Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity. Homodimer; disulfide-linked. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with AIMP1; regulates its retention in the endoplasmic reticulum. Interacts with OS9. Interacts with CNPY3. This interaction is disrupted in the presence of ATP. Interacts with TLR4 and TLR9, but not with TLR3. Belongs to the heat shock protein 90 family. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; Heat shock protein; Secreted; Secreted, signal peptide
Molecular Function: calcium ion binding; low-density lipoprotein receptor binding; protein binding; protein phosphatase binding; RNA binding; virion binding
Biological Process: actin rod formation; ER-associated protein catabolic process; negative regulation of apoptosis; receptor-mediated endocytosis; regulation of phosphoprotein phosphatase activity; response to hypoxia; retrograde protein transport, ER to cytosol; toll-like receptor signaling pathway