{PDOC52079}
{PS52079; FOXP_ZIP}
{BEGIN}
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* Forkhead box protein P (FoxP) family leucine zipper (ZIP) domain profile *
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The Forkhead  box  (Fox)  protein  superfamily  consists  of  a large group of
transcriptional regulators  with  a  forkhead/winged-helix  DNA-binding domain
(see <PDOC00564>),   which   are   essentially  implicated  in  regulation  of
development, homeostasis and metabolism. In human, based on sequence homology,
Fox proteins  are  further categorized into 19 subfamilies (FoxA to FoxS). The
FoxP family  consists of four members, FoxP1 to FoxP4, the evolutionary origin
of which  can be traced back to sea lampreys and invertebrates. Mammalian FoxP
family members  generally function as transcriptional repressors or activators
involved in  tumor  suppression,  development  and,  in  particular, immunity.
Unlike their  homologues  in  mammals,  most  invertebrate FoxPs have not been
functionally studied  and  their roles in invertebrate immunity remain unclear
[1].

FoxP subfamily  members  contain  a  zinc  finger  (ZF) (see <PDOC00028>) that
likely binds  DNA,  and  a  Leucine  Zipper  (ZIP), known to form antiparallel
coiled-coil dimers  (see  <PDB:4I1L>),  in  addition  to their forkhead domain
[1,2,3,4]

The profile  we developed covers the entire FoxP ZIP domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: October 2025 / First entry.

[ 1] Gao J., Geng R., Deng H., Zuo H., Weng S., He J., Xu X.
     "A Novel Forkhead Box Protein P (FoxP) From Litopenaeus vannamei Plays
     a Positive  Role in Immune Response."
     Front. Immunol. 11:593987-593987(2020).
     PubMed=33381114; DOI=10.3389/fimmu.2020.593987
[ 2] Song X., Li B., Xiao Y., Chen C., Wang Q., Liu Y., Berezov A., Xu C.,
     Gao Y., Li Z., Wu S.L., Cai Z., Zhang H., Karger B.L., Hancock W.W.,
     Wells A.D., Zhou Z., Greene M.I.
     "Structural and biological features of FOXP3 dimerization relevant to
     regulatory T  cell function."
     Cell. Rep. 1:665-675(2012).
     PubMed=22813742; DOI=10.1016/j.celrep.2012.04.012
[ 3] Leng F., Zhang W., Ramirez R.N., Leon J., Zhong Y., Hou L., Yuki K.,
     van der Veeken J., Rudensky A.Y., Benoist C., Hur S.
     "The transcription factor FoxP3 can fold into two dimerization states
     with  divergent implications for regulatory T cell function and immune
     homeostasis."
     Immunity 55:1354-1369.e8(2022).
     PubMed=35926508; DOI=10.1016/j.immuni.2022.07.002
[ 4] Cruz P., Paredes N., Asela I., Kolimi N., Molina J.A.,
     Ramirez-Sarmiento C.A., Goutam R., Huang G., Medina E., Sanabria H.
     "Domain tethering impacts dimerization and DNA-mediated allostery in
     the human  transcription factor FoxP1."
     J. Chem. Phys. 158:0-0(2023).
     PubMed=37184020; DOI=10.1063/5.0138782

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