Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1.

@article{Somerville2003CharacterizationOA,
  title={Characterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1.},
  author={Robert P T Somerville and Jean-Michel Longpr{\'e} and Katherine A Jungers and Jeffrey M Engle and Monique Ross and Stephen P. Evanko and Thomas N Wight and Richard Leduc and Suneel S. Apte},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 11},
  pages={9503-13}
}
We demonstrate that in humans, two metalloproteases, ADAMTS-9 (1935 amino acids) and ADAMTS-20 (1911 amino acids) are orthologs of GON-1, an ADAMTS protease required for gonadal morphogenesis in Caenorhabditis elegans. ADAMTS-9 and ADAMTS-20 have an identical modular structure, are distinct in possessing 15 TSRs and a unique C-terminal domain, and have a similar gene structure, suggesting that they comprise a new subfamily of human ADAMTS proteases. ADAMTS20 is very sparingly expressed… CONTINUE READING

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