| Type: | Domain | Name: | Coagulation factor 5/8 C-terminal domain |
| Description: | Blood coagulation factors V and VIII contain a C-terminal, twice repeated, domain of about 150 amino acids, which is called F5/8 type C, FA58C, or C1/C2-like 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 sharesa 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 havebeen detected in other extracellular and membrane proteins [, , ] In coagulation factors V and VIII the repeated domains compose part of alarger functional domain which promotes binding to anionic phospholipids on the surface of platelets and endothelial cells []. The C-terminal domain ofthe second FA58C repeat (C2) of coagulation factor VIII has been shown to be responsible for phosphatidylserine-binding and essential for activity [, ].It forms an amphipathic alpha-helix, which binds to the membrane [].FA58C contains two conserved cysteines in most proteins, which link the extremities of the domain by a disulphide bond [, , ]. A further disulphidebond is located near the C-terminal of the second FA58C domain in MFGM [].+------------------------------------------------------------------------+ | +-+ || | | | CxPLGxxQITASxxxxxRLxxxWxxxxWxxxxxxQGxxxxxxxxxxxxGNxxxxxxxxxxRxPxcxcLRxExGC'C': conserved cysteine involved in a disulphide bond. 'c': cysteine involved in a disulphide bond in MFGM . 'x': any amino acid.upper case letters: conserved residues. | Short Name: | FA58C |
