Coagulation factor 5/8, C-terminal domain
IPR000421
Definition
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 [[cite:PMID:3092220], [cite:PMID:8390675], [cite: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 [[cite:PMID:2110840], [cite:PMID:7515064]]. It forms an amphipathic α-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 [[cite:PMID:8504111], [cite:PMID:7613471], [cite:PMID:8856064]]. A further disulphide bond is located near the C-terminal of the second FA58C domain in MFGM [swissprot:Q08431] PMID:8856064. +------------------------------------------------------------------------+ | +-+ | | | | | CxPLGxxQITASxxxxxRLxxxWxxxxWxxxxxxQGxxxxxxxxxxxxGNxxxxxxxxxxRxPxcxcLRxExGC 'C': conserved cysteine involved in a disulphide bond. 'c': cysteine involved in a disulphide bond in MFGM [swissprot:Q08431]. 'x': any amino acid. upper case letters: conserved residues.
23 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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