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Protein

Apolipoprotein E

Gene

Apoe

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionHeparin-binding
Biological processLipid transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-3000480 Scavenging by Class A Receptors
R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-MMU-8957275 Post-translational protein phosphorylation
R-MMU-8963888 Chylomicron assembly
R-MMU-8963901 Chylomicron remodeling
R-MMU-8964026 Chylomicron clearance
R-MMU-8964058 HDL remodeling
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:88057 Apoe

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) threonineBy similarity1
Modified residuei135Methionine sulfoxide1 Publication1
Modified residuei139PhosphoserineCombined sources1
Glycosylationi304O-linked (GalNAc...) threonineBy 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, 6 interactors
IntActiP08226, 6 interactors
MINTiP08226
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

InterProiView protein in InterPro
IPR000074 ApoA_E
PfamiView protein in Pfam
PF01442 Apolipoprotein, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiAPOE_MOUSE
AccessioniPrimary (citable) accession number: P08226
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1990
Last modified: May 23, 2018
This is version 174 of the entry and version 2 of the sequence. See 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

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