Search by BoMiProt ID - Bomi30

Primary Information

BoMiProt ID Bomi30
Protein Name Radixin
Organism Bos taurus
Uniprot IDQ32LP2
Milk FractionWhey
Ref Sequence ID NP_001069217.1
Aminoacid Length 583
Molecular Weight 68568
FASTA Sequence Download
Gene Name RDX
Gene ID 517111
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

Presence in other biological fluids/tissue/cells adherence junctions in rat liver, intestinal microvilli, microvilli, filopodia, uropods, ruffling membranes, retraction fibers, the cleavage furrow of dividing cells, and adhesion sites where actin filaments are associated with the plasma membrane
Protein Function cytoskeletal crosslinkers in actin-rich cell surface structures; essential for cortical cytoskeleton organization, cell motility, adhesion and proliferation;
Biochemical Properties radixin -domain is an extremely long; linear monomer with an enhanced number of electrostatic, salt bridge interactions predicted to contribute synergistically to its thermal stability; presence of polyproline stretch; presence of an N-terminal membrane binding domain (FERM domain), which can bind the membrane via phosphatidylinositol (4,5)-bisphosphate (PIP2), a α-helical linker region and a C-terminal actin-binding domain
Significance in milk Ezrin-radixin-moeisin binding phosphoprotein is required for the development of lactating mammary glands
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions 297-310,311-336,374-407,460-526
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments Radixin (∼80 kDa), ezrin (∼82 kDa) and moesin (∼75 kDa) are very closely related to the band 4.1 superfamily on account of a shared ∼300 residue four-point one, ezrin, radixin, moesin (FERM) domain at the amino-terminus
Bibliography 1. Lurz, R., Orlova, E. V., Günther, D., Dube, P., Dröge, A., Weise, F., … Tavares, P. (2001). Structural conversion between open and closed forms of radixin: Low-angle shadowing electron microscopy. Journal of Molecular Biology, 310(5), 973–978. https://doi.org/10.1006/jmbi.2001.4818.
2. Hirao, M., Sato, N., Kondo, T., Yonemura, S., Monden, M., Sasaki, T., … Tsukita, S. (1996). Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. The Journal of Cell Biology, 135(1), 37–51. https://doi.org/10.1083/jcb.135.1.37.
3. Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., Tsukita, S., & Hakoshima, T. (2003). Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex. EMBO Journal, 22(3), 502–514. https://doi.org/10.1093/emboj/cdg039.
4 Hoeflich, K. P., Tsukita, S., Hicks, L., Kay, C. M., Tsukita, S., & Ikura, M. (2003). Insights into a single rod-like helix in activated radixin required for membrane-cytoskeletal cross-linking. Biochemistry, 42(40), 11634–11641. https://doi.org/10.1021/bi0350497.