ADAMTS13

This gene encodes a member of a family of proteins containing several distinct regions, including a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. The enzyme encoded by this gene specifically cleaves von Willebrand Factor (vWF). Defects in this gene are associated with thrombotic thrombocytopenic purpura. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013]

Full Name

ADAM Metallopeptidase With Thrombospondin Type 1 Motif 13

Function

Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.

Biological Process

Cell-matrix adhesion
Cellular response to interferon-gamma
Cellular response to interleukin-4
Cellular response to lipopolysaccharide
Cellular response to tumor necrosis factor
Extracellular matrix organization
Glycoprotein metabolic process
Integrin-mediated signaling pathway
Peptide catabolic process
Platelet activation
Protein processing
Proteolysis
Response to amine
Response to potassium ion
Response to toxic substance

Cellular Location

Secreted. Secretion enhanced by O-fucosylation of TSP type-1 repeats.

Involvement in disease

Thrombotic thrombocytopenic purpura, hereditary (TTP): An autosomal recessive hematologic disease characterized by hemolytic anemia with fragmentation of erythrocytes, thrombocytopenia, diffuse and non-focal neurologic findings, decreased renal function and fever.

PTM

Glycosylated. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X2-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS13. May also be C-glycosylated on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and also N-glycosylated. These other glycosylations can also facilitate secretion.
The precursor is processed by a furin endopeptidase which cleaves off the pro-domain.