Protein Domain : IPR001846

Type:  Domain Name:  von Willebrand factor, type D domain
Description:  A family of growth regulators (originally called cef10, connective tissue growth factor, fisp-12, cyr61, or, alternatively, beta IG-M1 and beta IG-M2), all belong to immediate-early genes expressed after induction by growth factors or certain oncogenes. Sequence analysis of this family revealed the presence of four distinct modules. Each module has homologues in other extracellular mosaic proteins such as Von Willebrand factor, slit, thrombospondins, fibrillar collagens, IGF-binding proteins and mucins. Classification and analysis of these modules suggests the location of binding regions and, by analogy to better characterised modules in other proteins, sheds some light onto the structure of this new family [].The vWF domain is found in various plasma proteins: complement factors B, C2, CR3 and CR4; the integrins (I-domains); collagen types VI, VII, XII and XIV; and other extracellular proteins [, , ]. Although 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. Proteinsthat incorporate vWF domains participate in numerous biological events (e.g. cell adhesion, migration, homing, pattern formation, and signaltransduction), involving interaction with a large array of ligands []. A number of human diseases arise from mutations in VWA domains. Secondary structure prediction from 75 aligned vWF sequences has revealed a largely alternating sequence of alpha-helices and beta-strands [].One of the functions of von Willebrand factor (vWF) is to serve as a carrier of clotting factor VIII (FVIII). The native conformation of the D' domain of vWF is not only required for factor VIII (FVIII) binding but also for normal multimerisation and optimal secretion. The interaction between blood clotting factor VIII and VWF is necessary for normal survival of blood clotting factor VIII in blood circulation. The VWFD domain is a highly structured region, in which the first conserved Cys has been found to form a disulphide bridge with the second conserved one []. Short Name:  VWF_type-D
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0 Child Features

0 Contains

3 Cross Referencess

Identifier
PF00094
PS51233
SM00216

2 Found Ins

DB identifier Type Name
IPR012111 Family Hemolectin/hemocytin
IPR012011 Family von Willebrand factor

0 GO Annotation

0 Ontology Annotations

0 Parent Features

9 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Gohir.D11G242200.1.p PAC:38079751 Gossypium hirsutum 559  
Gohir.D11G242200.2.p PAC:38079752 Gossypium hirsutum 512  
Bobra.0161s0051.1.p PAC:40716600 Botryococcus braunii 286  
Bobra.0115s0010.1.p PAC:40724063 Botryococcus braunii 295  
Gotom.D11G276500.1.p A0A5D2ISI9 PAC:42224911 Gossypium tomentosum 559  
Gobar.D11G260500.1.p A0A2P5S9R0 PAC:42339187 Gossypium barbadense 559  
Gohir.D11G242200.2.p PAC:42380056 Gossypium hirsutum 512  
Gohir.D11G242200.1.p PAC:42380055 Gossypium hirsutum 559  
Godar.D11G274200.1.p A0A5D2ARL5 PAC:42535624 Gossypium darwinii 559  

5 Publications

First Author Title Year Journal Volume Pages PubMed ID
            1864378
            8145250
            8412987
            7687569
            10807780