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P08226 (APOE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apolipoprotein E

Short name=Apo-E
Gene names
Name:Apoe
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length311 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.

Subcellular location

Secreted.

Tissue specificity

Secreted in plasma.

Post-translational modification

Phosphorylation sites are present in the extracellular medium By similarity.

Sequence similarities

Belongs to the apolipoprotein A1/A4/E family.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentChylomicron
HDL
Secreted
VLDL
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMOxidation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

artery morphogenesis

Inferred from genetic interaction PubMed 16230502. Source: MGI

cGMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

cardiovascular system development

Inferred from mutant phenotype PubMed 19816508. Source: MGI

cellular calcium ion homeostasis

Inferred from direct assay PubMed 8185566. Source: MGI

cellular response to cholesterol

Inferred from electronic annotation. Source: Ensembl

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cholesterol catabolic process

Inferred from mutant phenotype PubMed 9826706. Source: MGI

cholesterol efflux

Inferred from direct assay PubMed 15269218. Source: MGI

cholesterol homeostasis

Inferred from mutant phenotype PubMed 1423598PubMed 7798939. Source: MGI

cholesterol metabolic process

Inferred from mutant phenotype PubMed 1423598PubMed 8647961. Source: MGI

chylomicron remnant clearance

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle assembly

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

lipid homeostasis

Inferred from mutant phenotype PubMed 17720994. Source: MGI

lipid metabolic process

Inferred from genetic interaction PubMed 11120757. Source: MGI

lipoprotein biosynthetic process

Inferred from genetic interaction PubMed 14595002. Source: MGI

lipoprotein catabolic process

Inferred from mutant phenotype PubMed 17720994. Source: MGI

lipoprotein metabolic process

Inferred from mutant phenotype PubMed 9788969. Source: MGI

low-density lipoprotein particle remodeling

Inferred from mutant phenotype PubMed 15654758. Source: BHF-UCL

maintenance of location in cell

Inferred from mutant phenotype PubMed 17720994. Source: MGI

negative regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood vessel endothelial cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cholesterol biosynthetic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from genetic interaction PubMed 21784977. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of platelet activation

Inferred from electronic annotation. Source: Ensembl

nitric oxide mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

phospholipid efflux

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon extension

Inferred from electronic annotation. Source: Ensembl

positive regulation of cGMP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cholesterol efflux

Inferred from electronic annotation. Source: Ensembl

positive regulation of cholesterol esterification

Inferred from mutant phenotype PubMed 15654758. Source: BHF-UCL

positive regulation of low-density lipoprotein particle receptor catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of membrane protein ectodomain proteolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

regulation of Cdc42 protein signal transduction

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from mutant phenotype PubMed 17720994. Source: MGI

response to dietary excess

Inferred from mutant phenotype PubMed 17720994. Source: MGI

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from mutant phenotype PubMed 8773783. Source: MGI

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

reverse cholesterol transport

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

vasodilation

Inferred from mutant phenotype PubMed 9826706. Source: MGI

very-low-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle remodeling

Inferred from mutant phenotype PubMed 15654758. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

chylomicron

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Traceable author statement. Source: Reactome

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 15269218PubMed 7798939PubMed 9186920PubMed 9300780. Source: MGI

extrinsic component of external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

high-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

intermediate-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

late endosome

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle

Inferred from direct assay PubMed 15654758. Source: BHF-UCL

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionantioxidant activity

Inferred from electronic annotation. Source: Ensembl

beta-amyloid binding

Inferred from sequence or structural similarity. Source: UniProtKB

cholesterol transporter activity

Inferred from direct assay PubMed 15269218. Source: MGI

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydroxyapatite binding

Inferred from electronic annotation. Source: Ensembl

lipoprotein particle binding

Inferred from direct assay PubMed 11553788. Source: MGI

metal chelating activity

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine-sterol O-acyltransferase activator activity

Inferred from mutant phenotype PubMed 15654758. Source: BHF-UCL

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 311293Apolipoprotein E
PRO_0000001990

Regions

Repeat72 – 93221
Repeat94 – 115222
Repeat116 – 137223
Repeat138 – 159224
Repeat160 – 181225
Repeat182 – 203226
Repeat204 – 225227
Repeat226 – 247228
Region72 – 2471768 X 22 AA approximate tandem repeats
Region150 – 16011LDL receptor binding Potential
Region154 – 1574Heparin-binding By similarity
Region221 – 2288Heparin-binding By similarity

Amino acid modifications

Modified residue1351Methionine sulfoxide

Experimental info

Sequence conflict1631E → D in AAA37251. Ref.2

Secondary structure

................ 311
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08226 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: 3B36FA897CC34170

