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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.

November 2003 / Profile revised.

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

DOMON, PS50836; DOMON domain profile  (MATRIX)

Sequences known to belong to this class detected by the profile: ALL Other sequence(s) detected in Swiss-Prot: NONE

• Domain architecture view of Swiss-Prot proteins matching PS50836 • Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS50836 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50836 • Scan Swiss-Prot/TrEMBL entries against PS50836 • view ligand binding statistics

1	Authors	Aravind L.
	Title	DOMON: an ancient extracellular domain in dopamine beta-monooxygenase and other proteins.
	Source	Trends Biochem. Sci. 26:524-526(2001).
	PubMed ID	11551777

2	Authors	Ponting C.P.
	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).
	PubMed ID	11532994

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