ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases - General features and genomic distribution of the ADAM-TS family

We report the primary structure of three novel, putative zinc metalloprotea ses designated ADAM-TS5, ADAM-TS6, and ADAM-TS7. All have a similar domain organization, comprising a preproregion, a reprolysin-type catalytic domain , a disintegrin-like domain, a thrornbospondin type-1 (TS) module, a cystei ne-rich domain, a spacer domain without cysteine residues, and a COOH-termi nal TS module. These genes are differentially regulated during mouse embryo genesis and in adult; tissues, with Adamts5 highly expressed in the periimp lantation period in embryo and trophoblast. These proteins are similar to f our other cognate gene products, defining a distinct family of human reprol ysin-like metalloproteases, the ADAM-TS family. The other members of the fa mily are ADAM-TS1, an inflammation-induced gene, the procollagen I/II amino -propeptide processing enzyme (PCINP, ADAM-TS2), and proteins predicted by the KIAA0366 and KIAA0688 genes (ADAM-TS3 and ADAM-TS4). Individual ADAM-TS members differ in the number of COOH-terminal TS modules, and some have un ique COOH-terminal domains. The ADAM-TS genes are dispersed in human and mo use genomes.