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P02650 (APOE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length312 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.

Miscellaneous

The mature protein has no cysteine residues; however, in different allelic variants where cysteine residues replace arginine at positions 155 or 168, binding of Apo-E to cell membrane receptors is decreased. The amino end of this protein is therefore thought to interact with the receptor.

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 termComplete 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 direct assay PubMed 19809892. Source: RGD

artery morphogenesis

Inferred from electronic annotation. Source: Ensembl

cGMP-mediated signaling

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to cholesterol

Inferred from expression pattern PubMed 21169230. Source: RGD

cellular response to growth factor stimulus

Inferred from expression pattern PubMed 19713443PubMed 20535563. Source: RGD

cellular response to interleukin-1

Inferred from expression pattern PubMed 22171672. Source: RGD

cholesterol catabolic process

Inferred from electronic annotation. Source: Ensembl

cholesterol efflux

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from electronic annotation. Source: Ensembl

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 transport

Inferred from direct assay PubMed 12482838PubMed 2492020. Source: RGD

lipoprotein biosynthetic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein catabolic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Inferred from direct assay PubMed 2492020. Source: RGD

low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

maintenance of location in cell

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from direct assay PubMed 17314289. Source: RGD

negative regulation of platelet activation

Inferred from electronic annotation. Source: Ensembl

neuron projection regeneration

Traceable author statement PubMed 12898539. Source: RGD

nitric oxide mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

oligodendrocyte differentiation

Inferred from expression pattern PubMed 21972082. Source: RGD

peripheral nervous system axon regeneration

Inferred from expression pattern PubMed 2120218. Source: RGD

phospholipid efflux

Inferred from electronic annotation. Source: Ensembl

positive regulation of axon extension

Inferred from direct assay PubMed 21040802. Source: RGD

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 electronic annotation. Source: Ensembl

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

response to dietary excess

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from expression pattern PubMed 11839466. Source: RGD

response to insulin

Inferred from expression pattern PubMed 22691999. Source: RGD

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from expression pattern PubMed 21907828. Source: RGD

reverse cholesterol transport

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from electronic annotation. Source: Ensembl

vasodilation

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Ensembl

very-low-density lipoprotein particle remodeling

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 11839466PubMed 7806565. Source: RGD

cell surface

Inferred from direct assay PubMed 2493483. Source: RGD

chylomicron

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay PubMed 7616121PubMed 8875469. Source: RGD

dendrite

Inferred from direct assay PubMed 8875469. Source: RGD

discoidal high-density lipoprotein particle

Inferred from direct assay PubMed 2493483. Source: RGD

endoplasmic reticulum

Inferred from direct assay PubMed 2493483. Source: RGD

endosome

Inferred from direct assay PubMed 2493483. Source: RGD

extracellular space

Inferred from direct assay PubMed 16947119. Source: RGD

extrinsic component of external side of plasma membrane

Inferred from direct assay PubMed 7616121. Source: RGD

intermediate-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

late endosome

Inferred from direct assay PubMed 7806565. Source: RGD

low-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

lysosome

Inferred from direct assay PubMed 2493483. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 8875469. Source: RGD

nuclear envelope

Inferred from direct assay PubMed 2493483. Source: RGD

plasma membrane

Inferred from direct assay PubMed 21169230. Source: RGD

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 electronic annotation. Source: Ensembl

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydroxyapatite binding

Inferred from direct assay PubMed 21839718. Source: RGD

lipid transporter activity

Inferred from direct assay PubMed 12482838PubMed 2492020. Source: RGD

lipoprotein particle binding

Inferred from electronic annotation. Source: Ensembl

metal chelating activity

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine-sterol O-acyltransferase activator activity

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Inferred from direct assay PubMed 2492020. Source: RGD

receptor binding

Inferred from physical interaction PubMed 17889837. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Chain19 – 312294Apolipoprotein E
PRO_0000001996

