MYL3

Myosin, light chain 3, alkali; ventricular, skeletal, slow
Identifiers
Symbols	MYL3; CMH8; MLC1SB; MLC1V; VLC1
External IDs	OMIM: 160790 MGI: 97268 HomoloGene: 20099 GeneCards: MYL3 Gene
Gene Ontology Molecular function • motor activity • actin monomer binding • calcium ion binding • structural constituent of muscle • myosin II heavy chain binding Cellular component • cytosol • muscle myosin complex • myosin complex • sarcomere • A band • I band Biological process • regulation of the force of heart contraction • regulation of striated muscle contraction • skeletal muscle tissue development • muscle filament sliding • positive regulation of ATPase activity • ventricular cardiac muscle tissue morphogenesis • cardiac muscle contraction Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4634	17897
Ensembl	ENSG00000160808	ENSMUSG00000059741
UniProt	P08590	Q61935
RefSeq (mRNA)	NM_000258	NM_010859.2
RefSeq (protein)	NP_000249	NP_034989.1
Location (UCSC)	Chr 3: 46.9 – 46.92 Mb	Chr 9: 110.67 – 110.67 Mb
PubMed search	[1]	[2]

Myosin light chain 3 is a protein that in humans is encoded by the 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.

Further reading

• Schaub MC, Hefti MA, Zuellig RA, Morano I (1998). "Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms". Cardiovasc. Res. 37 (2): 381–404. doi:10.1016/S0008-6363(97)00258-7. PMID 9614495. 
• Stragier P, Kunkel B, Kroos L, Losick R (1989). "Chromosomal rearrangement generating a composite gene for a developmental transcription factor". Science 243 (4890): 507–12. doi:10.1126/science.2536191. PMID 2536191. 
• Fodor WL, Darras B, Seharaseyon J et al (1989). "Human ventricular/slow twitch myosin alkali light chain gene characterization, sequence, and chromosomal location". J. Biol. Chem. 264 (4): 2143–9. PMID 2789520. 
• Hoffmann E, Shi QW, Floroff M et al (1988). "Molecular cloning and complete nucleotide sequence of a human ventricular myosin light chain 1". Nucleic Acids Res. 16 (5): 2353. doi:10.1093/nar/16.5.2353. PMC 338240. PMID 3357795. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=338240. 
• Kurabayashi M, Komuro I, Tsuchimochi H et al (1988). "Molecular cloning and characterization of human atrial and ventricular myosin alkali light chain cDNA clones". J. Biol. Chem. 263 (27): 13930–6. PMID 3417683. 
• Henry GD, Trayer IP, Brewer S, Levine BA (1985). "The widespread distribution of alpha-N-trimethylalanine as the N-terminal amino acid of light chains from vertebrate striated muscle myosins". Eur. J. Biochem. 148 (1): 75–82. doi:10.1111/j.1432-1033.1985.tb08809.x. PMID 3979397. 
• Kovalyov LI, Shishkin SS, Efimochkin AS et al (1996). "The major protein expression profile and two-dimensional protein database of human heart". Electrophoresis 16 (7): 1160–9. doi:10.1002/elps.11501601192. PMID 7498159. 
• Poetter K, Jiang H, Hassanzadeh S et al (1996). "Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle". Nat. Genet. 13 (1): 63–9. doi:10.1038/ng0596-63. PMID 8673105. 
• Takeuchi K, Senba S, Furukawa K et al (1999). "Localization of 17-kDa myosin light chain isoforms in cultured aortic smooth muscle cells". J. Biochem. 125 (2): 334–42. PMID 9990131. 
• Andersen PS, Havndrup O, Bundgaard H et al (2002). "Myosin light chain mutations in familial hypertrophic cardiomyopathy: phenotypic presentation and frequency in Danish and South African populations". J. Med. Genet. 38 (12): E43. doi:10.1136/jmg.38.12.e43. PMC 1734772. PMID 11748309. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1734772. 
• Olson TM, Karst ML, Whitby FG, Driscoll DJ (2002). "Myosin light chain mutation causes autosomal recessive cardiomyopathy with mid-cavitary hypertrophy and restrictive physiology". Circulation 105 (20): 2337–40. doi:10.1161/01.CIR.0000018444.47798.94. PMID 12021217. 
• Moretti A, Weig HJ, Ott T et al (2002). "Essential myosin light chain as a target for caspase-3 in failing myocardium". Proc. Natl. Acad. Sci. U.S.A. 99 (18): 11860–5. doi:10.1073/pnas.182373099. PMC 129359. PMID 12186978. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=129359. 
• Strausberg RL, Feingold EA, Grouse LH et al (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Richard P, Charron P, Carrier L et al (2003). "Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy". Circulation 107 (17): 2227–32. doi:10.1161/01.CIR.0000066323.15244.54. PMID 12707239. 
• Xie B, Huang R, Huang L et al (2004). "The functional domains of human ventricular myosin light chain 1". Biophys. Chem. 106 (1): 57–66. doi:10.1016/S0301-4622(03)00172-8. PMID 14516912. 
• Suzuki Y, Yamashita R, Shirota M et al (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=515316. 
• Gerhard DS, Wagner L, Feingold EA et al (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 

External links

• GeneReviews/NIH/NCBI/UW entry on Familial Hypertrophic Cardiomyopathy Overview