PS51042

CUT domain profile

PROSITE profiles entry
Member databasePROSITE profiles
PROSITE profiles typedomain
Short nameCUT

Description

The CUT domain, first discovered in the Drosophila Cut protein, consists of about 88 amino acids and is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. However, the homeodomain of this gene family has properties quite distinct from the classical homeodomain. On its own these homeodomain has little DNA-binding affinity or specificity. DNA-binding is mediated mostly by the CUT domain, but the sequence specificity and binding kinetics are greatly influenced by the presence of the homeodomain. The CUT proteins can be grouped into sub-families according to the presence of one, two, or three cut repeats. Congruent with their structural diversity, these cut-homeoproteins are transcriptional regulators that participate in a variety of functional contexts. Proteins currently known to contain a CUT domain are: - The Drosophila Cut protein and its mammalian homologs (CDP/Cux/Clox, and Cux2 proteins). They generally function as transcriptional repressors in both proliferating and differentiating cells. - The SATB1 protein which contains two cut repeats, is thought to function at the level of chromatin structure to modulate gene activity. - The mammalian HNF-6 (hepatocyte nuclear factor-6)
[1]
, which defines the prototypical Onecut proteins. It functions as a key regulator of liver gene expression. The profile we developed covers the entire CUT domain.

References

1.Isoforms of hepatocyte nuclear factor-6 differ in DNA-binding properties, contain a bifunctional homeodomain, and define the new ONECUT class of homeodomain proteins. Lannoy VJ, Burglin TR, Rousseau GG, Lemaigre FP. J. Biol. Chem. 273, 13552-62, (1998). View articlePMID: 9593691

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