Vil1 villin 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Vil1provided by MGI
Official Full Name: villin 1provided by MGI
Primary source: MGI:MGI:98930
See related: Ensembl:ENSMUSG00000026175 AllianceGenome:MGI:98930
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Vil
Summary: Enables cysteine-type endopeptidase inhibitor activity involved in apoptotic process. Involved in several processes, including cellular response to hepatocyte growth factor stimulus; intestinal D-glucose absorption; and regulation of plasma membrane bounded cell projection organization. Located in several cellular components, including brush border; filopodium tip; and lamellipodium. Is expressed in several structures, including brain; egg cylinder; gut; metanephros; and reproductive system. Orthologous to human VIL1 (villin 1). [provided by Alliance of Genome Resources, Apr 2022]
Expression: Biased expression in large intestine adult (RPKM 318.1), small intestine adult (RPKM 235.7) and 4 other tissues See more
Orthologs: human all
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Genomic context

Location:: 1 C3; 1 38.54 cM

Exon count:: 20

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	1	NC_000067.7 (74448543..74474719)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	1	NC_000067.6 (74409384..74435560)

Chromosome 1 - NC_000067.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Mouse intestinal tuft cells express advillin but not villin.
Title: Mouse intestinal tuft cells express advillin but not villin.
Induction of cell stress alters the actin cytoskeleton in intestinal epithelial cells via changes in the actin-binding proteins villin-1 and gelsolin.
Title: Villin-1 and Gelsolin Regulate Changes in Actin Dynamics That Affect Cell Survival Signaling Pathways and Intestinal Inflammation.
This study also highlights the potential role of villin's pro-apoptotic function in the pathogenesis of inflammatory bowel disease, ischemia-reperfusion injury, enteroinvasive bacterial and parasitic infections.
Title: Both the anti- and pro-apoptotic functions of villin regulate cell turnover and intestinal homeostasis.
Competition between tryptophan fluorescence and electron transfer during unfolding of the villin headpiece.
Title: Competition between tryptophan fluorescence and electron transfer during unfolding of the villin headpiece.
villin severs F-actin to ensure microvillus depolarization and enterocyte remodeling upon intestinal injury
Title: Enterocyte loss of polarity and gut wound healing rely upon the F-actin-severing function of villin.
Villin-Cre(+);Klf4(fl/fl) have greater susceptibility to chemical-induced gastric carcinogenesis and increased rates of gastric tumor progression than control mice.
Title: Disruption of Klf4 in villin-positive gastric progenitor cells promotes formation and progression of tumors of the antrum in mice.
The data establish that meprins interact with and cleave villin and actin, and these cytoskeletal proteins are substrates for meprins.
Title: Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusion.
Villin is an actin regulatory protein that organizes, integrates and regulates multiple epithelial cell functions.
Title: Regulation of cell structure and function by actin-binding proteins: villin's perspective.
Data show that villin, characteristic markers of brush borders, become abnormally distributed along these atypical basolateral membranes in gal3(-/-) mice.
Title: Loss of galectin-3 impairs membrane polarisation of mouse enterocytes in vivo.
different regulatory sequences of the villin gene regulate expression in the intestinal epithelium
Title: Cis elements of the villin gene control expression in restricted domains of the vertical (crypt) and horizontal (duodenum, cecum) axes of the intestine.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Targeted (2) 1 citation
Endonuclease-mediated (3) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D1Mit24 (e-PCR), detects polymorphism
- UniSTS:116253

