Primary Information
BoMiProt ID	Bomi124
Protein Name	Vimentin
Organism	Bos taurus
Uniprot ID	P48616
Milk Fraction	Whey
Ref Sequence ID	NP_776394.2
Aminoacid Length	466
Molecular Weight	53728
FASTA Sequence	Download
Gene Name	VIM
Gene ID	280955
Protein Existence Status	Reviewed: Experimental evidence at protein level
Secondary Information
Protein Function	Vimentin is a cytoskeletal type III intermediate filament protein; contributes to epithelial to mesenchymal transition progression; provides mechanical stability; regulation of signalling, protein trafficking and gene expression;
Biochemical Properties	PIP and PIP2 inhibit the polymerization of vimentin; Labelled actin filaments were examined in vitro by fluorescence microscopy and were seen to break in the presence of polymerizing vimentin; vimentin assembly is the coiled-coil dimers; two of these dimers associate into an antiparallel, approximately half-staggered tetramer ; this tetrameric complex forms during renaturation of vimentin from 8 M urea to low-salt buffers; addition of salt initiates filament assembly; increase in ionic strength results in the lateral association of eight tetramers into a one-unit-length filament
Significance in milk	Role in mammary gland development; mammary gland development is delayed in the absence of vimentin;
PTMs	Sumoylation by ubc9; glycosylation by OGT, O-linked β-N-acetylglucosamine; ADP ribosylation by ADP-ribosyl transferase SpyA; numerous phosphorylation sites
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	1-58,459-466
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	phosphorylation is strongly associated with promoting cell migration; phosphorylation induces interaction with 14-3-3 which influences cell growth and tumorigenesis, autophagy and promotes Akt-mediated tumorigenesisl phosphorylation sites appear to promote its pro-migratory function; late M phase phosphorylation was altered with increased GlcNAcylation in vimentin
Bibliography	1. Ku, N.-O., Michie, S., Resurreccion, E. Z., Broome, R. L., & Omary, M. B. (2002). Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression. Proceedings of the National Academy of Sciences of the United States of America, 99(7), 4373–4378. https://doi.org/10.1073/pnas.072624299. 2. Kim, S., Wong, P., & Coulombe, P. A. (2006). A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth. Nature, 441(7091), 362–365. https://doi.org/10.1038/nature04659. 3. Hyder, C. L., Pallari, H.-M., Kochin, V., & Eriksson, J. E. (2008). Providing cellular signposts--post-translational modifications of intermediate filaments. FEBS Letters, 582(14), 2140–2148. https://doi.org/10.1016/j.febslet.2008.04.064. 4. Peuhu, E., Virtakoivu, R., Mai, A., Wärri, A., & Ivaska, J. (2017). Epithelial vimentin plays a functional role in mammary gland development. Development (Cambridge, England), 144(22), 4103–4113. https://doi.org/10.1242/dev.154229. 5. Premchandar, A., Mücke, N., Poznański, J., Wedig, T., Kaus-Drobek, M., Herrmann, H., & Dadlez, M. (2016). Structural Dynamics of the Vimentin Coiled-coil Contact Regions Involved in Filament Assembly as Revealed by Hydrogen-Deuterium Exchange. The Journal of Biological Chemistry, 291(48), 24931–24950. https://doi.org/10.1074/jbc.M116.748145.