Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_295031. Retinoid metabolism and transport.
REACT_314625. Chylomicron-mediated lipid transport.
REACT_326379. HDL-mediated lipid transport.
REACT_346699. Scavenging by Class A Receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Apolipoprotein E
Short name:
Apo-E
Gene namesi
Name:Apoe
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:88057. Apoe.

Subcellular locationi

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Add
BLAST
Chaini19 – 311293Apolipoprotein EPRO_0000001990Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi25 – 251O-linked (GalNAc...)By similarity
Modified residuei135 – 1351Methionine sulfoxide1 Publication
Modified residuei139 – 1391PhosphoserineBy similarity
Glycosylationi304 – 3041O-linked (GalNAc...)By similarity

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.By similarity

Keywords - PTMi

Glycoprotein, Oxidation, Phosphoprotein

Proteomic databases

MaxQBiP08226.
PaxDbiP08226.
PRIDEiP08226.

PTM databases

PhosphoSiteiP08226.

Expressioni

Tissue specificityi

Secreted in plasma.

Gene expression databases

BgeeiP08226.
CleanExiMM_APOE.
ExpressionAtlasiP08226. baseline and differential.
GenevisibleiP08226. MM.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1
311
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 313Combined sources
Helixi34 – 5017Combined sources
Helixi55 – 628Combined sources
Helixi65 – 9026Combined sources
Helixi97 – 13438Combined sources
Turni135 – 1373Combined sources
Helixi141 – 17232Combined sources
Helixi184 – 1918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YA9X-ray2.09A20-200[»]
ProteinModelPortaliP08226.
SMRiP08226. Positions 19-305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08226.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati72 – 93221Add
BLAST
Repeati94 – 115222Add
BLAST
Repeati116 – 137223Add
BLAST
Repeati138 – 159224Add
BLAST
Repeati160 – 181225Add
BLAST
Repeati182 – 203226Add
BLAST
Repeati204 – 225227Add
BLAST
Repeati226 – 247228Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 2471768 X 22 AA approximate tandem repeatsAdd
BLAST
Regioni150 – 16011LDL receptor bindingSequence AnalysisAdd
BLAST
Regioni154 – 1574Heparin-bindingBy similarity
Regioni221 – 2288Heparin-bindingBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG44867.
GeneTreeiENSGT00730000111315.
HOGENOMiHOG000034006.
HOVERGENiHBG010582.
InParanoidiP08226.
KOiK04524.
OMAiPLQERAQ.
OrthoDBiEOG793B87.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631E → D in AAA37251 (PubMed:3865219).Curated

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1YA9X-ray2.09A20-200[»]
ProteinModelPortaliP08226.
SMRiP08226. Positions 19-305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiP08226.

Proteomic databases

MaxQBiP08226.
PaxDbiP08226.
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

eggNOGiNOG44867.
GeneTreeiENSGT00730000111315.
HOGENOMiHOG000034006.
HOVERGENiHBG010582.
InParanoidiP08226.
KOiK04524.
OMAiPLQERAQ.
OrthoDBiEOG793B87.
PhylomeDBiP08226.
TreeFamiTF334458.

Enzyme and pathway databases

ReactomeiREACT_295031. Retinoid metabolism and transport.
REACT_314625. Chylomicron-mediated lipid transport.
REACT_326379. HDL-mediated lipid transport.
REACT_346699. Scavenging by Class A Receptors.

Miscellaneous databases

ChiTaRSiApoe. mouse.
EvolutionaryTraceiP08226.
NextBioi279703.
PROiP08226.
SOURCEiSearch...

Gene expression databases

BgeeiP08226.
CleanExiMM_APOE.
ExpressionAtlasiP08226. baseline and differential.
GenevisibleiP08226. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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.
  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.
  7. "CD36 ligands promote sterile inflammation through assembly of a Toll-like receptor 4 and 6 heterodimer."
    Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J., Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A., Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.
    Nat. Immunol. 11:155-161(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.

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: July 22, 2015
This is version 145 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

External Data

Dasty 3

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 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.