ADAMTS20
ADAMTS20 (ADAM metallopeptidase with thrombospondin type 1 motif 20, also known as GON-1) is a secreted, zinc-dependent metalloprotease of the ADAMTS family. It cleaves the proteoglycan versican and sheds MMP14 from the cell surface, and it contributes to extracellular matrix proteolysis and ciliogenesis. Browse Assay Genie's current range of ADAMTS20 research reagents below, or read on for the biology behind the target.
ADAMTS20 is a member of the ADAMTS family of zinc-dependent proteases. Its best-defined catalytic activity is the cleavage of a peptide bond in the large aggregating proteoglycan versican, at the Glu1428-Ala1429 site. It also catalyses the shedding of the endopeptidase MMP14 at the Tyr314-Gly315 site, releasing the catalytic domain from the cell surface and so preventing downstream pro-MMP2 activation. Through these activities the protein is involved in extracellular matrix proteolysis, and it has also been linked to ciliogenesis.
UniProt additionally notes that ADAMTS20 may have a protease-independent role in promoting the transport of a variety of secretory cargos from the endoplasmic reticulum to the Golgi apparatus. The ADAMTS20 gene encodes a protein with a signal peptide that is cleaved to release the mature peptide. The mature protein is secreted and found in the extracellular matrix, and UniProt also records it in the cilium. The mouse ortholog is Adamts20.
ADAMTS20 belongs to the HGNC gene group of ADAM metallopeptidases with thrombospondin type 1 motif. Its previous name was a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 20, and GON-1 is a recorded alias. According to the NCBI Gene summary, the protein may be involved in tissue remodelling. Researchers studying ADAMTS20 often work with an ADAMTS20 antibody or ADAMTS20 protein to follow its processing and localisation in matrix and ciliary compartments.
ADAMTS20 cleaves versican in the extracellular matrix and is proposed to contribute to tissue remodelling.
By shedding the MMP14 catalytic domain from the cell surface, ADAMTS20 prevents downstream pro-MMP2 activation.
ADAMTS20 is involved in ciliogenesis and is found in the cilium, making it relevant to studies of cilium formation.
A possible protease-independent role in endoplasmic reticulum to Golgi transport of secretory cargos is of interest in trafficking studies.
ADAMTS20 is a secreted metalloprotease that cleaves versican at the Glu1428-Ala1429 site and sheds MMP14 at the Tyr314-Gly315 site, preventing downstream pro-MMP2 activation. It is involved in extracellular matrix proteolysis and ciliogenesis, and may also aid endoplasmic reticulum to Golgi transport independently of its protease activity.
The HGNC name is ADAM metallopeptidase with thrombospondin type 1 motif 20, and GON-1 is a recorded alias. UniProt calls it a disintegrin and metalloproteinase with thrombospondin motifs 20. An earlier HGNC name was a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 20.
A mouse ortholog, Adamts20, is recorded for the human gene. The source data list no rat ortholog. Researchers working in other species should check the datasheet of any product for its validated reactivity.
Other ADAMTS family proteases involved in extracellular matrix proteolysis and tissue remodelling.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P59510; product specifications from Assay Genie datasheets.