Abstract
We have isolated and characterized the complete human villin gene. The villin gene is located on chromosome 2q35-36 in humans and on chromosome 1 in mice. Villin belongs to a family of calcium-regulated actin-binding proteins that share structural and functional homologies. The villin gene is expressed mainly in cells that develop a brush border, such as mucosal cells of the small and large intestine and epithelial cells of the kidney proximal tubules. Villin gene expression is strictly regulated during adult life and embryonic development in the digestive and urogenital tracts and, thus, may be used as a marker of the digestive and renal cell lineages. The human villin gene has one copy per haploid genome, encompasses about 25 kilobases, and contains 19 exons. Analysis of the structural organization of this gene shows that the two mRNAs that encode villin in humans arise by alternative choice of one of the two polyadenylylation signals located within the last exon. The overall organization of the exons reflects the gene duplication event from which this family of actin-binding proteins originated.
MeSH Terms
Actins/genetics
Animals
Base Sequence
Calcium-Binding Proteins/genetics
Carrier Proteins/genetics
Chromosome Mapping
Chromosomes, Human, Pair 2
DNA/genetics,isolation & purification
Exons
Genomic Library
Humans
Introns
Lymphocytes/physiology
Mice
Microfilament Proteins/genetics
Molecular Sequence Data
RNA Splicing
RNA, Messenger/genetics
Transcription, Genetic
Chemicals
Actins
Calcium-Binding Proteins
Carrier Proteins
Microfilament Proteins
RNA, Messenger
villin
DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Pringault E
Département de Biologie Moléculaire, Institut Pasteur, Paris, France.
Robine S
Louvard D
References (22)
22 references, click to expand
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Localization of the villin gene on human chromosome 2q35-q36 and on mouse chromosome 1.
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Functional comparison of villin and gelsolin. Effects of Ca2+, KCl, and polyphosphoinositides.
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Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity.
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