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Clusterin (Dimeric acid glycoprotein) (DAG) (Sulfated glycoprotein 2) (SGP-2) (Testosterone repressed prostate message 2) (TRPM-2) [Cleaved into: Clusterin beta chain; Clusterin alpha chain]

 CLUS_RAT                Reviewed;         447 AA.
P05371;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
20-JUN-2018, entry version 138.
RecName: Full=Clusterin;
AltName: Full=Dimeric acid glycoprotein;
Short=DAG;
AltName: Full=Sulfated glycoprotein 2;
Short=SGP-2;
AltName: Full=Testosterone repressed prostate message 2;
Short=TRPM-2;
Contains:
RecName: Full=Clusterin beta chain;
Contains:
RecName: Full=Clusterin alpha chain;
Flags: Precursor;
Name=Clu;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-45 AND 227-241,
PROTEOLYTIC PROCESSING, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=3651384; DOI=10.1021/bi00386a008;
Collard M.W., Griswold M.D.;
"Biosynthesis and molecular cloning of sulfated glycoprotein 2
secreted by rat Sertoli cells.";
Biochemistry 26:3297-3303(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Prostate;
PubMed=2920020; DOI=10.1042/bj2570293;
Bettuzzi S., Hiipakka R.A., Gilna P., Liao S.;
"Identification of an androgen-repressed mRNA in rat ventral prostate
as coding for sulphated glycoprotein 2 by cDNA cloning and sequence
analysis.";
Biochem. J. 257:293-296(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=Sprague-Dawley;
PubMed=7680346;
Wong P., Pineault J.M., Lakins J., Taillefer D., Leger J., Wang C.,
Tenniswood M.;
"Genomic organization and expression of the rat TRPM-2 (clusterin)
gene, a gene implicated in apoptosis.";
J. Biol. Chem. 268:5021-5031(1993).
[4]
PROTEIN SEQUENCE OF 22-51 AND 227-256, SUBCELLULAR LOCATION, SUBUNIT,
AND PROTEOLYTIC PROCESSING.
PubMed=3415696; DOI=10.1016/S0006-291X(88)81051-9;
Cheng C.Y., Chen C.C., Feng Z., Marshall A., Bardin C.W.;
"Rat clusterin isolated from primary Sertoli cell-enriched culture
medium is sulfated glycoprotein-2 (SGP-2).";
Biochem. Biophys. Res. Commun. 155:398-404(1988).
[5]
CHARACTERIZATION OF TRPM-2.
PubMed=2299741;
Bandyk M.G., Sawczuk I.S., Olsson C.A., Katz A.E., Buttyan R.;
"Characterization of the products of a gene expressed during androgen-
programmed cell death and their potential use as a marker of
urogenital injury.";
J. Urol. 143:407-413(1990).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: 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. When
secreted, protects cells against apoptosis and against cytolysis
by complement. 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. Promotes proteasomal degradation
of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional
activity. Promotes apoptosis when in the nucleus. Inhibits
apoptosis when associated with the mitochondrial membrane by
interference with BAX-dependent release of cytochrome c into the
cytoplasm. Plays a role in the regulation of cell proliferation
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Antiparallel disulfide-linked heterodimer of an alpha
chain and a beta chain. Self-associates and forms higher
oligomers. Interacts with a broad range of misfolded proteins,
including APP, APOC2 and LYZ. Slightly acidic pH promotes
interaction with misfolded proteins. Forms high-molecular weight
oligomers upon interaction with misfolded proteins. Interacts with
APOA1, LRP2, CLUAP1 AND PON1. Interacts with the complement
complex. Interacts with SYVN1, COMMD1, BTRC, CUL1 and with
ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein
ligase complexes. Interacts (via alpha chain) with BAX in stressed
cells, where BAX undergoes a conformation change leading to
association with the mitochondrial membrane. Does not interact
with BAX in unstressed cells. Interacts (via alpha chain) with
XRCC6 (By similarity). Found in a complex with LTF, CLU, EPPIN and
SEMG1 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3415696,
ECO:0000269|PubMed:3651384}. Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}. Mitochondrion membrane {ECO:0000250}; Peripheral
membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Cytoplasm, cytosol {ECO:0000250}. Microsome {ECO:0000250}.
