|Protein Name||Integrin alpha FG-GAP repeat containing 1|
|Ref Sequence Id||NP_001033621.1|
|Amino Acid Lenth||611|
|Protein Existence Status||Unreviewed: Experimental evidence at transcript level|
|Protein Function||ubiquitously expressed cell surface receptors that play a critical role in regulating the interaction between a cell and its microenvironment to control cell fate; integrins can influence a wide variety of cellular phenotypes, including adhesion, migration, proliferation, survival, differentiation, mechano-sensing and cytoskeletal organisation, thereby implicating integrins in processes such as tissue development and repair, angiogenesis, immune response and haemostasis; deregulation of integrin signalling is associated with various pathological processes, including autoimmunity, inflammation and cancer|
|Biochemical Properties||integrin family contains 18 α- and eight β-subunits that bind noncovalently to form 24 distinct αβ integrin heterodimers with each β subunit binding several α- subunits. The α- and β-subunits are both type I transmembrane receptors and share structural similarities, such as a large extracellular domain, a single transmembrane domain and a cytoplasmic tail; α subunit contains a metal ion-dependent adhesion site; Integrin α-subunits containing this inserted αI domain are the collagen receptors (α1, α2, α10 and α11) and the leukocyte receptors; these receptors pair predominantly with β1 and are required for tissue integrity in organs such as muscle, kidney and skin ; α-subunits form heterodimers with β1 and β3 subunits and bind ECM ligands; βI domain contains two other metal ion-binding sites called the adjacent metal ion-dependent adhesion site and the synergistic metal ion-binding site; β-subunit stalk/leg section that contains four cysteine-rich integrin epidermal growth factor-like (IEGF) modules; β-tails are more highly conserved that the α-tails and are the primary moderator of intracellular ligand interactions; ß contain a phosphotyrosine-binding (PTB) domain - important for binding multiple integrin adaptor proteins;|
|Significance in milk||ß1 integrin is required for mammary epithelial cells to express milk proteins|
|Linking IDs||Bomi2353 Bomi2354 Bomi2355 Bomi2356|
|Bibliography||1. Xia, T., Takagi, J., Coller, B. S., Wang, J. H., & Springer, T. A. (2004, November 4). Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature, Vol. 432, pp. 59–67. https://doi.org/10.1038/nature02976. |
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3. Calderwood, D. A., Fujioka, Y., De Pereda, J. M., García-Alvarez, B., Nakamoto, T., Margolis, B., … Ginsberg, M. H. (2003). Integrin β cytoplasmic domain interactions with phosphotyrosine-binding domains: A structural prototype for diversity in integrin signaling. Proceedings of the National Academy of Sciences of the United States of America, 100(5), 2272–2277. https://doi.org/10.1073/pnas.262791999.
4. Tomaselli, K. J., Damsky, C. H., & Reichardt, L. F. (1987). Interactions of a neuronal cell line (PC12) with laminin, collagen IV, and fibronectin: Identification of integrin-related glycoproteins involved in attachment and process outgrowth. Journal of Cell Biology, 105(5), 2347–2358. https://doi.org/10.1083/jcb.105.5.2347.
5. Munger, J. S., Huang, X., Kawakatsu, H., Griffiths, M. J. D., Dalton, S. L., Wu, J., … Sheppard, D. (1999). The integrin αvβ6 binds and activates latent TGFβ1: A mechanism for regulating pulmonary inflammation and fibrosis. Cell, 96(3), 319–328. https://doi.org/10.1016/S0092-8674(00)80545-0.