Coagulation factor 5/8 C-terminal domain (IPR000421)

Short name: FA58C

Overlapping homologous superfamilies

Domain relationships



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 [PMID: 3092220, PMID: 8390675, PMID: 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 [PMID: 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 [PMID: 2110840, PMID: 7515064]. It forms an amphipathic alpha-helix, which binds to the membrane [PMID: 7893714]. FA58C contains two conserved cysteines in most proteins, which link the extremities of the domain by a disulphide bond [PMID: 8504111, PMID: 7613471, PMID: 8856064]. A further disulphide bond is located near the C-terminal of the second FA58C domain in MFGM Q08431 [PMID: 8856064].

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'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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns
PROSITE patterns
PROSITE profiles