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Protein

Apolipoprotein E

Gene

Apoe

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

GO - Molecular functioni

GO - Biological processi

  • AMPA glutamate receptor clustering Source: MGI
  • artery morphogenesis Source: MGI
  • cardiovascular system development Source: MGI
  • cellular calcium ion homeostasis Source: MGI
  • cGMP-mediated signaling Source: MGI
  • cholesterol biosynthetic process Source: GO_Central
  • cholesterol catabolic process Source: MGI
  • cholesterol efflux Source: MGI
  • cholesterol homeostasis Source: BHF-UCL
  • cholesterol metabolic process Source: MGI
  • chylomicron remnant clearance Source: MGI
  • fatty acid homeostasis Source: MGI
  • G-protein coupled receptor signaling pathway Source: MGI
  • high-density lipoprotein particle assembly Source: MGI
  • high-density lipoprotein particle clearance Source: MGI
  • high-density lipoprotein particle remodeling Source: MGI
  • lipid homeostasis Source: MGI
  • lipid metabolic process Source: MGI
  • lipid transport involved in lipid storage Source: BHF-UCL
  • lipoprotein biosynthetic process Source: MGI
  • lipoprotein catabolic process Source: MGI
  • lipoprotein metabolic process Source: MGI
  • long-chain fatty acid transport Source: MGI
  • low-density lipoprotein particle remodeling Source: BHF-UCL
  • maintenance of location in cell Source: MGI
  • negative regulation of beta-amyloid formation Source: MGI
  • negative regulation of blood coagulation Source: MGI
  • negative regulation of blood vessel endothelial cell migration Source: MGI
  • negative regulation of cholesterol biosynthetic process Source: MGI
  • negative regulation of endothelial cell proliferation Source: MGI
  • negative regulation of inflammatory response Source: UniProtKB
  • negative regulation of MAP kinase activity Source: MGI
  • negative regulation of neuron apoptotic process Source: GO_Central
  • negative regulation of neuron death Source: MGI
  • negative regulation of platelet activation Source: MGI
  • negative regulation of presynaptic membrane organization Source: MGI
  • nitric oxide mediated signal transduction Source: MGI
  • NMDA glutamate receptor clustering Source: MGI
  • phospholipid efflux Source: MGI
  • positive regulation by host of viral process Source: MGI
  • positive regulation of cGMP biosynthetic process Source: MGI
  • positive regulation of cholesterol efflux Source: MGI
  • positive regulation of cholesterol esterification Source: BHF-UCL
  • positive regulation of dendritic spine development Source: MGI
  • positive regulation of dendritic spine maintenance Source: MGI
  • positive regulation of lipid biosynthetic process Source: MGI
  • positive regulation of lipid transport across blood brain barrier Source: MGI
  • positive regulation of low-density lipoprotein particle receptor catabolic process Source: MGI
  • positive regulation of membrane protein ectodomain proteolysis Source: MGI
  • positive regulation of nitric-oxide synthase activity Source: MGI
  • positive regulation of phospholipid efflux Source: MGI
  • positive regulation of postsynaptic membrane organization Source: MGI
  • protein import Source: MGI
  • receptor-mediated endocytosis Source: MGI
  • regulation of axon extension Source: GO_Central
  • regulation of beta-amyloid clearance Source: MGI
  • regulation of Cdc42 protein signal transduction Source: MGI
  • regulation of cholesterol transport Source: GO_Central
  • regulation of gene expression Source: MGI
  • regulation of plasma lipoprotein particle levels Source: BHF-UCL
  • response to dietary excess Source: MGI
  • response to oxidative stress Source: MGI
  • retinoid metabolic process Source: Reactome
  • reverse cholesterol transport Source: MGI
  • triglyceride catabolic process Source: GO_Central
  • triglyceride homeostasis Source: BHF-UCL
  • triglyceride metabolic process Source: MGI
  • vasodilation Source: MGI
  • very-low-density lipoprotein particle clearance Source: MGI
  • very-low-density lipoprotein particle remodeling Source: BHF-UCL
  • virion assembly Source: MGI
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiR-MMU-174800. Chylomicron-mediated lipid transport.
R-MMU-194223. HDL-mediated lipid transport.
R-MMU-3000480. Scavenging by Class A Receptors.
R-MMU-975634. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein E
Short name:
Apo-E
Gene namesi
Name:Apoe
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:88057. Apoe.

