PROSITE documentation PDOC50836
DOMON domain profile


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 [1].

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

  • Mammalian dopamine β-monooxygenase (DM). It is involved in the conversion of dopamine to the catecholamine noradrenaline, a crucial physiological modulator of the sympathetic nervous system, T-cell-mediated immunity and fetal development.
  • Drosophila tyramine-β-hydroxylase (TBH), an orthologue of DM. It is needed for the biosynthesis of the neurotransmitter octopamine from tyramine.
  • Human brain protein C9orf4.
  • Mouse SDR2 protein.
  • Botryllus schlosseri PAR protein, a soluble immunoglobulin molecule homologue.
  • Caenorhabditis elegans uncharacterized protein C09F9.2.
  • Arabidopsis thaliana uncharacterized protein At5g54830.

The profile we developed covers the entire DOMON domain.

Last update:

November 2003 / Profile revised.


Technical section

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

DOMON, PS50836; DOMON domain profile  (MATRIX)


1AuthorsAravind L.
TitleDOMON: an ancient extracellular domain in dopamine beta-monooxygenase and other proteins.
SourceTrends Biochem. Sci. 26:524-526(2001).
PubMed ID11551777

2AuthorsPonting C.P.
TitleDomain homologues of dopamine beta-hydroxylase and ferric reductase: roles for iron metabolism in neurodegenerative disorders?
SourceHum. Mol. Genet. 10:1853-1858(2001).
PubMed ID11532994

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