|PROSITE documentation PDOC50836|
The DOMON domain is an 110-125 residue long domain which has been identified in the physiologically important enzyme dopamine β-monooxygenase and in several other secreted and transmembrane proteins from both plants and animals. It has been named after DOpamine β-MOnooxygenase N-terminal domain. The DOMON domain can be found in one to four copies and in association with other domains, such as the Cu-ascorbate dependent monooxygenase domain, the epidermal growth factor domain (see <PDOC00021>), the trypsin inhibitor-like domain (TIL), the SEA domain (see <PDOC50024>), and the Reelin domain. The architectures of the DOMON domain proteins strongly suggest a function in extracellular adhesion [1,2].
The sequence conservation is predominantly centered around patches of hydrophobic residues. The secondary structure prediction of the DOMON domain points to an all-β-strand fold with seven or eight core strands supported by a buried core of conserved hydrophobic residues. There is a characteristic motif with two small positions (Gly or Ser) corresponding to a conserved turn immediately C-terminal to strand three. It has been proposed that the DOMON domain might form a β-sandwich structure, with the strands distributed into two β sheets as is seen in many extracellular adhesion domains such as the immunoglobulin, fibronectin type-III, cadherin and PKD (see <PDOC50093>) domains .
Some proteins known to contain a DOMON domain are listed below:
The profile we developed covers the entire DOMON domain.
November 2003 / Profile revised.
PROSITE method (with tools and information) covered by this documentation:
|DOMON, PS50836; DOMON domain profile (MATRIX)|
|Title||DOMON: an ancient extracellular domain in dopamine beta-monooxygenase and other proteins.|
|Source||Trends Biochem. Sci. 26:524-526(2001).|
|Title||Domain homologues of dopamine beta-hydroxylase and ferric reductase: roles for iron metabolism in neurodegenerative disorders?|
|Source||Hum. Mol. Genet. 10:1853-1858(2001).|