Taxonomic distribution of proteins containing Zpr1 domains

The Zpr1 domain within your query sequence starts at position 257 and ends at position 387, and its E-value is 1.56e-65.

The cytoplasmic zinc finger protein ZPR1 accumulates in the nucleolus ofproliferating cells.

Galcheva-Gargova Z, Gangwani L, Konstantinov KN, Mikrut M, Theroux SJ, Enoch T, Davis RJ
Mol Biol Cell. 1998; 9: 2963-71

The zinc finger protein ZPR1 translocates from the cytoplasm to thenucleus after treatment of cells with mitogens. The function of nuclearZPR1 has not been defined. Here we demonstrate that ZPR1 accumulates inthe nucleolus of proliferating cells. The role of ZPR1 was examined usinga gene disruption strategy. Cells lacking ZPR1 are not viable. Biochemicalanalysis demonstrated that the loss of ZPR1 caused disruption of nucleolarfunction, including preribosomal RNA expression. These data establish ZPR1as an essential protein that is required for normal nucleolar function inproliferating cells.

Interaction of ZPR1 with translation elongation factor-1alpha inproliferating cells.

Gangwani L, Mikrut M, Galcheva-Gargova Z, Davis RJ
J Cell Biol. 1998; 143: 1471-84

The zinc finger protein ZPR1 is present in the cytoplasm of quiescentmammalian cells and translocates to the nucleus upon treatment withmitogens, including epidermal growth factor (EGF). Homologues of ZPR1 wereidentified in yeast and mammals. These ZPR1 proteins bind to eukaryotictranslation elongation factor-1alpha (eEF-1alpha). Studies of mammaliancells demonstrated that EGF treatment induces the interaction of ZPR1 witheEF-1alpha and the redistribution of both proteins to the nucleus. In theyeast Saccharomyces cerevisiae, genetic analysis demonstrated that ZPR1 isan essential gene. Deletion analysis demonstrated that the NH2-terminalregion of ZPR1 is required for normal growth and that the COOH-terminalregion was essential for viability in S. cerevisiae. The yeast ZPR1protein redistributes from the cytoplasm to the nucleus in response tonutrient stimulation. Disruption of the binding of ZPR1 to eEF-1alpha bymutational analysis resulted in an accumulation of cells in the G2/M phaseof cell cycle and defective growth. Reconstitution of the ZPR1 interactionwith eEF-1alpha restored normal growth. We conclude that ZPR1 is essentialfor cell viability and that its interaction with eEF-1alpha contributes tonormal cellular proliferation.

Binding of zinc finger protein ZPR1 to the epidermal growth factorreceptor.

Galcheva-Gargova Z, Konstantinov KN, Wu IH, Klier FG, Barrett T, Davis RJ
Science. 1996; 272: 1797-802

ZPR1 is a zinc finger protein that binds to the cytoplasmic tyrosinekinase domain of the epidermal growth factor receptor (EGFR). Deletionanalysis demonstrated that this binding interaction is mediated by thezinc fingers of ZPR1 and subdomains X and XI of the EGFR tyrosine kinase.Treatment of mammalian cells with EGF caused decreased binding of ZPR1 tothe EGFR and the accumulation of ZPR1 in the nucleus. The effect of EGF toregulate ZPR1 binding is dependent on tyrosine phosphorylation of theEGFR. ZPR1 therefore represents a prototype for a class of molecule thatbinds to the EGFR and is released from the receptor after activation.

Growth factor-induced tyrosine phosphorylation of Hrs, a novel 115-kilodalton protein with a structurally conserved putative zinc finger domain.

Komada M, Kitamura N
Mol Cell Biol. 1995; 15: 6213-21

The activation of growth factor receptor tyrosine kinases leads to tyrosine phosphorylation of many intracellular proteins which are thought to play crucial roles in growth factor signaling pathways. We previously showed that tyrosine phosphorylation of a 115-kDa protein is rapidly induced in cells treated with hepatocyte growth factor. To clarify the structure and possible function of the 115-kDa protein (designated Hrs for hepatocyte growth factor-regulated tyrosine kinase substrate), we purified this protein from B16-F1 mouse melanoma cells by anti-phosphotyrosine immunoaffinity chromatography and determined its partial amino acid sequences. On the basis of the amino acid sequences, we molecularly cloned the cDNA for mouse Hrs. The nucleotide sequence of the cDNA revealed that Hrs is a novel 775-amino-acid protein with a putative zinc finger domain that is structurally conserved in several other proteins. This protein also contained a proline-rich region and a proline- and glutamine-rich region. The expression of Hrs mRNA was detected in all adult mouse tissues tested and also in embryos. To analyze the Hrs cDNA product, we prepared a polyclonal antibody against bacterially expressed Hrs. Using this antibody, we showed by subcellular fractionation that Hrs is localized to the cytoplasm; we also showed that that tyrosine phosphorylation of Hrs is induced in cells treated with epidermal growth factor or platelet-derived growth factor. These results suggest that Hrs plays a unique and important role in the signaling pathway of growth factors.