Aliases for MYL3 Gene
- Myosin, Light Chain 3, Alkali; Ventricular, Skeletal, Slow 2 3
- Myosin, Light Polypeptide 3, Alkali; Ventricular, Skeletal, Slow 2 3
- Myosin Light Chain 1, Slow-Twitch Muscle B/Ventricular Isoform 3 4
- Ventricular/Slow Twitch Myosin Alkali Light Chain 3 4
- Cardiac Myosin Light Chain 1 3 4
- MLC1SB 3 4
- CMLC1 3 4
- Myosin Light Chain 3 3
External Ids for MYL3 Gene
MYL3 encodes myosin light chain 3, an alkali light chain also referred to in the literature as both the ventricular isoform and the slow skeletal muscle isoform. Mutations in MYL3 have been identified as a cause of mid-left ventricular chamber type hypertrophic cardiomyopathy. [provided by RefSeq, Jul 2008]
GeneCards Summary for MYL3 Gene
MYL3 (Myosin, Light Chain 3, Alkali; Ventricular, Skeletal, Slow) is a Protein Coding gene. Diseases associated with MYL3 include myl3-related familial hypertrophic cardiomyopathy and cardiomyopathy, familial hypertrophic, 8. Among its related pathways are RhoGDI Pathway and Regulation of actin cytoskeleton. GO annotations related to this gene include calcium ion binding and motor activity. An important paralog of this gene is MYL1.
UniProtKB/Swiss-Prot for MYL3 Gene
Regulatory light chain of myosin. Does not bind calcium
Myosins are a large family of motor proteins that share the common features of ATP hydrolysis, actin binding and potential for kinetic energy transduction. Originally isolated from muscle cells (hence the name), almost all eukaryotic cells are now known to contain myosins. Structurally, mysoins contain a head domain that binds to actin filaments (microfilaments) and is the site of ATP hydrolysis. The tail domain interacts with cargo molecules, and the neck acts as a linker between the head and tail and is the site of regulatory myosin light chain binding. There are 17 myosin families and the most well characterized is myosin II. Myosin II is found predominantly in myocytes and mediates plus-ended movement along microfilaments. It is involved in muscle contraction through cyclic interactions with actin-rich thin filaments, creating a contractile force. It is regulated by phosphorylation via myosin light chain kinase (MLCK) and by intracellular Ca2+ concentrations.