villin1 Recombinant Rabbit Monoclonal Antibody [JU34-75] (ET7106-62)

UNIPROT #

P09327

PROTEIN NAME

villin1

SYNONYMS

D2S1471 antibody;OTTHUMP00000164145 antibody;VIL antibody;VIL1 antibody;VILI_HUMAN antibody;Villin 1 antibody;Villin-1 antibody;Villin1 antibody

SEQUENCE SIMILARITIES

Belongs to the villin/gelsolin family.

TISSUE SPECIFICITY

Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes (at protein level).

POST-TRANSLATIONAL MODIFICATION

Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity). Phosphorylated on tyrosine residues by SRC. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine-phosphorylated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca(2+) requirements. The tyrosine-phosphorylated form does not regulate actin-capping activity. Tyrosine phosphorylation is essential for cell migration: tyrosine phosphorylation sites in the N-terminus half regulate actin reorganization and cell morphology, whereas tyrosine phosphorylation sites in the C-terminus half regulate cell migration via interaction with PLCG1.

SUBCELLULAR LOCATION

Cytoskeleton.

FUNCTION

Caldesmon, Filamin 1, Nebulin and Villin are differentially expressed and regulated Actin binding proteins. Both muscular (CDh) and non-muscular (CDl) forms of Caldesmon have been identified and each has been shown to bind to Actin as well as to calmodulin and myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CDl is widely expressed in non-muscle tissues and cells. Filamin 1, which is ubiquitously expressed and exists as a homodimer, functions to crosslink Actin to filaments. Nebulin is a large filamentous protein specific to muscle tissue that may function as a ruler for filament length. Several isoforms of Nebulin are produced by alternative exon usage. Villin is Ca2+-regulated and is the major structural component of the brush border of absorptive cells.