Due to improvement work scheduled on this server, some services may not be fully operational on Tuesday December 12 daytime (CEST).
To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS. To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017. From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...] View this page in https
The VWFC domain is named after the von Willebrand factor (VWF) type C repeat
which is found twice in this multidomain protein [1,2]. It has a length of
about 70 amino acids covering 10 well conserved cysteines. Proteins with such
a domain [1,2,3,4] are listed below.
Human von Willebrand factor (VWF), a multifunctional protein involved in
maintaining homeostasis. It consists of 4 VWFD domains, 3 VWFA domains, 3
VWFB domains, 3 VWFC domains, an X domain and a C-terminal cystine knot .
Silk moth hemocytin, an humoral lectin which is involved in a self-defence
mechanism. It is composed of 2 FA58C domains (see <PDOC00988>), a C-type
lectin domain (see <PDOC00537>), 2 VWFC domains, and a CTCK (see
Several vertebrate heavily glycosylated mucins. Human mucin 2 is secreted
by the epithelia of different mucus membrane-containing organs. It is a
highly polymorphic multidomain molecule. Rat intestinal mucin-like peptide
coats the epithelia of the intestines. Both proteins share a modular
architecture similar to VWF. Xenopus mucin B.1 contains a Sushi domain, a
VWFC domain, a X domain and a C-terminal cystine knot. Other mucins that
contain the VWFC domain are human tracheobronchial mucin (MUC5), bovine
submaxillary mucin-like protein, human and pig apomucin.
Cef-10/cyr61/CTGF/fisp-12/nov protein family. The members of this family
are structurally related to insulin-like growth factor binding proteins
(see <PDOC00194>) and could function as growth factor-binding proteins.
They contain an insulin-like growth factor-binding domain, a VWFC repeat, a
thrombospondin type 1 repeat (Tsp1) and a C-terminal cystine knot.
Vertebrate thrombospondins 1 and 2. These adhesive glycoproteins mediate
cell-to-cell and cell-to-matrix interactions. They are composed of a common
thrombospondin N-terminal domain (TspN), a VWFC domain, three Tsp type 1
repeats (Tsp1), 3 to 4 EGF-like domains and 7 calcium-binding Tsp3 repeats.
Vertebrate propeptides of fibrillar collagens α 1(I, II & III) and 2(V)
chains that contain an N-terminal VWFC domain, a collagenous region of
about 1000 amino acids and a C-terminus common to fibrillar collagens
Vertebrate integral membrane protein DGCR2/IDD, a potential adhesion
receptor with 1 LDL-receptor class A domain (see <PDOC00929>), a C-type
lectin and a VWFC domain.
Chordin, a Xenopus developmental protein that contains four VWFC domains.
Of these proteins, the best characterized one is the von Willebrand factor for
which the duplicated VWFC domain is thought to participate in oligomerization,
but not in the initial dimerization step . The presence of this region in
other complex-forming proteins leads to the assumption that the VWFC domain
might be involved in forming larger protein complexes [1,2].
The profile we developed covers the entire VWFC domain.
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.