Search by BoMiProt ID - Bomi77


Primary Information

BoMiProt ID Bomi77
Protein Name Integrin alpha FG-GAP repeat containing 1
Organism Bos taurus
Uniprot IdQ2TBX9
Milk FractionWhey
Ref Sequence Id NP_001033621.1
Amino Acid Lenth 611
Molecular Weight 67804
Fasta Sequence https://www.uniprot.org/uniprot/Q2TBX9.fasta
Gene Name ITFG1
Gene Id 512545
Protein Existence Status Unreviewed: Experimental evidence at transcript level

Secondry Information

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.
2. Lee, J. O., Rieu, P., Arnaout, M. A., & Liddington, R. (1995). Crystal structure of the A domain from the a subunit of integrin CR3 (CD11 b/CD18). Cell, 80(4), 631–638. https://doi.org/10.1016/0092-8674(95)90517-0.
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.