Discoidin domain (also known as F5/8 type C domain, or C2-like domain) is major
protein domain
In molecular biology, a protein domain is a region of a protein's Peptide, polypeptide chain that is self-stabilizing and that Protein folding, folds independently from the rest. Each domain forms a compact folded Protein tertiary structure, thre ...
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 .
Human proteins containing this domain
AEBP1;
BTBD9;
CASPR4;
CNTNAP1;
CNTNAP2;
CNTNAP3;
CNTNAP4;
CNTNAP5;
CPXM1;
CPXM2;
DCBLD1;
DCBLD2;
DDR1;
DDR2;
EDIL3;
F5;
F8;
F8B;
MFGE8;
NRP1;
NRP2;
RS1;
SSPO;
UNC13A
References
;Notes
Further reading
{{DEFAULTSORT:Discoidin Domain
Protein domains
Single-pass transmembrane proteins