Svil Gene Summary [Rat]

Predicted to enable actin filament binding activity and phosphatidylinositol-4,5-bisphosphate binding activity. Predicted to be involved in several processes, including actin filament severing; actin polymerization or depolymerization; and barbed-end actin filament capping. Predicted to act upstream of or within muscle cell differentiation. Predicted to be located in several cellular components, including costamere; focal adhesion; and sarcolemma. Predicted to be active in actin cytoskeleton and cytoplasm. Human ortholog(s) of this gene implicated in myofibrillar myopathy 10. Orthologous to human SVIL (supervillin). [provided by Alliance of Genome Resources, Jul 2025]

Details

Type
Protein Coding
Official Symbol
Svil
Official Name
supervillin [Source:RGD Symbol;Acc:1306354]
Ensembl ID
ENSRNOG00000018110
Bio databases IDs NCBI: 361256 Ensembl: ENSRNOG00000018110
Aliases supervillin
Synonyms B430302E16Rik, LOC100503917, MFM10, supervillin
Species
Rat, Rattus norvegicus
OrthologiesHumanMouse

Protein Domains

A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Svil often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
  • actin filament binding
  • Actin depolymerization factor/cofilin- and gelsolin-like domains
  • Gelsolin repeat
  • Villin headpiece domain
  • protein binding

Top Findings

The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
binds
disease
  • multiple sclerosis
  • myofibrillar myopathy type 10
  • fracture of bone
  • Rett syndrome
  • acute myeloid leukemia
  • fibromuscular dysplasia
  • vertigo
  • infection by Influenza A virus subtype H1N1
regulated by
  • ERG
  • D-glucose
  • L-serine
  • KCNJ2
  • TNF
  • doxorubicin
  • metribolone
  • HK cells
  • Anaplasma phagocytophilum
  • ANLN
role in cell
  • cell viability
  • cell death
  • activation in
  • differentiation
  • accumulation in
  • survival
  • binding in
  • reorganization
  • polarization
  • deubiquitination in

Subcellular Expression

Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
  • Plasma Membrane
  • Cytoplasm
  • cell periphery
  • focal adhesions
  • podosomes
  • actin cytoskeleton
  • Nucleus
  • costameres
  • actin filaments
  • midbody
  • cytosol
  • membrane ruffles
  • nucleoplasm
  • sarcolemma
  • cleavage furrow
  • lamellipodia

Gene Ontology Annotations

Describes the biological processes, cellular components, and molecular functions associated with the rat Svil gene, providing context for its role in the cell.

Biological Process

Functions and activities the gene product is involved in
  • barbed-end actin filament capping
  • actin filament severing
  • actin polymerization or depolymerization
  • skeletal muscle tissue development
  • positive regulation of cytokinesis

Cellular Component

Where in the cell the gene product is active
  • nucleus
  • focal adhesion
  • cytoplasm
  • cleavage furrow
  • actin cytoskeleton
  • cytosol
  • costamere
  • midbody
  • cell projection
  • plasma membrane
  • podosome

Molecular Function

What the gene product does at the molecular level
  • actin filament binding
  • phosphatidylinositol-4,5-bisphosphate binding
  • protein binding

Gene-Specific Assays for Results You Can Trust

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