PROSITE documentation PDOC52079Forkhead box protein P (FoxP) family leucine zipper (ZIP) domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC52079
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.
Last update:October 2025 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Gao J. Geng R. Deng H. Zuo H. Weng S. He J. Xu X. |
| Title | A Novel Forkhead Box Protein P (FoxP) From Litopenaeus vannamei Plays a Positive Role in Immune Response. | |
| Source | Front. Immunol. 11:593987-593987(2020). | |
| PubMed ID | 33381114 | |
| DOI | 10.3389/fimmu.2020.593987 |
| 2 | Authors | 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. |
| Title | Structural and biological features of FOXP3 dimerization relevant to regulatory T cell function. | |
| Source | Cell. Rep. 1:665-675(2012). | |
| PubMed ID | 22813742 | |
| DOI | 10.1016/j.celrep.2012.04.012 |
| 3 | Authors | 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. |
| Title | The transcription factor FoxP3 can fold into two dimerization states with divergent implications for regulatory T cell function and immune homeostasis. | |
| Source | Immunity 55:1354-1369.e8(2022). | |
| PubMed ID | 35926508 | |
| DOI | 10.1016/j.immuni.2022.07.002 |
| 4 | Authors | Cruz P. Paredes N. Asela I. Kolimi N. Molina J.A. Ramirez-Sarmiento C.A. Goutam R. Huang G. Medina E. Sanabria H. |
| Title | Domain tethering impacts dimerization and DNA-mediated allostery in the human transcription factor FoxP1. | |
| Source | J. Chem. Phys. 158:0-0(2023). | |
| PubMed ID | 37184020 | |
| DOI | 10.1063/5.0138782 |
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