Primary Information
BoMiProt ID	Bomi7302
Protein Name	Myosin light chain 1/3, skeletal muscle isoform/MLC1/MLC3/MLC1F/MLC3F/Myosin light chain alkali 1/2/Myosin light chain A1/A2
Organism	Bos taurus
Uniprot ID	A0JNJ5
Milk Fraction	whey
Ref Sequence ID	NP_001073046.1
Aminoacid Length	192
Molecular Weight	20932
FASTA Sequence	Download
Gene Name	MYL1
Gene ID	317657
Protein Existence Status	Reviewed
Secondary Information
Protein Function	Non-regulatory(Alkali) myosin light chain required for proper formation and/or maintenance of myofibers, and thus appropriate muscle function
Biochemical Properties	Myosin is a hexamer of 2 heavy chains and 4 light chains.Non-regulatory(Alkali) myosin light chain has a structure closely related to that of the EF hand calcium binding protein family such as troponin C and calmodulin.The main secondary structure of MYL1 protein is predicted to be α-helical.MYL1a protein comprised 52.00% alpha helix, 3.33% beta sheet and 44.67% random coil. The MYL1b protein was predicted to contain 55.73% alpha helix, 2.60% beta sheet and 41.67% random coil. Alpha helices and random coils were the dominant secondary structural features in both proteins, and few beta sheets are predicted.
PTMs	Methylation and phosphorylation,N-glycosylation
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation	>sp|A0JNJ5|MYL1_BOVIN Myosin light chain 1/3, skeletal muscle isoform OS=Bos taurus OX=9913 GN=MYL1 PE=2 SV=1 MAPKKDVKKPAAAAAPAPAPAPAPAPAPAPPKEEKIDLSAIKIEFSKQQQDEFKEAFLLF DRTGECKIT*69LS*71QVGDVLRALGTNPT*85NAEVKKVLGNPS*97NEEMNAKKIEFEQFLPMLQAISN NKDQGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALMAGQEDSNGCI NYEAFVKHIMSN
Predicted Disorder Regions	(1-43)
DisProt Annotation
TM Helix Prediction	no TM helices
Significance of PTMs	Several N-glycosylation and phosphorylation sites.MYL1a was predicted to have three N-glycosylation sites Asn41, Asn53 and Asn100 whereas MYL1b was predicted to have three N-glycosylation sites (Asn83, Asn95 and Asn142). MYL1a was predicted to have two phosphorylation sites (Ser55 and Tyr85), whereas MYL1b was predicted to have four phosphorylation sites Ser39, 46, 97 and Tyr127. Studies have shown that myosin light chain proteins can be regulated by phosphorylation and the phosphorylation of myosin light chain proteins is related to the proliferation of tumour cells.
Linking IDs
Bibliography	1.Zhang, C., Wang, G., Ji, Z., Liu, Z., Hou, L., Liu, G., & Wang, J. (2015). Molecular cloning, characterisation and mRNA expression analysis of the sheep myosin light chain 1 gene. Gene, 569(1), 51-59. 2.Smith, S. B., Davis, S. K., Wilson, J. J., Stone, R. T., Wu, F. Y., Garcia, D. K., Lunt, D. K., & Schiavetta, A. M. (1995). Bovine fast-twitch myosin light chain 1: cloning and mRNA amount in muscle of cattle treated with clenbuterol. The American journal of physiology, 268(5 Pt 1), E858–E865. https://doi.org/10.1152/ajpendo.1995.268.5.E858