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XB130 : ウィキペディア英語版
XB130

XB130 (also known as AFAP1L2) is a cytosolic adaptor protein and signal transduction mediator. XB130 regulates cell proliferation, cell survival, cell motility and gene expression. XB130 is highly similar to AFAP and is thus known as actin filament associated protein 1-like 2 (AFAP1L2). XB130 is a substrate and regulator of multiple tyrosine kinase-mediated signaling. XB130 is highly expressed in the thyroid and spleen.
== Molecular structure ==

The XB130 gene is located on human chromosome 10q25.3 and encodes an 818 amino acid protein. It has a molecular weight of approximately 130 kDa and is structurally similar to actin-filament-associated protein (AFAP) and is thus known as AFAP1L2.〔Xu, J., Bai, X.H., Lodyga, M., Han, B., Xiao, H., Keshavjee, S., Hu, J., Zhang, H., Yang, B.B., and Liu, M. 2007. XB130, a novel adaptor protein for signal transduction. J Biol Chem 282:16401-16412〕 Several tyrosine phosphorylation sites and a proline rich sequence are included in the N-terminal region of XB130, which allows it to interact and activate c-Src-containing proteins, as well as bind to p85α of PI3K. Two pleckstrin-homology domains are located in the middle portion, giving XB130 its lipid-binding ability. The C-terminal region contains a coiled-coil domain, which shares partial similarity with AFAP's leucine zipper domain.〔Snyder, B.N., Cho, Y., Qian, Y., Coad, J.E., Flynn, D.C., and Cunnick, J.M. 2011. AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes. Eur J Cell Biol 90:376-389〕 Both the C-terminal and N-terminal regions of XB130 are required for XB130's role in its translocation to the lamellipodia.〔 Despite XB130's structural similarity to AFAP, XB130 does not behave like an actin filament-associated protein. The actin-binding site present in AFAP is only partially present in XB130.

抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)
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