PROSITE documentation PDOC51046
GON domain profile


The ADAMTSs (a disintegrin and metalloproteinase domain with thrombospondin type-1 modules) are a family of zinc dependent metalloproteinases that play important roles in a variety of normal and pathological conditions. These enzymes show a complex domain organization including signal sequence, propeptide, metalloproteinase domain (see <PDOC50215>), disintegrin-like domain (see <PDOC00351>), central TS-1 motif (see <PDOC50092>), cysteine-rich region, and a variable number of TS-like repeats at the C-terminal region. The GON domain is a ~200-residue module, whose presence is a hallmark of a subfamily of structurally and evolutionarily related ADAMTSs, called GON-ADAMTSs. The GON domain is characterized by the presence of several conserved cysteine residues and is likely to be globular [1,2].

Some proteins known to contain a GON domain are listed below:

  • Mammalian ADAMTS-9.
  • Mammalian ADAMTS-20.
  • Caenorhabditis elegans gon-1, a protease required for gonadal morphogenesis.

The profile we developed covers the entire GON domain.

Last update:

December 2004 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

GON, PS51046; GON domain profile  (MATRIX)


1AuthorsLlamazares M. Cal S. Quesada V. Lopez-Otin C.
TitleIdentification and characterization of ADAMTS-20 defines a novel subfamily of metalloproteinases-disintegrins with multiple thrombospondin-1 repeats and a unique GON domain.
SourceJ. Biol. Chem. 278:13382-13389(2003).
PubMed ID12562771

2AuthorsSomerville R.P.T. Longpre J.-M. Jungers K.A. Engle J.M. Ross M. Evanko S. Wight T.N. Leduc R. Apte S.S.
TitleCharacterization of ADAMTS-9 and ADAMTS-20 as a distinct ADAMTS subfamily related to Caenorhabditis elegans GON-1.
SourceJ. Biol. Chem. 278:9503-9513(2003).
PubMed ID12514189

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