The domain within your query sequence starts at position 20 and ends at position 150; the E-value for the F5_F8_type_C domain shown below is 5.8e-11.



PFAM accession number:PF00754
Interpro abstract (IPR000421): 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 [(PUBMED:3092220), (PUBMED:8390675), (PUBMED:8639264)] 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 [(PUBMED:3125864)]. 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 [(PUBMED:2110840), (PUBMED:7515064)]. It forms an amphipathic alpha-helix, which binds to the membrane [(PUBMED:7893714)]. FA58C contains two conserved cysteines in most proteins, which link the extremities of the domain by a disulphide bond [(PUBMED:8504111), (PUBMED:7613471), (PUBMED:8856064)]. A further disulphide bond is located near the C-terminal of the second FA58C domain in MFGM Q08431 [(PUBMED:8856064)].

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'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.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry F5_F8_type_C