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0VWF_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameVWF
DescriptionVon willebrand factor precursor (vwf) .
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (NAS)
0005515 protein binding (IPI)
0007155 cell adhesion (TAS)
0030168 platelet activation (NAS)
0009611 response to wounding (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
A family of growth regulators (originally called cef10.onnective tissue growth factor.isp-12.yr61.r.lternatively.eta IG-M1 and beta IG-M2).ll 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.lit.hrombospondins.ibrillar collagens.GF-binding proteins and mucins. Classification and analysis of these modules suggests the location of binding regions and.y analogy to better characterized modules in other proteins.heds some light onto the structure of this new family .The vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal 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.igration.oming.attern formation.nd signaltransduction).nvolving 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 multimerization and optimal secretion .
  IPR001846:von Willebrand factor, type D
The von Willebrand factor is a large multimeric glycoprotein found in bloodplasma. Mutant forms are involved in the aetiology of bleeding disorders . In von Willebrand factor.he type A domain (vWF) is the prototype fora protein superfamily. The vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal 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.igration.oming.attern formation.nd signaltransduction).nvolving 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 . Foldrecognition algorithms were used to score sequence compatibility with alibrary of known structures: the vWF domain fold was predicted to be adoubly-wound.pen.wisted beta-sheet flanked by alpha-helices . 3D structures have been determined for the I-domains of integrins CD11b(with bound magnesium) and CD11a (with bound manganese) . The domain adopts a classic alpha/beta Rossmann fold and contains an unusual metal ion coordination site at its surface. It has been suggested that this siterepresents a general metal ion-dependent adhesion site (MIDAS) for binding protein ligands . The residues constituting the MIDAS motif in the CD11band CD11a I-domains are completely conserved.ut the manner in which the metal ion is coordinated differs slightly .
  IPR002035:von Willebrand factor, type A
Four recent crystal structures of growth factors--nerve growth factor.ransforming growth factor-beta.latelet-derived growth factor.nd human chorionic gonadotropin--from four separate superfamilies revealed that these proteins are structurally related and share a common overall topology . These proteins have very little sequence homology.ut they all have an unusual arrangement of six cysteines linked to form a "cystine-knot" conformation. The active forms of these proteins are dimers.ither homo- or heterodimers . Because of their shape.here appears to be an intrinsic requirement for the cystine-knot growth factors to form dimers. This extra level of organization increases the variety of structures built around this simple structural motif .
  IPR006207:Cystine knot, C-terminal
The vWF domain is found in various plasma proteins:complement factors B.2.R3 and CR4; the integrins (I-domains); collagen types VI.II.II and XIV; and other extracellular proteins . Although the majority of VWA-containing proteins are extracellular.he most ancient ones present in all eukaryotes are all intracellular proteins involved in functions such as transcription.NA repair.ibosomal 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.igration.oming.attern formation.nd signaltransduction).nvolving 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 .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 . For the von Willebrand factor the duplicated VWFC domain is thought to participate in oligomerization.ut not in the initial dimerization step . The presence of this region in a number of other complex-forming proteins points to the possible involvment of the VWFC domain in complex formation.
  IPR001007:von Willebrand factor, type C
This domain is found in proteinase inhibitors as well as in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7.-6.-5.-10 and 8-9.This inhibitor domain belongs to MEROPS inhibitor family I8 (clan IA). Proteins containing this domain inhibit peptidases belonging to families S1 ().8 ().nd M4 () and are restricted to the chordata.ematoda.rthropoda and echinodermata. Examples of proteins containing this domain are:chymotrypsin/elastase inhibitor from Ascaris suum (pig roundworm)Acp62F protein from Drosophila melanogasterBombina trypsin inhibitor from Bombina maxima (large-webbed bell toad)Bombyx subtilisin inhibitor from Bombyx mori (silk moth)von Willebrand factor
  IPR002919:Protease inhibitor I8, cysteine-rich trypsin inhibitor-like
This SSF signature was designed to identify serine proteases inhibitors belonging to the grasshopper PMP inhibitor family .nd to the desert locust SGCI/SGTI family .oth of which belong to MEROPS inhibitor family I19.lan IW. The PMP inhibitors have a conserved array of six cysteine residues (Cys-Xaa(9-12)-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa(2-3)-Gly-Xaa(3-4)-Cys-Thr-Xaa(3)-Cys).hich are involved in an identical disulfide bridge pattern (Cys(1)-Cys(4).ys(2)-Cys(6).ys(3)-Cys(5)) . Some of the PMP inhibitors are fucosylated.he function of the fucose moiety being unknown.The signature also matches many proteins which are not known to be proteinase inhibitors.nd which are annotated as mucin.CO-spondin.ollagen alpha 1.agged1.agged2 or von Willebrand factor.ype D and type C.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009041:Proteinase inhibitor, PMP and SGCI
von Willebrand factor (vWF) is a multimeric adhesive protein that plays a key role in platelet function by mediating the initiation and progression of thrombus formation at sites of vascular injury . Binding of vWF to platelet membrane glycoprotein GPIb-alpha () of the GPIb-IX-V complex supports the arrest of bleeding after tissue trauma. The rapid association of GP1b-alpha with vWF not only initiates platelet deposition at the sites of vascular injury but is essential for maintaining thrombus growth in blood flowing at high shear rates.
