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Protein

Clusterin

Gene

CLU

Organism
Equus caballus (Horse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Clusterin
Cleaved into the following 2 chains:
Gene namesi
Name:CLU
OrganismiEquus caballus (Horse)
Taxonomic identifieri9796 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus
Proteomesi
  • UP000002281 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Nucleus, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 449428ClusterinPRO_0000005526Add
BLAST
Chaini22 – 227206Clusterin beta chainBy similarityPRO_0000005527Add
BLAST
Chaini228 – 449222Clusterin alpha chainBy similarityPRO_0000005528Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi85 – 851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi101 ↔ 313Interchain (between beta and alpha chains)By similarity
Glycosylationi102 – 1021N-linked (GlcNAc...)Sequence analysis
Disulfide bondi112 ↔ 305Interchain (between beta and alpha chains)By similarity
Disulfide bondi115 ↔ 302Interchain (between beta and alpha chains)By similarity
Disulfide bondi120 ↔ 295Interchain (between beta and alpha chains)By similarity
Disulfide bondi128 ↔ 285Interchain (between beta and alpha chains)By similarity
Modified residuei132 – 1321PhosphoserineBy similarity
Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence analysis
Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence analysis
Glycosylationi317 – 3171N-linked (GlcNAc...)Sequence analysis
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence analysis
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence analysis
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence analysis
Modified residuei396 – 3961PhosphoserineBy similarity

Post-translational modificationi

Heavily N-glycosylated. About 30% of the protein mass is comprised of complex N-linked carbohydrate (By similarity).By similarity
Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen.By similarity
Polyubiquitinated, leading to proteasomal degradation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ29482.
PeptideAtlasiQ29482.
PRIDEiQ29482.

Interactioni

Subunit structurei

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).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9796.ENSECAP00000005450.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi77 – 804Nuclear localization signalBy similarity
Motifi443 – 4475Nuclear localization signalBy similarity

Sequence similaritiesi

Belongs to the clusterin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHRB. Eukaryota.
ENOG410YYKB. LUCA.
GeneTreeiENSGT00530000063668.
HOGENOMiHOG000111799.
HOVERGENiHBG006908.
InParanoidiQ29482.
KOiK17252.
OMAiMKFYARV.
OrthoDBiEOG7K6PV4.
TreeFamiTF333030.

Family and domain databases

InterProiIPR016016. Clusterin.
IPR000753. Clusterin-like.
IPR016015. Clusterin_C.
IPR016014. Clusterin_N.
[Graphical view]
PfamiPF01093. Clusterin. 1 hit.
[Graphical view]
PIRSFiPIRSF002368. Clusterin. 1 hit.
SMARTiSM00035. CLa. 1 hit.
SM00030. CLb. 1 hit.
[Graphical view]
PROSITEiPS00492. CLUSTERIN_1. 1 hit.
PS00493. CLUSTERIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q29482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLLLLVGL LLTLENGQVL GDKAVSDREL QEMSTQGSNY INKEIKNALK
60 70 80 90 100
GVKQIKNLIE QTNEERKSLL GTLEEAKKKK EGALNDTKDS EMKLKESQGV
110 120 130 140 150
CNETMTALWE ECKPCLKQTC MKFYARVCRS GSGLVGHQLE EFLNQSSPFY
160 170 180 190 200
FWINGDRIDS LLENDRQQTH VLDVMQDSFD RASSIMDELF QDRFFTREPQ
210 220 230 240 250
DTYYYSPFSS PHRRSSLLFN PKSRFARNIM HFPMYRHLNF NDMFQPFFDM
260 270 280 290 300
IHQAQQAMNL HLHRLPDQLP MTEFSEGDNH DRTVCKEIRH NSTGCLKMKD
310 320 330 340 350
QCEKCQEILS VDCSTNNPSQ MQLRQELNNS LQLAEKFTKL YDELLQSYQE
360 370 380 390 400
KMLNTSSLLK QLNEQFSWVS QLANLTQGED QYYLQVTTVS SHNSDSEVPS
410 420 430 440
GLTRVVVKLF DSYPITVTVP EVVSRNNPKF METVAEKALQ EYRQKNREE
Length:449
Mass (Da):52,154
Last modified:November 1, 1996 - v1
Checksum:i705A60504515F7C0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46797 mRNA. Translation: AAA80313.1.
RefSeqiNP_001075413.1. NM_001081944.1.
UniGeneiEca.18000.

Genome annotation databases

EnsembliENSECAT00000007460; ENSECAP00000005450; ENSECAG00000007010.
GeneIDi100034172.
KEGGiecb:100034172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L46797 mRNA. Translation: AAA80313.1.
RefSeqiNP_001075413.1. NM_001081944.1.
UniGeneiEca.18000.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9796.ENSECAP00000005450.

Proteomic databases

PaxDbiQ29482.
PeptideAtlasiQ29482.
PRIDEiQ29482.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSECAT00000007460; ENSECAP00000005450; ENSECAG00000007010.
GeneIDi100034172.
KEGGiecb:100034172.

Organism-specific databases

CTDi1191.

Phylogenomic databases

eggNOGiENOG410IHRB. Eukaryota.
ENOG410YYKB. LUCA.
GeneTreeiENSGT00530000063668.
HOGENOMiHOG000111799.
HOVERGENiHBG006908.
InParanoidiQ29482.
KOiK17252.
OMAiMKFYARV.
OrthoDBiEOG7K6PV4.
TreeFamiTF333030.

Family and domain databases

InterProiIPR016016. Clusterin.
IPR000753. Clusterin-like.
IPR016015. Clusterin_C.
IPR016014. Clusterin_N.
[Graphical view]
PfamiPF01093. Clusterin. 1 hit.
[Graphical view]
PIRSFiPIRSF002368. Clusterin. 1 hit.
SMARTiSM00035. CLa. 1 hit.
SM00030. CLb. 1 hit.
[Graphical view]
PROSITEiPS00492. CLUSTERIN_1. 1 hit.
PS00493. CLUSTERIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Nucleotide sequence of the complementary DNA encoding equine clusterin."
    Barber J.A., Farris J.A., Troedsson M.H.T., Crabo B.G., Foster D.
    Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.

Entry informationi

Entry nameiCLUS_HORSE
AccessioniPrimary (citable) accession number: Q29482
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.