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P08226

- APOE_MOUSE

UniProt

P08226 - APOE_MOUSE

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Protein

Apolipoprotein E

Gene

Apoe

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. antioxidant activity Source: Ensembl
  2. beta-amyloid binding Source: UniProtKB
  3. cholesterol transporter activity Source: MGI
  4. heparin binding Source: UniProtKB-KW
  5. hydroxyapatite binding Source: Ensembl
  6. lipoprotein particle binding Source: MGI
  7. metal chelating activity Source: Ensembl
  8. phosphatidylcholine-sterol O-acyltransferase activator activity Source: BHF-UCL
  9. phospholipid binding Source: Ensembl

GO - Biological processi

  1. aging Source: Ensembl
  2. artery morphogenesis Source: MGI
  3. cardiovascular system development Source: MGI
  4. cellular calcium ion homeostasis Source: MGI
  5. cellular response to cholesterol Source: Ensembl
  6. cellular response to growth factor stimulus Source: Ensembl
  7. cellular response to interleukin-1 Source: Ensembl
  8. cGMP-mediated signaling Source: Ensembl
  9. cholesterol catabolic process Source: MGI
  10. cholesterol efflux Source: MGI
  11. cholesterol homeostasis Source: MGI
  12. cholesterol metabolic process Source: MGI
  13. chylomicron remnant clearance Source: Ensembl
  14. fatty acid homeostasis Source: Ensembl
  15. G-protein coupled receptor signaling pathway Source: Ensembl
  16. high-density lipoprotein particle assembly Source: Ensembl
  17. high-density lipoprotein particle clearance Source: Ensembl
  18. high-density lipoprotein particle remodeling Source: Ensembl
  19. lipid homeostasis Source: MGI
  20. lipid metabolic process Source: MGI
  21. lipoprotein biosynthetic process Source: MGI
  22. lipoprotein catabolic process Source: MGI
  23. lipoprotein metabolic process Source: MGI
  24. long-chain fatty acid transport Source: Ensembl
  25. low-density lipoprotein particle remodeling Source: BHF-UCL
  26. maintenance of location in cell Source: MGI
  27. negative regulation of beta-amyloid formation Source: Ensembl
  28. negative regulation of blood vessel endothelial cell migration Source: Ensembl
  29. negative regulation of cholesterol biosynthetic process Source: Ensembl
  30. negative regulation of cholesterol efflux Source: Ensembl
  31. negative regulation of dendritic spine development Source: Ensembl
  32. negative regulation of dendritic spine maintenance Source: Ensembl
  33. negative regulation of endothelial cell proliferation Source: Ensembl
  34. negative regulation of inflammatory response Source: UniProtKB
  35. negative regulation of lipid transport across blood brain barrier Source: Ensembl
  36. negative regulation of MAP kinase activity Source: Ensembl
  37. negative regulation of neuron apoptotic process Source: Ensembl
  38. negative regulation of phospholipid efflux Source: Ensembl
  39. negative regulation of platelet activation Source: Ensembl
  40. negative regulation of postsynaptic membrane organization Source: Ensembl
  41. negative regulation of presynaptic membrane organization Source: Ensembl
  42. nitric oxide mediated signal transduction Source: Ensembl
  43. oligodendrocyte differentiation Source: Ensembl
  44. phospholipid efflux Source: Ensembl
  45. positive regulation of axon extension Source: Ensembl
  46. positive regulation of beta-amyloid formation Source: Ensembl
  47. positive regulation of cGMP biosynthetic process Source: Ensembl
  48. positive regulation of cholesterol efflux Source: Ensembl
  49. positive regulation of cholesterol esterification Source: BHF-UCL
  50. positive regulation of dendritic spine development Source: Ensembl
  51. positive regulation of dendritic spine maintenance Source: Ensembl
  52. positive regulation of lipid biosynthetic process Source: Ensembl
  53. positive regulation of lipid transport across blood brain barrier Source: Ensembl
  54. positive regulation of low-density lipoprotein particle receptor catabolic process Source: Ensembl
  55. positive regulation of membrane protein ectodomain proteolysis Source: Ensembl
  56. positive regulation of neurofibrillary tangle assembly Source: Ensembl
  57. positive regulation of neuron death Source: Ensembl
  58. positive regulation of nitric-oxide synthase activity Source: Ensembl
  59. positive regulation of phospholipid efflux Source: Ensembl
  60. positive regulation of postsynaptic membrane organization Source: Ensembl
  61. positive regulation of presynaptic membrane organization Source: Ensembl
  62. receptor-mediated endocytosis Source: Ensembl
  63. regulation of beta-amyloid clearance Source: Ensembl
  64. regulation of Cdc42 protein signal transduction Source: Ensembl
  65. regulation of gene expression Source: MGI
  66. regulation of tau-protein kinase activity Source: Ensembl
  67. response to dietary excess Source: MGI
  68. response to ethanol Source: Ensembl
  69. response to insulin Source: Ensembl
  70. response to oxidative stress Source: MGI
  71. response to retinoic acid Source: Ensembl
  72. reverse cholesterol transport Source: Ensembl
  73. triglyceride metabolic process Source: Ensembl
  74. vasodilation Source: MGI
  75. very-low-density lipoprotein particle clearance Source: Ensembl
  76. very-low-density lipoprotein particle remodeling Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_196581. Scavenging by Class A Receptors.
REACT_198569. Retinoid metabolism and transport.
REACT_213857. HDL-mediated lipid transport.
REACT_216017. Chylomicron-mediated lipid 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
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:88057. Apoe.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. chylomicron Source: UniProtKB-KW
  3. cytosol Source: Reactome
  4. dendrite Source: Ensembl
  5. extracellular region Source: Reactome
  6. extracellular space Source: MGI
  7. extracellular vesicular exosome Source: Ensembl
  8. extrinsic component of external side of plasma membrane Source: Ensembl
  9. Golgi apparatus Source: Ensembl
  10. high-density lipoprotein particle Source: UniProtKB-KW
  11. intermediate-density lipoprotein particle Source: Ensembl
  12. late endosome Source: Ensembl
  13. low-density lipoprotein particle Source: BHF-UCL
  14. neuronal cell body Source: Ensembl
  15. nucleus Source: Ensembl
  16. very-low-density lipoprotein particle Source: UniProtKB-KW
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
Modified residuei135 – 1351Methionine sulfoxide1 Publication