  IPR012011:von Willebrand factor
IPR001846:VWD 
Evalue:-54.6382721639824 
Location:377-540IPR002035:VWA 
Evalue:-48.6197891235352 
Location:1498-1664IPR001846:VWD 
Evalue:-44.698970004336 
Location:1938-2101IPR002035:VWA 
Evalue:-43.7695503234863 
Location:1691-1864IPR001846:VWD 
Evalue:-42.6575775146484 
Location:867-1013IPR001846:VWD 
Evalue:-36.8860549926758 
Location:35-179IPR002035:VWA 
Evalue:-35.9208183288574 
Location:1277-1457IPR006207:CT 
Evalue:-34.3872161432803 
Location:2727-2812IPR001007:VWC 
Evalue:-23.8860569000244 
Location:2431-2494IPR001007:VWC 
Evalue:-23.4814853668213 
Location:2257-2325IPR001007:VWC 
Evalue:-20.4685211181641 
Location:2582-2644IPR002919:TIL 
Evalue:-12.4948501586914 
Location:652-707IPR002919:TIL 
Evalue:-12.0705814361572 
Location:295-348IPR002919:TIL 
Evalue:-9.95860767364502 
Location:1146-1196IPR002919:Cysrich_TIL 
Evalue:0 
Location:765-837IPR002919:Cysrich_TIL 
Evalue:0 
Location:2201-2254IPR009041:PMP_SGCI 
Evalue:0 
Location:838-866
SequencesProtein: VWF_HUMAN (2813 aa)
mRNA: X04385
Local Annotation
Synapse Ontology
the mechanism by which the restiong potential is held.
sdb:0288 maintain membrane potential  (Evidence:keywords)
KO assignmentK03900
  Level 3 annotation:
    von Willebrand factor
  Level 2 annotation:
    ECM-receptor interaction
    CAM ligands
    Focal adhesion
    Complement and coagulation cascades
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 75 residues, 5928407-5928630Exon2: 34 residues, 5929212-5929310Exon3: 15 residues, 5931270-5931310Exon4: 45 residues, 5931817-5931946Exon5: 35 residues, 5932922-5933021Exon6: 41 residues, 5946912-5947029Exon7: 15 residues, 5947553-5947594Exon8: 62 residues, 5948637-5948818Exon9: 39 residues, 5951025-5951136Exon10: 52 residues, 5955537-5955687Exon11: 70 residues, 5961212-5961418Exon12: 37 residues, 5962576-5962681Exon13: 27 residues, 5964471-5964546Exon14: 36 residues, 5964989-5965092Exon15: 68 residues, 5971245-5971445Exon16: 116 residues, 5973288-5973630Exon17: 66 residues, 5973841-5974034Exon18: 75 residues, 5975428-5975649Exon19: 61 residues, 5991043-5991221Exon20: 16 residues, 5991513-5991557Exon21: 57 residues, 5992907-5993072Exon22: 50 residues, 5995515-5995659Exon23: 49 residues, 5995942-5996083Exon24: 41 residues, 5996180-5996297Exon25: 461 residues, 5997791-5999170Exon26: 47 residues, 6001326-6001462Exon27: 55 residues, 6002166-6002325Exon28: 54 residues, 6003057-6003214Exon29: 40 residues, 6005006-6005120Exon30: 49 residues, 6005332-6005473Exon31: 51 residues, 6008768-6008915Exon32: 47 residues, 6010870-6011005Exon33: 48 residues, 6014114-6014253Exon34: 36 residues, 6015814-6015918Exon35: 55 residues, 6023717-6023878Exon36: 33 residues, 6026149-6026244Exon37: 82 residues, 6031969-6032210Exon38: 74 residues, 6036283-6036499Exon39: 67 residues, 6037275-6037471Exon40: 35 residues, 6042380-6042481Exon41: 48 residues, 6043672-6043811Exon42: 47 residues, 6044563-6044700Exon43: 17 residues, 6050723-6050770Exon44: 39 residues, 6051757-6051869Exon45: 43 residues, 6053045-6053168Exon46: 74 residues, 6054761-6054978Exon47: 43 residues, 6074886-6075011Exon48: 71 residues, 6089800-6090009Exon49: 36 residues, 6090292-6090395Exon50: 57 residues, 6100600-6100765Exon51: 20 residues, 6102568-6102623Exon52: 35 residues, 6103847-6103946Exon53: 2 residues, -Jump to VWF_HUMAN  
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Loci Cluster (Details)Loci: 4009 6326275-6354976 ~-29K 8222(SCNN1A)(-)Loci: 2731 6424326-6431144 ~-7K 8225(TNFRSF7)(+)Loci: 4010 6441666-6450104 ~-8K 8228(VAMP1)(-)Loci: 4011 6518966-6535498 ~-17K 8239(-)Loci: 4012 6549509-6586812 ~-37K 8245(CHD4)(-)Loci: 4013 6598261-6615548 ~-17K 8247(GPR92)(-)Loci: 2732 6703481-6711289 ~-8K 8256(COPS7A)(+)Loci: 2733 6846966-6850253 ~-3K 8271(TPI1)(+)Loci: 2734 7174236-7201985 ~-28K 8292(CLSTN3)(+)Loci: 4008 5928407-6103946 ~-176K 8213(VWF)(-)Link out to UCSC