MYL3

MYL3
Identifiers
Aliases	MYL3, CMH8, MLC1SB, MLC1V, VLC1, MLC-lV/sb, VLCl, myosin light chain 3
External IDs	MGI: 97268 HomoloGene: 20099 GeneCards: MYL3
Gene ontology Molecular function • calcium ion binding • structural constituent of muscle • motor activity • actin monomer binding • myosin II heavy chain binding Cellular component • cytosol • muscle myosin complex • sarcomere • A band • I band • myosin complex Biological process • ventricular cardiac muscle tissue morphogenesis • regulation of striated muscle contraction • skeletal muscle tissue development • positive regulation of ATPase activity • cardiac muscle contraction • regulation of the force of heart contraction • muscle filament sliding Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4634	17897
Ensembl	ENSG00000160808	ENSMUSG00000059741
UniProt	P08590	P09542
RefSeq (mRNA)	NM_000258	NM_010859
RefSeq (protein)	NP_000249 NP_000249.1	NP_034989
Location (UCSC)	Chr 3: 46.86 – 46.88 Mb	Chr 9: 110.74 – 110.77 Mb
PubMed search

4634

17897

ENSG00000160808

ENSMUSG00000059741

P08590

P09542

NM_000258

NM_010859

NP_000249
NP_000249.1

NP_034989

Myosin essential light chain (ELC), ventricular/cardiac isoform is a protein that in humans is encoded by the MYL3 gene. This cardiac ventricular/slow skeletal ELC isoform is distinct from that expressed in fast skeletal muscle (MYL1) and cardiac atrial muscle (MYL4). Ventricular ELC is part of the myosin molecule and is important in modulating cardiac muscle contraction.

Cardiac, ventricular ELC is 21.9 kDa and composed of 195 amino acids (See human MYL3 sequences features here). Cardiac ELC and the second light chain, regulatory light chain (RLC, MYL2), are non-covalently bound to IQXXXRGXXXR motifs in the 9 nm S1-S2 lever arm of the myosin head, both alpha (MYH6) and beta (MYH7) isoforms. Both light chains are members of the EF-hand superfamily of proteins, which possess helix-loop-helix motifs in two globular domains connected by an alpha-helical linker. Though EF hand motifs are specialized to bind divalent ions such as calcium, cardiac ELC does not bind calcium at physiological levels. The N-terminal region of cardiac ELC is functionlly unique in that it is positively charged, being rich in Lysine residues (amino acids 4-14), with subsequent unique structure governed by Proline-Alanine repeats (amino acids 15-36).

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Wikipedia