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Symbol ADAMTS13 contributors: mct/pgu - updated : 23-02-2017
HGNC name ADAM metallopeptidase with thrombospondin type 1 motif, 13
HGNC id 1366
  • a N terminal signal sequence
  • a propeptide domain
  • a reprolysin-type catalytic domain and disintegrin loop
  • a thrombospondin type I (TSP1) module
  • a cysteine-rich/spacer domains essential for VWF-CP activity, required for ADAMTS13 binding to von Willebrand factor
  • seven TSP-like modules
  • a WXXW motif in its thrombospondin type 1 repeat domain (TSR1), important for the secretion of ADAMTS13 and that modulates the proteolytic cleavage of VWF by ADAMTS13 under denaturing conditions
  • a disintegrin-like domain having an essential role
  • in ADAMTS13 function
  • at the C terminus two segments with homology to the CUB domain, thrombospondin type 1 and CUB domains modulating interaction with von Willebrand factor (VWF C-terminal binding site may participate as the initial step of a multistep interaction ultimately leading to proteolysis of VWF by ADAMTS13)
  • conjugated MetalloP
    mono polymer heptamer
    isoforms Precursor
    interspecies homolog to murine Adamts13
  • ADAMTS (a disintegrin and metalloproteinase with thrombospondin motif) protein family
  • CATEGORY enzyme
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    text plasma (low level)
    basic FUNCTION
  • specifically cleaves the Tyr-1605-Met-1606 bond in the A2 domain of von Willebrand factor (VWF) to regulate the polymer distribution of VWF in circulation, which is critical for primary hemostasis
  • may playing a functional role in the local regulation of platelet function at the site of vascular injury or thrombus formation
  • could participate in the pathophysiology of preeclampsia
  • regulates the platelet aggregation function of VWF via proteolysis)
  • ADAMTS13 activity is an important determinant in platelet-vessel wall interaction
  • ADAMTS13 function is dependent upon multiple exosites that specifically bind the unraveled VWF A2 domain and enable proteolysis
  • regulates blood coagulation by cleaving von Willebrand factor (VWF), reducing its procoagulant activity
  • might have a potential regulation role for VWF inside cells
  • regulates a key physiological process of coagulation in the circulation by cleaving VWF multimers into small, inactive fragments
  • CELLULAR PROCESS protein, degradation
    text normal vascular homeostasis
    a component
    small molecule metal binding,
  • Zn2+
  • protein
  • cooperative activity between the middle carboxyl-terminal THBS1 repeats and the distal carboxyl-terminal CUB domains of ADAMTS13 may be crucial for recognition and cleavage of VWF under flow
  • interacting with THBS1 (THBS1 played competitively inhibitory role in ADAMTS13 binding and cleaving of VWF, and the potential competition might happen within A2 and A3 domains)
  • F8 accelerates proteolytic cleavage of VWF by ADAMTS13 under fluid shear stress
  • interacting with VWF (regulation of VWF multimeric size and platelet-tethering function is carried out by ADAMTS13, a plasma metalloprotease that is constitutively active)
  • binding of ADAMTS13 to Lys-PLG may play an important role to localize these two proteases at sites of thrombus formation or vascular injury where the fibrinolytic system is activated
  • PPIB is an important factor in the proper maturation and secretion of ADAMTS13
  • ADAMTS13-induced endothelial cell angiogenesis occurs via the upregulation of VEGFA and phosphorylation of KDR and this angiogenic activity depends on the C-terminal TSP1 repeats of ADAMTS13
  • ADAMTS13 proteolytically regulates the platelet-tethering function of von Willebrand factor (VWF)
  • ADAMTS13 is a specific von Willebrand factor (VWF)-cleaving protease, preventing microvascular thrombosis of VWF/platelet thrombi
  • is the key protease that regulates the multimeric state of VWF
  • cell & other
  • binding to endothelial cell plasma membrane through its COOH-terminal thrombospondin type 1 repeats
  • prebound ADAMTS13 to endothelial cells exhibits increased proteolysis of VWF
    activated by GP1BA for the cleavage of VWF
    Other is regulated by substrate-induced allosteric activation, which may optimize VWF cleavage under fluid shear stress
    becomes conformationally activated on demand through interaction of its C-terminal CUB domains with VWF, making it susceptible to immune recognition
    corresponding disease(s) TTPF
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional       loss of function
    in preeclampsia
    constitutional     --low  
    in the maternal and cord blood were lower in the preeclampsia group than in the control group
    Susceptibility to thrombotic disorders
    Variant & Polymorphism SNP , other ADAMTS13-binding IgG are present in patients with thrombotic thrombocytopenic purpura
    Candidate gene
    Therapy target
  • Adamts13 deficiency in mice does not affect adipose tissue development
  • Adamts13 levels are significantly reduced in the plasma of CypB-deficient mice