DoHPossible catecholamine-binding domain present in a variety of eukaryotic proteins.
|SMART accession number:||SM00664|
|Description:||A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press).|
|Interpro abstract (IPR005018):|
The DOMON domain is an 110-125 residue long domain which has been identified in the physiologically important enzyme dopamine beta-monooxygenase and in several other secreted and transmembrane proteins from both plants and animals. It has been named after DOpamine beta-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, the trypsin inhibitor-like domain (TIL), the SEA domain and the Reelin domain. The architectures of the DOMON domain proteins strongly suggest a function in extracellular adhesion [(PUBMED:11551777)].
The sequence conservation is predominantly centred around patches of hydrophobic residues. The secondary structure prediction of the DOMON domain points to an all-beta-strand fold with seven or eight core strands supported by a buried core of conserved hydrophobic residues. There is a chraracteristic 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 beta-sandwich structure, with the strands distributed into two beta sheets as is seen in many extracellular adhesion domains such as the immunoglobulin, fibronectin type III, cadherin and PKD domains [(PUBMED:11551777)].
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