Recombinant Human Actin, alpha skeletal muscle (ACTA1)

Function

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells

Subcellular Location

Cytoplasm, cytoskeleton

Disease Association

Congenital myopathy 2A, typical, autosomal dominant (CMYO2A) : A muscular disorder characterized by generalized muscle weakness, delayed motor milestones, hypotonia, and muscle fiber abnormalities on histologic examination. Histologic findings include abnormal thread- or rod-like structures (nemaline rods), intranuclear rods, clumped filaments, cores, or fiber-type disproportion. The spectrum of clinical phenotypes ranges from severe neonatal presentations to onset of a milder disorder in childhood. [The disease is caused by variants affecting the gene represented in this entry] | Congenital myopathy 2B, severe infantile, autosomal recessive (CMYO2B) : An autosomal recessive skeletal muscle disorder characterized by severe hypotonia with lack of spontaneous movements and respiratory insufficiency, usually leading to death in infancy or early childhood. Longer survival has been reported. [The disease is caused by variants affecting the gene represented in this entry] | Congenital myopathy 2C, severe infantile, autosomal dominant (CMYO2C) : An autosomal dominant skeletal muscle disorder characterized by severe congenital weakness usually resulting in death from respiratory failure in the first year or so of life. Patients present at birth with hypotonia, lack of antigravity movements, poor head control, and difficulties feeding or breathing, often requiring tube-feeding and mechanical ventilation. Decreased fetal movements may be observed in some cases. [The disease is caused by variants affecting the gene represented in this entry] | Myopathy, scapulohumeroperoneal (SHPM) : An autosomal dominant muscular disorder characterized by progressive muscle weakness with initial scapulo-humeral-peroneal and distal distribution. Over time, muscle weakness progresses to proximal muscle groups. Clinical characteristics include scapular winging, mild lower facial weakness, foot drop due to foot eversion and dorsiflexion weakness, and selective muscle atrophy. Age at onset and disease progression are variable. [The disease is caused by variants affecting the gene represented in this entry]

Subunit

Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Interacts with alpha-actinin (By similarity). Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). Interacts with TTID (PubMed:10958653). Interacts (via its C-terminus) with USP25; the interaction occurs for all USP25 isoforms but is strongest for isoform USP25m in muscle differentiating cells (PubMed:16501887)

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• Taylor A. et al. Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains. — Genomics (1988)
• Nowak K.J. et al. Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy. — Nat. Genet. (1999)
• Ebert L. et al. Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201). (JUN-)
• Gregory S.G. et al. The DNA sequence and biological annotation of human chromosome 1. — Nature (2006)
• Mural R.J. et al. PubMed: CI-5GBDQ6B103N1E (JUL-)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Hauser M.A. et al. Myotilin is mutated in limb girdle muscular dystrophy 1A. — Hum. Mol. Genet. (2000)