MGP Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins
MGP003306

UniProt Annotations

Entry Information
Gene Namevon Willebrand factor
Protein EntryVWF_HUMAN
UniProt IDP04275
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=P04275-1; Sequence=Displayed; Name=2; IsoId=P04275-2; Sequence=VSP_056527, VSP_056528, VSP_056529; Note=No experimental confirmation available.;
Diseasevon Willebrand disease 1 (VWD1) [MIM:193400]: A common hemorrhagic disorder due to defects in von Willebrand factor protein and resulting in impaired platelet aggregation. Von Willebrand disease type 1 is characterized by partial quantitative deficiency of circulating von Willebrand factor, that is otherwise structurally and functionally normal. Clinical manifestations are mucocutaneous bleeding, such as epistaxis and menorrhagia, and prolonged bleeding after surgery or trauma. {ECO:0000269|PubMed:10887119, ECO:0000269|PubMed:11698279}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Diseasevon Willebrand disease 2 (VWD2) [MIM:613554]: A hemorrhagic disorder due to defects in von Willebrand factor protein and resulting in altered platelet aggregation. Von Willebrand disease type 2 is characterized by qualitative deficiency and functional anomalies of von Willebrand factor. It is divided in different subtypes including 2A, 2B, 2M and 2N (Normandy variant). The mutant VWF protein in types 2A, 2B and 2M are defective in their platelet-dependent function, whereas the mutant protein in type 2N is defective in its ability to bind factor VIII. Clinical manifestations are mucocutaneous bleeding, such as epistaxis and menorrhagia, and prolonged bleeding after surgery or trauma. {ECO:0000269|PubMed:12406074, ECO:0000269|PubMed:1409710, ECO:0000269|PubMed:1419803, ECO:0000269|PubMed:1419804, ECO:0000269|PubMed:1420817, ECO:0000269|PubMed:1429668, ECO:0000269|PubMed:1672694, ECO:0000269|PubMed:1673047, ECO:0000269|PubMed:1729889, ECO:0000269|PubMed:1761120, ECO:0000269|PubMed:1832934, ECO:0000269|PubMed:1906179, ECO:0000269|PubMed:2010538, ECO:0000269|PubMed:2011604, ECO:0000269|PubMed:21592258, ECO:0000269|PubMed:2786201, ECO:0000269|PubMed:7620154, ECO:0000269|PubMed:7734373, ECO:0000269|PubMed:7789955, ECO:0000269|PubMed:8011991, ECO:0000269|PubMed:8123843, ECO:0000269|PubMed:8123844, ECO:0000269|PubMed:8338947, ECO:0000269|PubMed:8348943, ECO:0000269|PubMed:8376405, ECO:0000269|PubMed:8435341, ECO:0000269|PubMed:8486782, ECO:0000269|PubMed:8547152, ECO:0000269|PubMed:8622978}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Diseasevon Willebrand disease 3 (VWD3) [MIM:277480]: A severe hemorrhagic disorder due to a total or near total absence of von Willebrand factor in the plasma and cellular compartments, also leading to a profound deficiency of plasmatic factor VIII. Bleeding usually starts in infancy and can include epistaxis, recurrent mucocutaneous bleeding, excessive bleeding after minor trauma, and hemarthroses. {ECO:0000269|PubMed:10887119, ECO:0000269|PubMed:7989040, ECO:0000269|PubMed:8088787}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainThe von Willebrand antigen 2 is required for multimerization of vWF and for its targeting to storage granules.
FunctionImportant in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma.
InteractionSelf; NbExp=15; IntAct=EBI-981819, EBI-981819; Q76LX8:ADAMTS13; NbExp=5; IntAct=EBI-981819, EBI-981764; P07359:GP1BA; NbExp=2; IntAct=EBI-981819, EBI-297082; Q96CV9:OPTN; NbExp=2; IntAct=EBI-981819, EBI-748974;
PtmAll cysteine residues are involved in intrachain or interchain disulfide bonds.
PtmN- and O-glycosylated. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218}.
Sequence CautionSequence=AAB59512.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
SimilarityContains 1 CTCK (C-terminal cystine knot-like) domain. {ECO:0000255|PROSITE-ProRule:PRU00039}.
SimilarityContains 3 VWFA domains. {ECO:0000255|PROSITE- ProRule:PRU00219}.
SimilarityContains 3 VWFC domains. {ECO:0000255|PROSITE- ProRule:PRU00220}.
SimilarityContains 4 TIL (trypsin inhibitory-like) domains. {ECO:0000305}.
SimilarityContains 4 VWFD domains. {ECO:0000255|PROSITE- ProRule:PRU00580}.
Subcellular LocationSecreted {ECO:0000269|PubMed:10961880}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10961880}. Note=Localized to storage granules.
SubunitMultimeric. Interacts with F8. {ECO:0000269|PubMed:10961880, ECO:0000269|PubMed:9218428}.
Tissue SpecificityPlasma.
Web ResourceName=vWF; Note=von Willebrand factor (vWF) mutation db; URL="http://www.vwf.group.shef.ac.uk/";
Web ResourceName=Wikipedia; Note=Von Willebrand factor entry; URL="http://en.wikipedia.org/wiki/Von_Willebrand_factor";
  logo