FASTA31135,867
        10         20         30         40         50         60 
MKALWAVLLV TLLTGCLAEG EPEVTDQLEW QSNQPWEQAL NRFWDYLRWV QTLSDQVQEE 

        70         80         90        100        110        120 
LQSSQVTQEL TALMEDTMTE VKAYKKELEE QLGPVAEETR ARLGKEVQAA QARLGADMED 

       130        140        150        160        170        180 
LRNRLGQYRN EVHTMLGQST EEIRARLSTH LRKMRKRLMR DAEDLQKRLA VYKAGAREGA 

       190        200        210        220        230        240 
ERGVSAIRER LGPLVEQGRQ RTANLGAGAA QPLRDRAQAF GDRIRGRLEE VGNQARDRLE 

       250        260        270        280        290        300 
EVREHMEEVR SKMEEQTQQI RLQAEIFQAR LKGWFEPIVE DMHRQWANLM EKIQASVATN 

       310 
PIITPVAQEN Q 

« Hide

References

« Hide 'large scale' references
[1]"Structure and expression of mouse apolipoprotein E gene."
Horiuchi K., Tajima S., Menju M., Yamamoto A.
J. Biochem. 106:98-103(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Evolution of apolipoprotein E: mouse sequence and evidence for an 11-nucleotide ancestral unit."
Rajavashisth T.B., Kaptein J.S., Reue K.L., Lusis A.J.
Proc. Natl. Acad. Sci. U.S.A. 82:8085-8089(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[4]"Neuropathological changes in scrapie and Alzheimer's disease are associated with increased expression of apolipoprotein E and cathepsin D in astrocytes."
Diedrich J.F., Minnigan M., Carp R.I., Whitaker J.N., Race R., Frey W. II, Haase A.T.
J. Virol. 65:4759-4768(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-311.
[5]"Mass spectral analysis of the apolipoproteins on mouse high density lipoproteins. Detection of post-translational modifications."
Puppione D.L., Yam L.M., Bassilian S., Souda P., Castellani L.W., Schumaker V.N., Whitelegge J.P.
Biochim. Biophys. Acta 1764:1363-1371(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 43-48; 87-100; 114-122; 130-144; 183-188; 191-198; 202-214; 226-236 AND 253-284, IDENTIFICATION BY MASS SPECTROMETRY, OXIDATION AT MET-135 TO METHIONINE SULFOXIDE.
[6]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 114-122, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00466 Genomic DNA. Translation: BAA00361.1.
M12414 mRNA. Translation: AAA37251.1.
BC083351 mRNA. Translation: AAH83351.1.
M73490 mRNA. Translation: AAA37252.1.
PIRJU0036.
RefSeqNP_033826.2. NM_009696.3.
UniGeneMm.305152.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YA9X-ray2.09A20-200[»]
ProteinModelPortalP08226.
SMRP08226. Positions 19-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198164. 4 interactions.
IntActP08226. 5 interactions.
MINTMINT-242645.

PTM databases

PhosphoSiteP08226.

Proteomic databases

PaxDbP08226.
PRIDEP08226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003066; ENSMUSP00000003066; ENSMUSG00000002985.
ENSMUST00000173739; ENSMUSP00000133371; ENSMUSG00000002985.
ENSMUST00000174064; ENSMUSP00000133302; ENSMUSG00000002985.
ENSMUST00000174355; ENSMUSP00000134160; ENSMUSG00000002985.
GeneID11816.
KEGGmmu:11816.
UCSCuc009fmy.2. mouse.

Organism-specific databases

CTD348.
MGIMGI:88057. Apoe.

Phylogenomic databases

eggNOGNOG44867.
HOGENOMHOG000034006.
HOVERGENHBG010582.
InParanoidP08226.
KOK04524.
OMAPLQERAQ.
OrthoDBEOG793B87.
PhylomeDBP08226.
TreeFamTF334458.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.
REACT_189085. Disease.
REACT_196573. Binding and Uptake of Ligands by Scavenger Receptors.

Gene expression databases

ArrayExpressP08226.
BgeeP08226.
CleanExMM_APOE.
GenevestigatorP08226.

Family and domain databases

InterProIPR000074. ApoA1_A4_E.
[Graphical view]
PfamPF01442. Apolipoprotein. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAPOE. mouse.
EvolutionaryTraceP08226.
NextBio279703.
PROP08226.
SOURCESearch...

Entry information

Entry nameAPOE_MOUSE
AccessionPrimary (citable) accession number: P08226
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot