supervillin
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. 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. 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. Belongs to the villin/gelsolin family. Expressed in many tissues. Most abundant in muscle, bone marrow, thyroid gland and salivary gland. Isoform 1 (archvillin) is muscle specific. 4 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
|
Protein type: Actin-binding; Contractile; Motility/polarity/chemotaxis; Nuclear receptor co-regulator |
Chromosomal Location of human Ortholog: 10p11.23 |
Cellular Component:
actin cytoskeleton; cell projection; cleavage furrow; costamere; cytoplasm; cytosol; microtubule minus-end; midbody; nucleus; plasma membrane; podosome
|
Molecular Function:
actin filament binding; phosphatidylinositol-4,5-bisphosphate binding; protein binding
|
Biological Process:
actin filament severing; actin polymerization or depolymerization; barbed-end actin filament capping; positive regulation of cytokinesis; skeletal muscle tissue development
|
Disease: Myofibrillar Myopathy 10
|
Reference #:
O95425
(UniProtKB)
|
Alt. Names/Synonyms: Archvillin; DKFZp686A17191; membrane-associated F-actin binding protein p205; p205/p250; Supervillin; SVIL
|
Gene Symbols: SVIL
|
Molecular weight:
247,746 Da
|
Basal Isoelectric point:
6.55
Predict pI for various phosphorylation states
|