Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation.
APOJ; CLI; Clusterin; Clustrin; DAG; 40; Aging-associated gene 4 protein; aging-associated protein 4; APO-J; Apolipoprotein J; Complement cytolysis inhibitor; complement lysis inhibitor; complement-associated protein SP-40; Complement-associated protein SP-40,40; Dimeric acid glycoprotein; Ku70-binding protein 1; KUB1; NA1/NA2; SGP-2; SGP2; SP-40; Sulfated glycoprotein 2; testosterone repressed prostate message; Testosterone repressed prostate message 2; testosterone repressed prostate message-2; testosterone-repressed prostate message; Testosterone-repressed prostate message 2; testostrone-repressed prostate message 2; TRPM-2; TRPM2
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