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chylomicron, HDL, Secreted, VLDL

Pathology & Biotechi

Disruption phenotypei

APOE single knockout mice are atherosclerosis-prone. Animals with a double knockout of APOE and CD36, fed a Western diet for 12 weeks, exhibit much lower levels of CXCL1, CXCL2 and CCL5 mRNA expression in the descending aorta and a corresponding decrease in atherosclerotic lesion formation, compared to APOE single knockout mice. Animals with a double knockout of APOE and TLR4 or TLR6 also have less aortic plaque formation than single knockout mice. All 3 double knockout show lower serum concentrations of IL1A, ILB and IL18.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
ChainiPRO_000000199019 – 311Apolipoprotein EAdd BLAST293

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi25O-linked (GalNAc...)By similarity1
Modified residuei135Methionine sulfoxide1 Publication1
Modified residuei139PhosphoserineCombined sources1
Glycosylationi304O-linked (GalNAc...)By similarity1

Post-translational modificationi

Phosphorylated by FAM20C in the extracellular medium.By similarity

Keywords - PTMi

Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

PaxDbiP08226.
PeptideAtlasiP08226.
PRIDEiP08226.

PTM databases

iPTMnetiP08226.
PhosphoSitePlusiP08226.

Expressioni

Tissue specificityi

Secreted in plasma.

Gene expression databases

BgeeiENSMUSG00000002985.
CleanExiMM_APOE.
ExpressionAtlasiP08226. baseline and differential.
GenevisibleiP08226. MM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi198164. 5 interactors.
IntActiP08226. 5 interactors.
MINTiMINT-242645.
STRINGi10090.ENSMUSP00000003066.

Structurei

Secondary structure

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 31Combined sources3
Helixi34 – 50Combined sources17
Helixi55 – 62Combined sources8
Helixi65 – 90Combined sources26
Helixi97 – 134Combined sources38
Turni135 – 137Combined sources3
Helixi141 – 172Combined sources32
Helixi184 – 191Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YA9X-ray2.09A20-200[»]
ProteinModelPortaliP08226.
SMRiP08226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08226.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati72 – 931Add BLAST22
Repeati94 – 1152Add BLAST22
Repeati116 – 1373Add BLAST22
Repeati138 – 1594Add BLAST22
Repeati160 – 1815Add BLAST22
Repeati182 – 2036Add BLAST22
Repeati204 – 2257Add BLAST22
Repeati226 – 2478Add BLAST22

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni72 – 2478 X 22 AA approximate tandem repeatsAdd BLAST176
Regioni150 – 160LDL receptor bindingBy similarityAdd BLAST11
Regioni154 – 157Heparin-bindingBy similarity4
Regioni221 – 228Heparin-bindingBy similarity8

Sequence similaritiesi

Belongs to the apolipoprotein A1/A4/E family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IVK0. Eukaryota.
ENOG4111MYC. LUCA.
GeneTreeiENSGT00730000111315.
HOGENOMiHOG000034006.
HOVERGENiHBG010582.
InParanoidiP08226.
KOiK04524.
OMAiMGSRTRD.
OrthoDBiEOG091G0IA5.
PhylomeDBiP08226.
TreeFamiTF334458.