Vil (e-PCR), detects polymorphism
- UniSTS:144756

UCDEQ387 (e-PCR)
- UniSTS:505464

D1Mcg101 (e-PCR), detects polymorphism
- UniSTS:142235

D1Mcg4 (e-PCR), detects polymorphism
- UniSTS:142239

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables actin binding	IEA Inferred from Electronic Annotation more info
enables actin filament binding	IBA Inferred from Biological aspect of Ancestor more info
enables actin filament binding	ISO Inferred from Sequence Orthology more info
enables calcium ion binding	ISO Inferred from Sequence Orthology more info
enables cysteine-type endopeptidase inhibitor activity involved in apoptotic process	IMP Inferred from Mutant Phenotype more info	PubMed
enables identical protein binding	ISO Inferred from Sequence Orthology more info
enables lysophosphatidic acid binding	ISO Inferred from Sequence Orthology more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables phosphatidylinositol-4,5-bisphosphate binding	IBA Inferred from Biological aspect of Ancestor more info
enables phosphatidylinositol-4,5-bisphosphate binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in actin filament capping	ISO Inferred from Sequence Orthology more info
involved_in actin filament depolymerization	ISO Inferred from Sequence Orthology more info
involved_in actin filament polymerization	ISO Inferred from Sequence Orthology more info
involved_in actin filament severing	IBA Inferred from Biological aspect of Ancestor more info
involved_in actin filament severing	ISO Inferred from Sequence Orthology more info
involved_in actin polymerization or depolymerization	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in barbed-end actin filament capping	IBA Inferred from Biological aspect of Ancestor more info
involved_in barbed-end actin filament capping	ISO Inferred from Sequence Orthology more info
involved_in cellular response to epidermal growth factor stimulus	ISO Inferred from Sequence Orthology more info
involved_in cellular response to hepatocyte growth factor stimulus	IDA Inferred from Direct Assay more info	PubMed
involved_in cytoplasmic actin-based contraction involved in cell motility	ISO Inferred from Sequence Orthology more info
involved_in cytoskeleton organization	IEA Inferred from Electronic Annotation more info
involved_in epidermal growth factor receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in intestinal D-glucose absorption	IGI Inferred from Genetic Interaction more info	PubMed
NOT involved_in microvillus assembly	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of actin filament bundle assembly	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of actin filament depolymerization	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of cell migration	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of epithelial cell migration	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of lamellipodium morphogenesis	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of multicellular organism growth	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of protein localization to plasma membrane	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of actin nucleation	ISO Inferred from Sequence Orthology more info
involved_in regulation of cell shape	ISO Inferred from Sequence Orthology more info
involved_in regulation of lamellipodium morphogenesis	IBA Inferred from Biological aspect of Ancestor more info
involved_in regulation of lamellipodium morphogenesis	IDA Inferred from Direct Assay more info	PubMed
involved_in regulation of microvillus length	IGI Inferred from Genetic Interaction more info	PubMed
involved_in regulation of wound healing	IDA Inferred from Direct Assay more info	PubMed
involved_in response to bacterium	ISO Inferred from Sequence Orthology more info
involved_in terminal web assembly	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
is_active_in actin cytoskeleton	IBA Inferred from Biological aspect of Ancestor more info
located_in actin filament bundle	ISO Inferred from Sequence Orthology more info
located_in brush border	IDA Inferred from Direct Assay more info	PubMed
located_in brush border	TAS Traceable Author Statement more info	PubMed
located_in cell projection	IEA Inferred from Electronic Annotation more info
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoskeleton	IEA Inferred from Electronic Annotation more info
located_in filopodium	IDA Inferred from Direct Assay more info	PubMed
located_in filopodium	ISO Inferred from Sequence Orthology more info
located_in filopodium tip	IDA Inferred from Direct Assay more info	PubMed
is_active_in lamellipodium	IBA Inferred from Biological aspect of Ancestor more info
located_in lamellipodium	IDA Inferred from Direct Assay more info	PubMed
located_in lamellipodium	ISO Inferred from Sequence Orthology more info
located_in microvillus	IDA Inferred from Direct Assay more info	PubMed
located_in microvillus	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in ruffle	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: villin-1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_009509.2 → NP_033535.2 villin-1

See identical proteins and their annotated locations for NP_033535.2

Status: VALIDATED

Source sequence(s)

AI663456, AK027908, BB871941, BY426484

Consensus CDS

CCDS15049.1

UniProtKB/Swiss-Prot

Q149B6, Q62468, Q91WH4

UniProtKB/TrEMBL

Q8CEJ4

Related

ENSMUSP00000027366.7, ENSMUST00000027366.13

Conserved Domains (7) summary

cd11288
Location:513 → 603

gelsolin_S5_like; Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins

cd11289
Location:136 → 225

gelsolin_S2_like; Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins

cd11290
Location:17 → 121

gelsolin_S1_like; Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins

cd11291
Location:619 → 715

gelsolin_S6_like; Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins

cd11292
Location:250 → 348

gelsolin_S3_like; Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins

cd11293
Location:392 → 492

gelsolin_S4_like; Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins

pfam02209
Location:793 → 827

VHP; Villin headpiece domain