| 词条 | Von Willebrand factor type C domain |
| 释义 |
| Symbol = VWC | Name = von Willebrand factor type C domain | image = | width = | caption = | Pfam= PF00093 | InterPro= IPR001007 | SMART= | Prosite = | SCOP = | TCDB = | OPM family= | OPM protein= | PDB= }}Von Willebrand factor, type C (VWFC or VWC)is a protein domain is found in various blood plasma proteins: complement factors B, C2, CR3 and CR4; the integrins (I-domains); collagen types VI, VII, XII and XIV; and other extracellular proteins.[1][2][3] FunctionAlthough the majority of VWA-containing proteins are extracellular, the most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription, DNA repair, ribosomal and membrane transport and the proteasome. A common feature appears to be involvement in multiprotein complexes. Proteins that incorporate vWF domains participate in numerous biological events (e.g. cell adhesion, migration, homing, pattern formation, and signal transduction), involving interaction with a large array of ligands.[1] Mutation effectsA number of human diseases arise from mutations in VWA domains.[2] The domain is named after the von Willebrand factor (VWF) type C repeat which is found in multidomain protein/multifunctional proteins involved in maintaining homeostasis.[3][4] For the von Willebrand factor the duplicated VWFC domain is thought to participate in oligomerization, but not in the initial dimerization step.[5] The presence of this region in a number of other complex-forming proteins points to the possible involvement of the VWFC domain in complex formation. Human proteins containing this domain
Chordin family
Collagen family
Mucin family
Thrombospondin superfamily
CCN family
References1. ^1 {{cite journal |vauthors=Colombatti A, Bonaldo P, Doliana R |title=Type A modules: interacting domains found in several non-fibrillar collagens and in other extracellular matrix proteins |journal=Matrix |volume=13 |issue=4 |pages=297–306 |year=1993 |pmid=8412987 |doi=10.1016/S0934-8832(11)80025-9}} {{InterPro content|IPR001007}}2. ^1 {{cite journal |vauthors=Smith KF, Haris PI, Chapman D, Perkins SJ, Williams SC, Sim RB |title=The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy. Its occurrence in collagen types VI, VII, XII and XIV, the integrins and other proteins by averaged structure predictions |journal=J. Mol. Biol. |volume=238 |issue=1 |pages=104–119 |year=1994 |pmid=8145250 |doi=10.1006/jmbi.1994.1271}} 3. ^1 {{cite journal |author=Bork P |title=Shuffled domains in extracellular proteins |journal=FEBS Lett. |volume=286 |issue=1 |pages=47–54 |year=1991 |pmid=1864378 |doi=10.1016/0014-5793(91)80937-X}} 4. ^{{cite journal |vauthors=Hunt LT, Barker WC |title=von Willebrand factor shares a distinctive cysteine-rich domain with thrombospondin and procollagen |journal=Biochem. Biophys. Res. Commun. |volume=144 |issue=2 |pages=876–882 |year=1987 |pmid=3495268 |doi=10.1016/S0006-291X(87)80046-3}} 5. ^{{cite journal |vauthors=Voorberg J, Fontijn R, Calafat J, Janssen H, van Mourik JA, Pannekoek H |title=Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids |journal=J. Cell Biol. |volume=113 |issue=1 |pages=195–205 |year=1991 |pmid=2007623|pmc=2288914|doi=10.1083/jcb.113.1.195 }} 3 : VWFC domain|Protein domains|Protein families |
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