The human ADAMTS9 gene is composed of 40 exons spanning a genomic region of about 172 kbp. The open reading frame of the coding region is 5808 bp.

No pseudogene reported.

ADAMTS9 is composed of a signal peptide, a propeptide, a metalloproteinase domain, a disintegrin-like domain, thrombospondin type 1-like repeats, a cystein-rich domain, a spacer domain, and a unique C-terminal domain (Somerville et al., 2003). A unique C-terminal domain was named as GON domain. The GON domain functions in the ER for protein transport from the ER to the Golgi (Yoshina et al., 2012). N-linked glycosylation of ADAMTS9 propeptide is found to be essential for ADAMTS9 secretion (Koo et al., 2007). ADAMTS9 is processed by furin extracellularly but not in the secretory pathway (Koo et al., 2006). Following furin processing, mature ADAMTS9 is released from the cell surface (Koo et al., 2007).
ADAMTS9 is required for early mouse development. ADAMTS9 null mice die before gastrulation. ADAMTS9+/- mice develop anomalous eye such as corneal clouding, corneal neovascularisation, and adhesions of the lens and iris to the cornea (Koo et al., 2010).

ADAMTS9 is found in adult human ovary, pancreas, heart, kidney, lung, placenta, and skeletal muscle. ADAMTS9 is found in fetal brain, heart, kidney, lung, liver, skeletal muscle, spleen and thymus. According to northern blot analysis, the highest mRNA levels are found in heart, placenta, and skeletal muscle (Clark et al., 2000; Somerville et al., 2003). ADAMTS9 is expressed in microvascular endothelial cells (Koo et al., 2010).
Following stimulation with TNFalpha, ADAMTS9 mRNA expression was enhanced in a human retinal pigment epithelial cell line (ARPE-19) (Bevitt et al., 2003). In a human chondrosarcoma cell line (OUMS-27) and human chondrocytes, exposure to IL-1 beta or TNF alpha upregulate ADAMTS9 mRNA expression (Demircan et al., 2005). Induction of ADAMTS9 mRNA by IL-1beta was reported to occur via NFATc binding to the ADAMTS9 promoter in the OUMS-27 and in human chondrocyte (Yaykasli et al., 2009). In the human lung carcinoma epithelial cell line (A549), exposure to TGF- beta or IL-13 or Epstein-Barr virus infection led to enhanced ADAMTS9 mRNA expression. IL-4 exposure had no effect on the expression of ADAMTS9 in A549 (Keating et al., 2006).

ADAMTS9 is present at the plasma membrane and the endoplasmic reticulum (Somerville et al., 2003; Yoshina et al., 2012).

ADAMTS9 cleaves aggrecan and versican (Somerville et al., 2003). ADAMTS9 is involved in cell migration and inhibition of angiogenesis (Koo et al., 2010).
ADAMTS9 is implicated in the transport from the endoplasmic reticulum to the Golgi. This function is GON-domain dependent but protease activity independent (Yoshina et al., 2012).

ADAMTS9 and ADAMTS20 have the identical domain organization and exon structure and a similar primaly sequence. The unique C-terminal domain, GON domain, is highly similar in ADAMTS9 and ADAMTS20 (Somerville et al., 2003).

A downregulation of ADAMTS9 has been observed in some carcinoma that is induced by aberrant methylation of the gene.
The major C-risk allele of rs4607103 near ADAMTS9, conferring increased risk of type 2 diabetes.