ID Q549A5_MOUSE Unreviewed; 448 AA. AC Q549A5; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=Clusterin {ECO:0000256|ARBA:ARBA00020334, ECO:0000256|PIRNR:PIRNR002368}; GN Name=Clu {ECO:0000313|MGI:MGI:88423}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAF06365.1}; RN [1] {ECO:0000313|EMBL:AAF06365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SvJ/129 {ECO:0000313|EMBL:AAF06365.1}; RA Zhu G., Ley-Ebert C., Barrie A.M. III, Witte D.P., Rosenberg M., RA Harmony J.A.K., Aronow B.J.; RT "Clusterin Gene Locus Structure and Function in Development, Homeostasis, RT and Tissue Injury."; RL (In) Landes R.G. (eds.); RL CLUSTERIN IN NORMAL BRAIN FUNCTIONS AND DURING NEURODEGENERATION., pp.1-16, RL Springer-Verlag, Austin, TX (1999). RN [2] {ECO:0000313|EMBL:AAF06365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SvJ/129 {ECO:0000313|EMBL:AAF06365.1}; RA Jordan-Starck T.C., Ley-Ebert C., Zhu G., Johnson J.A., Harmony J.A.K., RA Aronow B.J.; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AAF06365.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SvJ/129 {ECO:0000313|EMBL:AAF06365.1}; RX PubMed=11067863; DOI=10.1172/JCI9037; RA McLaughlin L., Zhu G., Mistry M., Ley-Ebert C., Stuart W.D., Florio C.J., RA Groen P.A., Witt S.A., Kimball T.R., Witte D.P., Harmony J.A., Aronow B.J.; RT "Apolipoprotein J/clusterin limits the severity of murine autoimmune RT myocarditis."; RL J. Clin. Invest. 106:1105-1113(2000). RN [4] {ECO:0000313|EMBL:AAF67184.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Balb/c {ECO:0000313|EMBL:AAF67184.1}; RC TISSUE=Uterus {ECO:0000313|EMBL:AAF67184.1}; RA You K.H., Jeon J.H.; RT "Identification of Truncated SGP-2 Lacking a Signal Peptide for RT Secretion."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Functions as extracellular chaperone that prevents CC aggregation of non native proteins. Prevents stress-induced aggregation CC of blood plasma proteins. {ECO:0000256|PIRNR:PIRNR002368}. CC -!- SUBUNIT: Antiparallel disulfide-linked heterodimer of an alpha chain CC and a beta chain. Self-associates and forms higher oligomers. CC {ECO:0000256|PIRNR:PIRNR002368}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000256|ARBA:ARBA00004514}. Cytoplasm, perinuclear region CC {ECO:0000256|ARBA:ARBA00004556}. Cytoplasmic vesicle, secretory CC vesicle, chromaffin granule {ECO:0000256|ARBA:ARBA00004248}. CC Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. Microsome CC {ECO:0000256|ARBA:ARBA00004144}. Mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004346}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004346}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004346}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. Secreted CC {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR002368}. CC -!- SIMILARITY: Belongs to the clusterin family. CC {ECO:0000256|ARBA:ARBA00010069, ECO:0000256|PIRNR:PIRNR002368, CC ECO:0000256|RuleBase:RU000629}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF182509; AAF06365.1; -; Genomic_DNA. DR EMBL; AF248057; AAF67184.1; -; mRNA. DR RefSeq; NP_038520.2; NM_013492.3. DR RefSeq; XP_006518567.1; XM_006518504.3. DR AlphaFoldDB; Q549A5; -. DR SMR; Q549A5; -. DR SwissPalm; Q549A5; -. DR MaxQB; Q549A5; -. DR PeptideAtlas; Q549A5; -. DR Antibodypedia; 631; 1388 antibodies from 52 providers. DR DNASU; 12759; -. DR GeneID; 12759; -. DR KEGG; mmu:12759; -. DR AGR; MGI:88423; -. DR CTD; 1191; -. DR MGI; MGI:88423; Clu. DR VEuPathDB; HostDB:ENSMUSG00000022037; -. DR HOGENOM; CLU_042162_2_0_1; -. DR OMA; QGSKYIN; -. DR OrthoDB; 4321242at2759; -. DR BioGRID-ORCS; 12759; 0 hits in 78 CRISPR screens. DR ChiTaRS; Clu; mouse. DR ExpressionAtlas; Q549A5; baseline and differential. DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl. DR GO; GO:0071944; C:cell periphery; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell. DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0097418; C:neurofibrillary