PROSITE documentation PDOC51042

CUT domain profile

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 (see <PDOC00027>). 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) [2], 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.