Endoplasmic reticulum {ECO:0000250}. Cytoplasmic vesicle,
secretory vesicle, chromaffin granule {ECO:0000250}. Note=Can
retrotranslocate from the secretory compartments to the cytosol
upon cellular stress. Detected in perinuclear foci that may be
aggresomes containing misfolded, ubiquitinated proteins. Detected
at the mitochondrion membrane upon induction of apoptosis (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in Sertoli cells (at protein level).
Detected in cultured Sertoli cells, testis, epididymis, liver and
brain. {ECO:0000269|PubMed:3651384}.
-!- DEVELOPMENTAL STAGE: Expressed by cells undergoing programmed
death as a result of the hormonal stimuli or a traumatic insult.
-!- PTM: Extensively glycosylated with sulfated N-linked
carbohydrates. {ECO:0000269|PubMed:3651384}.
-!- PTM: Proteolytically cleaved on its way through the secretory
system, probably within the Golgi lumen. {ECO:0000250}.
-!- PTM: Polyubiquitinated, leading to proteasomal degradation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the clusterin family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M16975; AAA41273.1; -; mRNA.
EMBL; X13231; CAA31618.1; -; mRNA.
EMBL; M64723; AAA42298.1; -; mRNA.
EMBL; M64733; AAA42299.1; -; Genomic_DNA.
PIR; A45890; A27205.
RefSeq; NP_444180.2; NM_053021.2.
UniGene; Rn.1780; -.
DisProt; DP00014; -.
SMR; P05371; -.
IntAct; P05371; 1.
MINT; P05371; -.
STRING; 10116.ENSRNOP00000022095; -.
CarbonylDB; P05371; -.
iPTMnet; P05371; -.
PhosphoSitePlus; P05371; -.
PaxDb; P05371; -.
PRIDE; P05371; -.
GeneID; 24854; -.
KEGG; rno:24854; -.
UCSC; RGD:3907; rat.
CTD; 1191; -.
RGD; 3907; Clu.
eggNOG; ENOG410IHRB; Eukaryota.
eggNOG; ENOG410YYKB; LUCA.
HOGENOM; HOG000111799; -.
HOVERGEN; HBG006908; -.
InParanoid; P05371; -.
KO; K17252; -.
PhylomeDB; P05371; -.
PRO; PR:P05371; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016235; C:aggresome; IDA:RGD.
GO; GO:0097440; C:apical dendrite; ISS:Alzheimers_University_of_Toronto.
GO; GO:0042583; C:chromaffin granule; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:CAFA.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0097418; C:neurofibrillary tangle; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0034366; C:spherical high-density lipoprotein particle; ISS:UniProtKB.
GO; GO:0051787; F:misfolded protein binding; ISS:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0000902; P:cell morphogenesis; ISS:Alzheimers_University_of_Toronto.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
GO; GO:0032286; P:central nervous system myelin maintenance; ISS:Alzheimers_University_of_Toronto.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISS:Alzheimers_University_of_Toronto.
GO; GO:0061077; P:chaperone-mediated protein folding; ISS:UniProtKB.
GO; GO:0031018; P:endocrine pancreas development; IMP:RGD.
GO; GO:0044849; P:estrous cycle; IEP:RGD.
GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:0001774; P:microglial cell activation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0061518; P:microglial cell proliferation; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISS:BHF-UCL.
GO; GO:0032463; P:negative regulation of protein homooligomerization; ISS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:RGD.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISS:Alzheimers_University_of_Toronto.
GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISS:UniProtKB.
GO; GO:1902998; P:positive regulation of neurofibrillary tangle assembly; ISS:Alzheimers_University_of_Toronto.
GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:Alzheimers_University_of_Toronto.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:1902949; P:positive regulation of tau-protein kinase activity; ISS:Alzheimers_University_of_Toronto.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:Alzheimers_University_of_Toronto.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0017038; P:protein import; ISS:Alzheimers_University_of_Toronto.
