Biology:Discoidin domain
| F5/8 type C domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of the membrane-binding C2 domain of factor VIII.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | F5_F8_type_C | ||||||||
| Pfam | PF00754 | ||||||||
| InterPro | IPR000421 | ||||||||
| PROSITE | PDOC00988 | ||||||||
| SCOP2 | 1fac / SCOPe / SUPFAM | ||||||||
| OPM superfamily | 46 | ||||||||
| OPM protein | 1sdd | ||||||||
| CDD | cd00057 | ||||||||
| |||||||||
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.[2][3][4] 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.[5] 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.[6][7] FA58C contains two conserved cysteines in most proteins, which link the extremities of the domain by a disulfide bond.[8][9][10] A further disulfide bond is located near the C-terminal of the second FA58C domain in MFGM Q08431.[10]
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
- ↑ "Structure and topography of the membrane-binding C2 domain of factor VIII in the presence of dodecylphosphocholine micelles". Biochem. J. 332 ( Pt 2) (Pt 2): 549–55. June 1998. doi:10.1042/bj3320549. PMID 9601086.
- ↑ "Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin". Proc. Natl. Acad. Sci. U.S.A. 83 (18): 6800–6804. 1986. doi:10.1073/pnas.83.18.6800. PMID 3092220.
- ↑ "A receptor tyrosine kinase found in breast carcinoma cells has an extracellular discoidin I-like domain". Proc. Natl. Acad. Sci. U.S.A. 90 (12): 5677–5681. 1993. doi:10.1073/pnas.90.12.5677. PMID 8390675.
- ↑ "Cloning and sequence analysis of human breast epithelial antigen BA46 reveals an RGD cell adhesion sequence presented on an epidermal growth factor-like domain". DNA Cell Biol. 15 (4): 281–286. 1996. doi:10.1089/dna.1996.15.281. PMID 8639264.
- ↑ "Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders". Blood 71 (3): 539–555. 1988. doi:10.1182/blood.V71.3.539.539. PMID 3125864.
- ↑ "Synthetic factor VIII peptides with amino acid sequences contained within the C2 domain of factor VIII inhibit factor VIII binding to phosphatidylserine". Blood 75 (10): 1999–2004. 1990. doi:10.1182/blood.V75.10.1999.1999. PMID 2110840.
- ↑ "Localization of functionally important epitopes within the second C-type domain of coagulation factor V using recombinant chimeras". J. Biol. Chem. 269 (22): 15898–15905. 1994. doi:10.1016/S0021-9258(17)40765-4. PMID 7515064.
- ↑ "Determination of the disulfide bridges in factor Va light chain". Biochemistry 32 (22): 5917–5923. 1993. doi:10.1021/bi00071a002. PMID 8504111.
- ↑ "Locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII (antihemophilic factor A)". Protein Sci. 4 (4): 740–746. 1995. doi:10.1002/pro.5560040413. PMID 7613471.
- ↑ 10.0 10.1 "Characterization of glycoprotein PAS-6/7 from membranes of bovine milk fat globules". Eur. J. Biochem. 240 (3): 628–636. September 1996. doi:10.1111/j.1432-1033.1996.0628h.x. PMID 8856064.
- Notes
Further reading
Baumgartner, S.; Hofmann, K.; Chiquet-Ehrismann, P.; Bucher, R. (1998). "The discoidin domain family revisited: New members from prokaryotes and a homology-based fold prediction". Protein Science 7 (7): 1626–1631. doi:10.1002/pro.5560070717. PMID 9684896.
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