C, Sakurai K, Tando T, Ishizaka A, Haraguchi T, Mizutani T, Fujishiro M, Shimomura R, Oka M, Ichinose M, Tsutsumi Y, Omata M, Iba H (June 2009). "Cdx2 and the Brm-type SWI/SNF complex cooperatively regulate villin expression in gastrointestinal cells". Exp. Cell Res. 315 (10): 1779–89. doi:10.1016/j.yexcr.2009.01.006. PMID 19371634.
• Nakamura E, Iwakawa M, Furuta R, Ohno T, Satoh T, Nakawatari M, Ishikawa K, Imadome K, Michikawa Y, Tamaki T, Kato S, Kitagawa T, Imai T (June 2009). "Villin1, a novel diagnostic marker for cervical adenocarcinoma". Cancer Biol. Ther. 8 (12): 1146–53. doi:10.4161/cbt.8.12.8477. PMID 19377296.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.