Clusterin (Aging-associated gene 4 protein) (Apolipoprotein J) (Apo-J) (Complement cytolysis inhibitor) (CLI) (Complement-associated protein SP-40,40) (Ku70-binding protein 1) (NA1/NA2) (Sulfated glycoprotein 2) (SGP-2) (Testosterone-repressed prostate message 2) (TRPM-2) [Cleaved into: Clusterin beta chain (ApoJalpha) (Complement cytolysis inhibitor a chain); Clusterin alpha chain (ApoJbeta) (Complement cytolysis inhibitor b chain)]
1_MMKTL 6_ LLFVG 11_ LLLTW 16_ ESGQV 21_ LGDQT 26_ VSDNE 31_ LQEMS 36_ NQGSK 41_ YVNKE 46_ IQNAV 51_ NGVKQ 56_ IKTLI 61_ EKTNE 66_ ERKTL 71_ LSNLE 76_ EAKKK 81_ KEDAL 86_ NETRE 91_ SETKL 96_ KELPG 101_ VCNET 106_ MMALW 111_ EECKP 116_ CLKQT 121_ CMKFY 126_ ARVCR 131_ SGSGL 136_ VGRQL 141_ EEFLN 146_ QSSPF 151_ YFWMN 156_ GDRID 161_ SLLEN 166_ DRQQT 171_ HMLDV 176_ MQDHF 181_ SRASS 186_ IIDEL 191_ FQDRF 196_ FTREP 201_ QDTYH 206_ YLPFS 211_ LPHRR 216_ PHFFF 221_ PKSRI 226_ VRSLM 231_ PFSPY 236_ EPLNF 241_ HAMFQ 246_ PFLEM 251_ IHEAQ 256_ QAMDI 261_ HFHSP 266_ AFQHP 271_ PTEFI 276_ REGDD 281_ DRTVC 286_ REIRH 291_ NSTGC 296_ LRMKD 301_ QCDKC 306_ REILS 311_ VDCST 316_ NNPSQ 321_ AKLRR 326_ ELDES 331_ LQVAE 336_ RLTRK 341_ YNELL 346_ KSYQW 351_ KMLNT 356_ SSLLE 361_ QLNEQ 366_ FNWVS 371_ RLANL 376_ TQGED 381_ QYYLR 386_ VTTVA 391_ SHTSD 396_ SDVPS 401_ GVTEV 406_ VVKLF 411_ DSDPI 416_ TVTVP 421_ VEVSR 426_ KNPKF 431_ METVA 436_ EKALQ 441_EYRKK
1: Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17407782, PubMed:17412999). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement: inhibits assembly of the complement membrane attack complex (MAC) by preventing polymerization of C9 pore component of the MAC complex (PubMed:2780565, PubMed:1903064, PubMed:2601725, PubMed:2721499, PubMed:1551440, PubMed:9200695, PubMed:34667172). Intracellular forms 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 (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity)
2: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity
3: Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Promotes cell death through interaction with BCL2L1 that releases and activates BAX (PubMed:21567405)