{PDOC50950}
{PS50950; ZF_THAP}
{BEGIN}
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* Zinc finger THAP-type profile *
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The  THAP-type  zinc  finger  (consensus:  C-x(2,4)-C-x(35,50)-C-x(2)-H) is an
~90-residue  domain  restricted  to  animals, which is shared between the THAP
family  of cellular DNA-binding proteins, and transposases from mobile genomic
parasites   [1,2].   THAP1,  the  prototype  of  the  THAP  family,  possesses
zinc-dependent   sequence-specific  DNA  binding  activity  and  recognizes  a
consensus DNA target sequence of 11 nucleotides [3]. The THAP-type zinc finger
can  be  found in one or more copies and can be associated with other domains,
such as the C2H2-type zinc finger (see <PDOC00028>).

The  structure  of  the  THAP-type  zinc  finger  (see <PDB:2JTG>) reveals the
presence  between  the C2CH zinc coordinating residues of a short antiparallel
beta-sheet   interspersed   by   a   long   loop-helix-loop   insertion.  This
loop-helix-loop motif has been shown to be essential for the identification of
a number of critical residues for DNA recognition [4].

Some proteins known to contain a THAP-type zinc finger are listed below:

 - Mammalian  Thanatos-associated protein-1 (THAP1). It potentiates both serum
   withdrawal- and   tumor   necrosis   factor  alpha-induced  apoptosis,  and
   interacts with  prostate-apoptosis-response  4 (Par4), a well-characterized
   proapoptotic factor.
 - Mammalian  death-associated  protein  DAP4/p52rIPK  or  THAP0.  It has been
   identified in  a  genetic  screen  for  genes involved in interferon-gamma-
   induced apoptosis  in  HeLa  cells  and in a two-hybrid screen for indirect
   activators of  the  interferon-induced kinase PKR, an important mediator of
   stress-induced apoptosis.
 - Mammalian THAP2 to THAP11.
 - Drosophila melanogaster dorsal interacting protein 2 (DIP2).
 - Drosophila melanogaster P element transposase.

The  profile  we  developed  covers  the  whole  THAP-type  zinc finger with 4
positions upstream, and about 20 positions downstream.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2008 / Text revised.

[ 1] Roussigne M., Kossida S., Lavigne A.-C., Clouaire T., Ecochard V.,
     Glories A., Amalric F., Girard J.-P.
     "The THAP domain: a novel protein motif with similarity to the
     DNA-binding domain of P element transposase."
     Trends Biochem. Sci. 28:66-69(2003).
     PubMed=12575992
[ 2] Roussigne M., Cayrol C., Clouaire T., Amalric F., Girard J.-P.
     "THAP1 is a nuclear proapoptotic factor that links
     prostate-apoptosis-response-4 (Par-4) to PML nuclear bodies."
     Oncogene 22:2432-2442(2003).
     PubMed=12717420; DOI=10.1038/sj.onc.1206271
[ 3] Clouaire T., Roussigne M., Ecochard V., Mathe C., Amalric F.,
     Girard J.P.
     "The THAP domain of THAP1 is a large C2CH module with zinc-dependent
     sequence-specific DNA-binding activity."
     Proc. Natl. Acad. Sci. U.S.A. 102:6907-6912(2005).
     PubMed=15863623; DOI=10.1073/pnas.0406882102
[ 4] Bessiere D., Lacroix C., Campagne S., Ecochard V., Guillet V.,
     Mourey L., Lopez F., Czaplicki J., Demange P., Milon A., Girard J.P.,
     Gervais V.
     "Structure-function analysis of the THAP zinc finger of THAP1, a large
     C2CH DNA-binding module linked to Rb/E2F pathways."
     J. Biol. Chem. 283:4352-4363(2008).
     PubMed=18073205; DOI=10.1074/jbc.M707537200

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