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Discoidin Domain Receptor
Discoidin domain (also known as F5/8 type C domain, or C2-like domain) is major protein domain of many blood coagulation factors. Blood coagulation factors Factor V, V and Factor VIII, VIII contain a C-terminal, twice repeated, domain of about 150 amino acids, which is often called "C2-like domain" (that is unrelated to the C2 domain). In the ''Dictyostelium discoideum'' (Slime mold) cell adhesion protein discoidin, a related domain, named discoidin I-like domain, DLD, or DS, has been found which shares a common C-terminal region of about 110 amino acids with the FA58C domain, but whose N-terminal 40 amino acids are much less conserved. Similar domains have been detected in other extracellular and membrane proteins. In coagulation factors V and VIII the repeated domains compose part of a larger functional domain which promotes binding to anionic phospholipids on the surface of platelets and endothelial cells. The C-terminal domain of the second FA58C repeat (C2) of coagulation fac ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
UNC13A
Unc-13 homolog A (''C. elegans'') is a protein that in humans is encoded by the UNC13A gene. Function This gene encodes a member of the UNC13 family. UNC13A plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. It is involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool. In ''Drosophila melanogaster'', the protein has been shown to define the vesicle release site by regulating the coupling distance between synaptic vesicles and calcium channels in cooperation with another isoform, UNC13B. It is particularly important in most glutamatergic-mediated synapses as well as GABA-mediated synapses. It plays a role in dendrite formation by melanocytes and in secretory granule priming in insulin secretion. Protein structure Several conserved domains have been found in UNC13A. These conserved do ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
SSPO
SCO-spondin is a protein that in humans is encoded by the ''SSPO'' gene. SCO-spondin is secreted by the subcommissural organ, and contributes to commissure, commissural Axon#Development and growth, axon growth and the formation of Reissner's fiber, a fibrous aggregation of secreted molecules extending from the subcommissural organ to the end of the spinal cord. References Further reading * * * * * * * {{protein-stub Extracellular matrix proteins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
