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SVIL

Domain

As opposed to other villin-type headpiece domains, supervillin HP (SVHP) doesn't bind F-actin due to the absence of a conformationally flexible region (V-loop).

Function

Isoform 1

Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420).

Isoform 2

May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity).

Involvement in disease

Myopathy, myofibrillar, 10

MFM10

A form of myofibrillar myopathy, a group of chronic neuromuscular disorders characterized at ultrastructural level by disintegration of the sarcomeric Z disk and myofibrils, and replacement of the normal myofibrillar markings by small dense granules, or larger hyaline masses, or amorphous material. MFM10 is an autosomal recessive disorder characterized by muscle pain, cramping, exercise fatigue, and progressive muscle rigidity.

None

The disease is caused by variants affecting the gene represented in this entry.

Sequence Similarities

Belongs to the villin/gelsolin family.

Tissue Specificity

Expressed in many tissues. Most abundant in muscle, bone marrow, thyroid gland and salivary gland. Isoform 1 (archvillin) is muscle specific.

Cellular localization

Alternative names

Supervillin, Archvillin, p205/p250, SVIL

swissprot:O95425 omim:604126 entrezGene:6840 swissprot:Q569J5