Family and domain databases

InterProiIPR000074. ApoA_E.
[Graphical view]
PfamiPF01442. Apolipoprotein. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08226-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALWAVLLV TLLTGCLAEG EPEVTDQLEW QSNQPWEQAL NRFWDYLRWV
60 70 80 90 100
QTLSDQVQEE LQSSQVTQEL TALMEDTMTE VKAYKKELEE QLGPVAEETR
110 120 130 140 150
ARLGKEVQAA QARLGADMED LRNRLGQYRN EVHTMLGQST EEIRARLSTH
160 170 180 190 200
LRKMRKRLMR DAEDLQKRLA VYKAGAREGA ERGVSAIRER LGPLVEQGRQ
210 220 230 240 250
RTANLGAGAA QPLRDRAQAF GDRIRGRLEE VGNQARDRLE EVREHMEEVR
260 270 280 290 300
SKMEEQTQQI RLQAEIFQAR LKGWFEPIVE DMHRQWANLM EKIQASVATN
310
PIITPVAQEN Q
Length:311
Mass (Da):35,867
Last modified:August 1, 1990 - v2
Checksum:i3B36FA897CC34170
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti163E → D in AAA37251 (PubMed:3865219).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00466 Genomic DNA. Translation: BAA00361.1.
M12414 mRNA. Translation: AAA37251.1.
BC083351 mRNA. Translation: AAH83351.1.
M73490 mRNA. Translation: AAA37252.1.
CCDSiCCDS20912.1.
PIRiJU0036.
RefSeqiNP_001292748.1. NM_001305819.1.
NP_001292772.1. NM_001305843.1.
NP_001292773.1. NM_001305844.1.
NP_033826.2. NM_009696.4.
UniGeneiMm.305152.

Genome annotation databases

EnsembliENSMUST00000003066; ENSMUSP00000003066; ENSMUSG00000002985.
ENSMUST00000173739; ENSMUSP00000133371; ENSMUSG00000002985.
ENSMUST00000174064; ENSMUSP00000133302; ENSMUSG00000002985.
ENSMUST00000174355; ENSMUSP00000134160; ENSMUSG00000002985.
GeneIDi11816.
KEGGimmu:11816.
UCSCiuc009fmy.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00466 Genomic DNA. Translation: BAA00361.1.
M12414 mRNA. Translation: AAA37251.1.
BC083351 mRNA. Translation: AAH83351.1.
M73490 mRNA. Translation: AAA37252.1.
CCDSiCCDS20912.1.
PIRiJU0036.
RefSeqiNP_001292748.1. NM_001305819.1.
NP_001292772.1. NM_001305843.1.
NP_001292773.1. NM_001305844.1.
NP_033826.2. NM_009696.4.
UniGeneiMm.305152.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YA9X-ray2.09A20-200[»]
ProteinModelPortaliP08226.
SMRiP08226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198164. 5 interactors.
IntActiP08226. 5 interactors.
MINTiMINT-242645.
STRINGi10090.ENSMUSP00000003066.

PTM databases

iPTMnetiP08226.
PhosphoSitePlusiP08226.

Proteomic databases

PaxDbiP08226.
PeptideAtlasiP08226.
PRIDEiP08226.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000003066; ENSMUSP00000003066; ENSMUSG00000002985.
ENSMUST00000173739; ENSMUSP00000133371; ENSMUSG00000002985.
ENSMUST00000174064; ENSMUSP00000133302; ENSMUSG00000002985.
ENSMUST00000174355; ENSMUSP00000134160; ENSMUSG00000002985.
GeneIDi11816.
KEGGimmu:11816.
UCSCiuc009fmy.3. mouse.

Organism-specific databases

CTDi348.
MGIiMGI:88057. Apoe.

Phylogenomic databases

eggNOGiENOG410IVK0. Eukaryota.
ENOG4111MYC. LUCA.
GeneTreeiENSGT00730000111315.
HOGENOMiHOG000034006.
HOVERGENiHBG010582.
InParanoidiP08226.
KOiK04524.
OMAiMGSRTRD.
OrthoDBiEOG091G0IA5.
PhylomeDBiP08226.
TreeFamiTF334458.

Enzyme and pathway databases

ReactomeiR-MMU-174800. Chylomicron-mediated lipid transport.
R-MMU-194223. HDL-mediated lipid transport.
R-MMU-3000480. Scavenging by Class A Receptors.
R-MMU-975634. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSiApoe. mouse.
EvolutionaryTraceiP08226.
PROiP08226.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000002985.
CleanExiMM_APOE.
ExpressionAtlasiP08226. baseline and differential.
GenevisibleiP08226. MM.

Family and domain databases

InterProiIPR000074. ApoA_E.
[Graphical view]
PfamiPF01442. Apolipoprotein. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAPOE_MOUSE
AccessioniPrimary (citable) accession number: P08226
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.