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Discoidin domain (also known as F5/8 type C domain, or C2-like domain) is major protein domain of many blood coagulation factors. Blood coagulation factors V and VIII contain a C-terminal, twice repeated, domain of about 150 amino acids, which is often called "C2-like domain" (that is unrelated to the C2 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 whi

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dbo:abstract
  • Discoidin domain (also known as F5/8 type C domain, or C2-like domain) is major protein domain of many blood coagulation factors. Blood coagulation factors V and VIII contain a C-terminal, twice repeated, domain of about 150 amino acids, which is often called "C2-like domain" (that is unrelated to the C2 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. FA58C contains two conserved cysteines in most proteins, which link the extremities of the domain by a disulfide bond. A further disulfide bond is located near the C-terminal of the second FA58C domain in MFGM Q08431. (en)
dbo:symbol
  • F5_F8_type_C
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dbo:wikiPageID
  • 14683611 (xsd:integer)
dbo:wikiPageLength
  • 6431 (xsd:nonNegativeInteger)
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  • 1040886238 (xsd:integer)
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dbp:caption
  • Structure of the membrane-binding C2 domain of factor VIII. (en)
dbp:cdd
  • cd00057 (en)
dbp:interpro
  • IPR000421 (en)
dbp:name
  • F5/8 type C domain (en)
dbp:opmFamily
  • 46 (xsd:integer)
dbp:opmProtein
  • 1 (xsd:integer)
dbp:pfam
  • PF00754 (en)
dbp:prosite
  • PDOC00988 (en)
dbp:scop
  • 1 (xsd:integer)
dbp:symbol
  • F5_F8_type_C (en)
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rdfs:comment
  • Discoidin domain (also known as F5/8 type C domain, or C2-like domain) is major protein domain of many blood coagulation factors. Blood coagulation factors V and VIII contain a C-terminal, twice repeated, domain of about 150 amino acids, which is often called "C2-like domain" (that is unrelated to the C2 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 whi (en)
rdfs:label
  • Discoidin domain (en)
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