GO; GO:0050821; P:protein stabilization; IDA:CAFA.
GO; GO:1900221; P:regulation of amyloid-beta clearance; ISS:Alzheimers_University_of_Toronto.
GO; GO:1901214; P:regulation of neuron death; ISS:Alzheimers_University_of_Toronto.
GO; GO:1902847; P:regulation of neuronal signal transduction; ISS:Alzheimers_University_of_Toronto.
GO; GO:0009416; P:response to light stimulus; IEP:RGD.
GO; GO:0051788; P:response to misfolded protein; ISS:UniProtKB.
GO; GO:0035864; P:response to potassium ion; IEP:RGD.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
InterPro; IPR016016; Clusterin.
InterPro; IPR000753; Clusterin-like.
InterPro; IPR016015; Clusterin_C.
InterPro; IPR033986; Clusterin_CS.
InterPro; IPR016014; Clusterin_N.
PANTHER; PTHR10970; PTHR10970; 1.
PANTHER; PTHR10970:SF1; PTHR10970:SF1; 1.
Pfam; PF01093; Clusterin; 1.
PIRSF; PIRSF002368; Clusterin; 1.
SMART; SM00035; CLa; 1.
SMART; SM00030; CLb; 1.
PROSITE; PS00492; CLUSTERIN_1; 1.
PROSITE; PS00493; CLUSTERIN_2; 1.
1: Evidence at protein level;
Chaperone; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Developmental protein; Differentiation; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
Microsome; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
Secreted; Signal; Spermatogenesis; Ubl conjugation.
SIGNAL 1 21 {ECO:0000269|PubMed:3415696,
ECO:0000269|PubMed:3651384}.
CHAIN 22 447 Clusterin.
/FTId=PRO_0000005544.
CHAIN 22 226 Clusterin beta chain.
/FTId=PRO_0000005545.
CHAIN 227 447 Clusterin alpha chain.
/FTId=PRO_0000005546.
MOTIF 77 80 Nuclear localization signal.
{ECO:0000250}.
MOTIF 441 445 Nuclear localization signal.
{ECO:0000250}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:P10909}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:P10909}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 353 353 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
CARBOHYD 373 373 N-linked (GlcNAc...) asparagine.
{ECO:0000305|PubMed:3651384}.
DISULFID 101 312 Interchain (between beta and alpha
chains). {ECO:0000250}.
DISULFID 112 304 Interchain (between beta and alpha
chains). {ECO:0000250}.
DISULFID 115 301 Interchain (between beta and alpha
chains). {ECO:0000250}.
DISULFID 120 294 Interchain (between beta and alpha
chains). {ECO:0000250}.
DISULFID 128 284 Interchain (between beta and alpha
chains). {ECO:0000250}.
CONFLICT 187 187 D -> H (in Ref. 1; AAA41273).
{ECO:0000305}.
SEQUENCE 447 AA; 51375 MW; 9E2FA33E5E0C146E CRC64;
MKILLLCVAL LLTWDNGMVL GEQEFSDNEL QELSTQGSRY VNKEIQNAVQ GVKHIKTLIE
KTNAERKSLL NSLEEAKKKK EGALDDTRDS EMKLKAFPEV CNETMMALWE ECKPCLKHTC
MKFYARVCRS GSGLVGRQLE EFLNQSSPFY FWMNGDRIDS LLESDRQQSQ VLDAMQDSFT
RASGIIDTLF QDRFFTHEPQ DIHHFSPMGF PHKRPHFLYP KSRLVRSLMP LSHYGPLSFH
NMFQPFFDMI HQAQQAMDVQ LHSPALQFPD VDFLKEGEDD PTVCKEIRHN STGCLKMKGQ
CEKCQEILSV DCSTNNPAQA NLRQELNDSL QVAERLTQQY NELLHSLQSK MLNTSSLLEQ
LNDQFTWVSQ LANLTQGDDQ YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE
VSKDNPKFMD TVAEKALQEY RRKSRME


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