ADAMTS9
ADAMTS9 (a disintegrin and metalloproteinase with thrombospondin motifs 9, also known as KIAA1312) is a secreted zinc metalloprotease of the ADAMTS family. It cleaves large proteoglycans and sheds the endopeptidase MMP14, and it also acts in ciliogenesis and secretory transport. Browse Assay Genie's current range of ADAMTS9 research reagents below, or read on for the biology behind the target.
ADAMTS9 is a metalloendopeptidase that cleaves the large aggregating proteoglycans aggrecan, at the Glu1838-Ala1839 bond, and versican, at the Glu1428-Ala1429 bond. It also catalyses the shedding of the endopeptidase MMP14 at the Tyr314-Gly315 site. This releases the catalytic domain from the cell surface and so prevents downstream pro-MMP2 activation. The enzyme is involved in extracellular matrix proteolysis and, in a manner that depends on its metalloendopeptidase activity, in the growth of the ciliary vesicle during ciliogenesis.
The protein also has a protease-independent function: it promotes the transport of a variety of secretory cargos from the endoplasmic reticulum to the Golgi apparatus. This fits its reported localisation, which spans the extracellular matrix, the endoplasmic reticulum, the cilium and recycling endosomes. The ADAMTS9 gene encodes a member of the ADAMTS family. Family members share a propeptide region, a metalloproteinase domain, a disintegrin-like domain and a thrombospondin type 1 (TS) motif, and they differ in the number of C-terminal TS motifs. Some have unique C-terminal domains. The mouse ortholog is Adamts9.
ADAMTS family members have been implicated in proteoglycan cleavage, in the control of organ shape during development and in the inhibition of angiogenesis. The ADAMTS9 gene lies on chromosome 3p14, a region known to be lost in hereditary renal tumours. Alternative splicing gives multiple transcript variants that encode different isoforms, which may undergo similar proteolytic processing. KIAA1312 is a former symbol for the gene, which HGNC places in the group of ADAM metallopeptidases with thrombospondin type 1 motif.
ADAMTS9 cleaves aggrecan and versican, making it a useful subject for studies of proteoglycan turnover and extracellular matrix remodelling.
Its metalloendopeptidase activity contributes to ciliary vesicle growth during ciliogenesis, which makes it relevant to studies of cilium assembly.
By shedding MMP14 from the cell surface, ADAMTS9 limits downstream pro-MMP2 activation, linking it to metalloprotease regulation.
A protease-independent role in endoplasmic reticulum to Golgi transport of secretory cargos makes ADAMTS9 relevant to secretory trafficking studies.
ADAMTS9 is a secreted metalloprotease that cleaves aggrecan and versican and sheds MMP14 from the cell surface. It contributes to extracellular matrix proteolysis and to ciliary vesicle growth during ciliogenesis. Separately, it promotes endoplasmic reticulum to Golgi transport of secretory cargos independently of its protease activity.
The HGNC full name is ADAM metallopeptidase with thrombospondin type 1 motif 9, and UniProt calls the protein A disintegrin and metalloproteinase with thrombospondin motifs 9. KIAA1312 is a previous symbol. The older name is a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 9. Alternative splicing produces several isoforms.
The ADAMTS9 gene lies in a chromosome 3p14 region known to be lost in hereditary renal tumours. ADAMTS family members are also linked to proteoglycan cleavage, organ shape control and angiogenesis inhibition. A mouse ortholog, Adamts9, exists; check the datasheet of any product for its validated reactivity.
Other ADAMTS family proteases, including proteoglycan-cleaving enzymes related to ADAMTS9.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q9P2N4; product specifications from Assay Genie datasheets.