RNA-binding protein involved in regulation of mRNA stability (PubMed:23592996). Binds AU-rich regions in the 3'-UTR of mRNAs and promotes their stabilization by recruiting a MKT1-containing complex (PubMed:23592996, PubMed:24470144). Stabilizes chaperone mRNAs during stress that causes an accumulation of misfolded or unfolded proteins in the cytoplasm (PubMed:23592996, PubMed:24470144, PubMed:27002830). Interacts (via MKT1-binding motif) with MKT1 (PubMed:23592996, PubMed:24470144). Interacts with PBP1 (via C-terminus); the interaction is direct (PubMed:23592996, PubMed:24470144). Expressed in the procyclic form and the bloodstream form at low levels. Induced during the response to misfolded or unfolded cytoplasmic proteins; including during thermal stress, sodium arsenite, or acidic pH (at protein level) (PubMed:23592996, PubMed:27002830). Not induced by endoplasmic reticulum stress (PubMed:27002830). The zinc finger domain binds AU-rich regions in the 3'-UTR of mRNAs. Phosphorylated at the N-terminus (PubMed:23592996, PubMed:27002830). CK1.2-dependent phosphorylation may lead to proteasome-dependent degradation of ZC3H11 in absence of stress (PubMed:27002830). RNAi-mediated knockdown in the bloodstream form is lethal and causes a reduction in chaperone mRNA levels in response to heat-induced stress (PubMed:23592996). RNAi-mediated knockdown in the procyclic form causes sensitivity to cytoplasmic protein folding stress (induced by high temperature, puromycin, arsenite, MG132 or ethanol), characterized by a reduction in chaperone mRNA levels (PubMed:23592996, PubMed:27002830).