InterPro: IPR000421 Coagulation factor 5/8 type, C-terminal

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 [1, 2, 3] 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 [4]. 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 [5, 6]. It forms an amphipathic alpha-helix, which binds to the membrane [7]. FA58C contains two conserved cysteines in most proteins, which link the extremities of the domain by a disulphide bond [8, 9, 10]. A further disulphide bond is located near the C-terminal of the second FA58C domain in MFGM Q08431 [10].

  +------------------------------------------------------------------------+
  |                                                               +-+      |
  |                                                               | |      |
  CxPLGxxQITASxxxxxRLxxxWxxxxWxxxxxxQGxxxxxxxxxxxxGNxxxxxxxxxxRxPxcxcLRxExGC

'C': conserved cysteine involved in a disulphide bond.
'c': cysteine involved in a disulphide bond in MFGM Q08431.
'x': any amino acid.
upper case letters: conserved residues.