| 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 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 factor VIII has been shown to be responsible for phosphatidylserine-binding and essential for activity [, ]. It forms an amphipathic α-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 disulphide bond 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. | Name | Coagulation factor 5/8, C-terminal domain |
| Short Name | FA58C | Type | Domain |
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