Description

IPR004457 is a Zinc finger, ZPR1-type.

<p>This entry represents ZPR1-type zinc finger domains. ZPR1 is an experimentally proven zinc-binding protein that binds the tyrosine kinase domain of the epidermal growth factor receptor (EGFR); binding is inhibited by EGF stimulation and tyrosine phosphorylation, and activation by EGF is followed by some redistribution of ZPR1 to the nucleus.</p> <p>The function of ZPR1 from archaea and eukaryotes is not yet clear. However, Zpr1 from yeast acts as a protein folding chaperone for elongation factor 1-alpha [[cite:PUB00103908]]. ZPR1 is present in both the cytoplasm and nucleoplasm and its subcellular distribution changes during proliferation [[cite:PUB00035839]]. ZPR1 binds to the cytoplasmic tyrosine kinase domain of the epidermal growth factor receptor (EGFR) [[cite:PUB00017397]] and is a component of downstream signaling of both EGFR and FGFR signaling [[cite:PUB00090578]]. It has been associated with susceptibility to type 2 diabetes [[cite:PUB00090579]] and is downregulated in patients with spinal muscular atrophy [[cite:PUB00090579]], a disease characterised by degeneration of the alpha-motor neurons in the spinal cord that can arise from mutations affecting the expression of Survival Motor Neurons (SMN) [[cite:PUB00035838]]. ZPR1 interacts with complexes formed by SMN [[cite:PUB00035839]], and may act as a modifier that affects the severity of SMA.</p> <p>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 [[cite:PUB00035807], [cite:PUB00035805], [cite:PUB00035806], [cite:PUB00035804], [cite:PUB00014077]]. 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 [[cite:PUB00035812]]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 16

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space: