Search by BoMiProt ID - Bomi7302


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 IdA0JNJ5
Milk Fractionwhey
Ref Sequence Id NP_001073046.1
Aminoacid Length 192
Molecular Weight 20932
Fasta Sequence https://www.uniprot.org/uniprot/A0JNJ5.fasta
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