Aliases for ACTG2 Gene
External Ids for ACTG2 Gene
Previous Symbols for ACTG2 Gene
Actins are highly conserved proteins that are involved in various types of cell motility and in the maintenance of the cytoskeleton. Three types of actins, alpha, beta and gamma, have been identified in vertebrates. Alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins co-exist in most cell types as components of the cytoskeleton and as mediators of internal cell motility. This gene encodes actin gamma 2; a smooth muscle actin found in enteric tissues. Alternative splicing results in multiple transcript variants encoding distinct isoforms. Based on similarity to peptide cleavage of related actins, the mature protein of this gene is formed by removal of two N-terminal peptides.[provided by RefSeq, Dec 2010]
GeneCards Summary for ACTG2 Gene
ACTG2 (Actin, Gamma 2, Smooth Muscle, Enteric) is a Protein Coding gene. Diseases associated with ACTG2 include visceral myopathy and myopathic intestinal pseudoobstruction. Among its related pathways are Akt Signaling and ERK Signaling. An important paralog of this gene is ACTB.
UniProtKB/Swiss-Prot for ACTG2 Gene
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells
Actin is a ubiquitous globular protein that is one of the most highly-conserved proteins known. It is found in two main states; G-actin is the globular monomeric form, whereas F-actin forms helical polymers. Both G- and F-actin are intrinsically flexible structures - a feature vital in actins role as a dynamic filament network. Actin has four major functions. Firstly, F-actin polymers form microfilaments - polar intracellular tracks for kinesin motor proteins, allowing the transport of vesicles, organelles and other cargo. Actin is a component of the cytoskeleton and links to alpha-actinin, E-cadherin and beta-catenin at adherens junctions. This gives mechanical support to cells and attaches them to each other and the extracellular matrix. In muscle cells, actin-rich thin filaments associate with myosin-rich thick filaments to form actomyosin myofibrils. Using energy from the hydrolysis of ATP, myofibrils undergo cyclic shortening through actin-myosin head interactions, which represents the mechanics of muscle contraction. Finally, actin has a role in cell motility through polymerization and depolymerization of fibrils.