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 By similarity

Experimental info

Sequence conflict1041A → T in CAA28650. Ref.1
Sequence conflict1101A → T no nucleotide entry Ref.3
Sequence conflict1101A → T in AAC60703. Ref.4
Sequence conflict1411E → D no nucleotide entry Ref.3
Sequence conflict1411E → D in AAC60703. Ref.4
Sequence conflict206 – 2138GAGAAQPL → RWRRPAP in CAA28650. Ref.1
Sequence conflict206 – 2138GAGAAQPL → RWRRPAP no nucleotide entry Ref.3
Sequence conflict309 – 3102LE → WR no nucleotide entry Ref.3
Sequence conflict309 – 3102LE → WR in AAC60703. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P02650 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 8180EEE933378D92

FASTA31235,753
        10         20         30         40         50         60 
MKALWALLLV PLLTGCLAEG ELEVTDQLPG QSDQPWEQAL NRFWDYLRWV QTLSDQVQEE 

        70         80         90        100        110        120 
LQSSQVTQEL TVLMEDTMTE VKAYKKELEE QLGPVAEETR ARLAKEVQAA QARLGADMED 

       130        140        150        160        170        180 
LRNRLGQYRN EVNTMLGQST EELRSRLSTH LRKMRKRLMR DADDLQKRLA VYKAGAQEGA 

       190        200        210        220        230        240 
ERGVSAIRER LGPLVEQGRQ RTANLGAGAA QPLRDRAQAL SDRIRGRLEE VGNQARDRLE 

       250        260        270        280        290        300 
EVREQMEEVR SKMEEQTQQI RLQAEIFQAR IKGWFEPLVE DMQRQWANLM EKIQASVATN 

       310 
SIASTTVPLE NQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete nucleotide sequence of the gene encoding the rat apolipoprotein E."
Fukazawa C., Matsumoto A., Taylor L.M.
Nucleic Acids Res. 14:9527-9528(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure and expression of the rat apolipoprotein E gene."
Fung W.-P., Howlett G.J., Schreiber G.
J. Biol. Chem. 261:13777-13783(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Rat apolipoprotein E mRNA. Cloning and sequencing of double-stranded cDNA."
McLean J.W., Fukazawa C., Taylor J.M.
J. Biol. Chem. 258:8993-9000(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Secretion by Saccharomyces cerevisiae of rat apolipoprotein E as a fusion to Mucor rennin."
Nomura N., Yamada H., Matsubara N., Horinouchi S., Beppu T.
Appl. Microbiol. Biotechnol. 42:865-870(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[5]"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].
Tissue: Ovary.
[6]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 87-100; 114-122; 130-144; 191-199; 202-216; 226-236 AND 262-270, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04979 Genomic DNA. Translation: CAA28650.1.
J02582 Genomic DNA. Translation: AAA40755.1.
S76779 mRNA. Translation: AAC60703.1.
BC086581 mRNA. Translation: AAH86581.1.
PIRLPRTE. A26189.
RefSeqNP_001257610.1. NM_001270681.1.
NP_001257611.1. NM_001270682.1.
NP_001257612.1. NM_001270683.1.
NP_001257613.1. NM_001270684.1.
NP_620183.2. NM_138828.3.
UniGeneRn.32351.

3D structure databases

ProteinModelPortalP02650.
SMRP02650. Positions 23-195.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247757. 1 interaction.
IntActP02650. 3 interactions.
MINTMINT-4585732.
STRING10116.ENSRNOP00000050968.

PTM databases

PhosphoSiteP02650.

Proteomic databases

PaxDbP02650.
PRIDEP02650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000041891; ENSRNOP00000050968; ENSRNOG00000018454.
GeneID25728.
KEGGrno:25728.
UCSCRGD:2138. rat.

Organism-specific databases

CTD348.
RGD2138. Apoe.

Phylogenomic databases

eggNOGNOG44867.
GeneTreeENSGT00730000111315.
HOGENOMHOG000034006.
HOVERGENHBG010582.
InParanoidP02650.
KOK04524.
OMAPLQERAQ.
OrthoDBEOG793B87.
PhylomeDBP02650.
TreeFamTF334458.

Gene expression databases

GenevestigatorP02650.

Family and domain databases

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

Other

NextBio607845.
PROP02650.

Entry information

Entry nameAPOE_RAT
AccessionPrimary (citable) accession number: P02650
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 122 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