InterPro : IPR001628

Name  Zinc finger, nuclear hormone receptor-type Short Name  Znf_hrmn_rcpt
Type  Domain Description  Steroid or nuclear hormone receptors constitute an important superfamily of transcription regulators that are involved in widely diverse physiological functions, including control of embryonic development, cell differentiation and homeostasis. The receptors function as dimeric molecules in nuclei to regulate the transcription of target genes in a ligand-responsive manner. Nuclear hormone receptors consist of a highly conserved DNA-binding domain that recognises specific sequences, connected via a linker region to a C-terminal ligand-binding domain (). In addition, certain nuclear hormone receptors have an N-terminal modulatory domain (). The DNA-binding domain can elicit either an activating or repressing effect by binding to specific regions of the DNA known as hormone-response elements [, ]. These response elements position the receptors, and the complexes recruited by them, close to the genes of which transcription is affected. The DNA-binding domains of nuclear receptors consist of two zinc-nucleated modules and a C-terminal extension, where residues in the first zinc module determine the specificity of the DNA recognition and residues in the second zinc module are involved in dimerisation. The DNA-binding domain is furthermore involved in several other functions including nuclear localisation, and interaction with transcription factors and co-activators [].Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis(African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents the two C4-type zinc finger modules involved in DNA-binding.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

12 Found In

Id Name Short Name Type
IPR016355 Steroidogenic factor 1 Steroidogenic_factor_1 Family
IPR001728 Thyroid hormone receptor ThyrH_rcpt Family
IPR003070 Orphan nuclear receptor Nuc_orph_rcpt Family
IPR016569 Methyltransferase, trithorax MeTrfase_trithorax Family
IPR003073 Orphan nuclear receptor, NURR type NURR_rcpt Family
IPR003075 Peroxisome proliferator-activated receptor, beta 1Cnucl_rcpt_B Family
IPR003076 Peroxisome proliferator-activated receptor, alpha 1Cnucl_rcpt_A Family
IPR003077 Peroxisome proliferator-activated receptor, gamma 1Cnucl_rcpt_G Family
IPR003078 Retinoic acid receptor Retinoic_acid_rcpt Family
IPR003069 Ecdysteroid receptor Ecdystd_rcpt Family
IPR003071 Orphan nuclear receptor, HMR type Nuc_orp_HMR_rcpt Family
IPR003072 Orphan nuclear receptor, NOR1 type NOR1_rcpt Family

1 Parent Features

Id Name Short Name Type
IPR013088 Zinc finger, NHR/GATA-type Znf_NHR/GATA Domain

8 Publications

First Author Title Year Journal Volume Pages
Matthews JM Zinc fingers--folds for many occasions. 2002 IUBMB Life 54 351-5
Gamsjaeger R Sticky fingers: zinc-fingers as protein-recognition motifs. 2007 Trends Biochem Sci 32 63-70
Hall TM Multiple modes of RNA recognition by zinc finger proteins. 2005 Curr Opin Struct Biol 15 367-73
Brown RS Zinc finger proteins: getting a grip on RNA. 2005 Curr Opin Struct Biol 15 94-8
Klug A Zinc finger peptides for the regulation of gene expression. 1999 J Mol Biol 293 215-8
Laity JH Zinc finger proteins: new insights into structural and functional diversity. 2001 Curr Opin Struct Biol 11 39-46
Moehren U Gene repression by nuclear hormone receptors. 2004 Essays Biochem 40 89-104
Claessens F DNA recognition by nuclear receptors. 2004 Essays Biochem 40 59-72

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)