tangle; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0099020; C:perinuclear endoplasmic reticulum lumen; IEA:Ensembl. DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl. DR GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl. DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl. DR GO; GO:0051787; F:misfolded protein binding; IEA:Ensembl. DR GO; GO:0140597; F:protein carrier chaperone; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0048156; F:tau protein binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0051082; F:unfolded protein binding; IEA:Ensembl. DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl. DR GO; GO:0032286; P:central nervous system myelin maintenance; IEA:Ensembl. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl. DR GO; GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl. DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl. DR GO; GO:0061518; P:microglial cell proliferation; IEA:Ensembl. DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IEA:Ensembl. DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; IEA:Ensembl. DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl. DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl. DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; IEA:Ensembl. DR GO; GO:1902998; P:positive regulation of neurofibrillary tangle assembly; IEA:Ensembl. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl. DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl. DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IEA:Ensembl. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl. DR GO; GO:0017038; P:protein import; IEA:Ensembl. DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl. DR GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IEA:Ensembl. DR GO; GO:1900221; P:regulation of amyloid-beta clearance; IEA:Ensembl. DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:1902847; P:regulation of neuronal signal transduction; IEA:Ensembl. DR GO; GO:0051788; P:response to misfolded protein; IEA:Ensembl. DR GO; GO:0009615; P:response to virus; IEA:Ensembl. DR InterPro; IPR016016; Clusterin. DR InterPro; IPR000753; Clusterin-like. DR InterPro; IPR016015; Clusterin_C. DR InterPro; IPR033986; Clusterin_CS. DR InterPro; IPR016014; Clusterin_N. DR PANTHER; PTHR10970; CLUSTERIN; 1. DR PANTHER; PTHR10970:SF1; CLUSTERIN; 1. DR Pfam; PF01093; Clusterin; 1. DR PIRSF; PIRSF002368; Clusterin; 1. DR SMART; SM00035; CLa; 1. DR SMART; SM00030; CLb; 1. DR PROSITE; PS00492; CLUSTERIN_1; 1. DR PROSITE; PS00493; CLUSTERIN_2; 1. PE 1: Evidence at protein level; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|PIRNR:PIRNR002368}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR002368}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR002368}; KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|PIRNR:PIRNR002368" FT CHAIN 22..448 FT /note="Clusterin" FT /evidence="ECO:0000256|PIRNR:PIRNR002368" FT /id="PRO_5014212507" FT DOMAIN 22..226 FT /note="Clusterin N-terminal" FT /evidence="ECO:0000259|SMART:SM00030" FT DOMAIN 227..442 FT /note="Clusterin C-terminal" FT /evidence="ECO:0000259|SMART:SM00035" FT COILED 59..93 FT /evidence="ECO:0000256|SAM:Coils" FT COILED 319..364 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 448 AA; 51656 MW; A860600A6F8D47F6 CRC64; MKILLLCVAL LLIWDNGMVL GEQEVSDNEL QELSTQGSRY INKEIQNAVQ GVKHIKTLIE KTNAERKSLL NSLEEAKKKK EDALEDTRDS EMKLKAFPEV CNETMMALWE ECKPCLKHTC MKFYARVCRS GSGLVGQQLE EFLNQSSPFY FWMNGDRIDS LLESDRQQSQ VLDAMQDSFA RASGIIDTLF QDRFFARELH DPHYFSPIGF PHKRPHFLYP KSRLVRSLMS PSHYGPPSFH NMFQPFFEMI HQAQQAMDVQ LHSPAFQFPD VDFLREGEDD RTVCKEIRRN STGCLKMKGQ CEKCQEILSV DCSTNNPAQA NLRQELNDSL QVAERLTEQY KELLQSFQSK MLNTSSLLEQ LNDQFNWVSQ LANLTQGEDK YYLRVSTVTT HSSDSEVPSR VTEVVVKLFD SDPITVVLPE EVSKDNPKFM DTVAEKALQE YRRKSRAE //