Post-translational modificationi

Phosphorylation sites are present in the extracellular medium.By similarity

Keywords - PTMi

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.
GenevestigatoriP08226.

Interactioni

Protein-protein interaction databases

BioGridi198164. 4 interactions.
IntActiP08226. 5 interactions.
MINTiMINT-242645.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
HOGENOMiHOG000034006.
HOVERGENiHBG010582.
InParanoidiP08226.
KOiK04524.
OMAiPLQERAQ.
OrthoDBiEOG793B87.
PhylomeDBiP08226.
TreeFamiTF334458.

Family and domain databases

InterProiIPR000074. ApoA1_A4_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:
EMBL
GenBank
DDBJ
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_033826.2. NM_009696.3.
UniGeneiMm.305152.

Genome annotation databases

EnsembliENSMUST00000003066; ENSMUSP00000003066; ENSMUSG00000002985.
ENSMUST00000173739; ENSMUSP00000133371; ENSMUSG00000002985.
ENSMUST00000174064; ENSMUSP00000133302; ENSMUSG00000002985.
ENSMUST00000174355; ENSMUSP00000134160; ENSMUSG00000002985.
GeneIDi11816.
KEGGimmu:11816.
UCSCiuc009fmy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D00466 Genomic DNA. Translation: BAA00361.1 .
M12414 mRNA. Translation: AAA37251.1 .
BC083351 mRNA. Translation: AAH83351.1 .
M73490 mRNA. Translation: AAA37252.1 .
CCDSi CCDS20912.1.
PIRi JU0036.
RefSeqi NP_033826.2. NM_009696.3.
UniGenei Mm.305152.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1YA9 X-ray 2.09 A 20-200 [» ]
ProteinModelPortali P08226.
SMRi P08226. Positions 19-305.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198164. 4 interactions.
IntActi P08226. 5 interactions.
MINTi MINT-242645.

PTM databases

PhosphoSitei P08226.

Proteomic databases

MaxQBi P08226.
PaxDbi P08226.
PRIDEi P08226.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000003066 ; ENSMUSP00000003066 ; ENSMUSG00000002985 .
ENSMUST00000173739 ; ENSMUSP00000133371 ; ENSMUSG00000002985 .
ENSMUST00000174064 ; ENSMUSP00000133302 ; ENSMUSG00000002985 .
ENSMUST00000174355 ; ENSMUSP00000134160 ; ENSMUSG00000002985 .
GeneIDi 11816.
KEGGi mmu:11816.
UCSCi uc009fmy.2. mouse.

Organism-specific databases

CTDi 348.
MGIi MGI:88057. Apoe.

Phylogenomic databases

eggNOGi NOG44867.
HOGENOMi HOG000034006.
HOVERGENi HBG010582.
InParanoidi P08226.
KOi K04524.
OMAi PLQERAQ.
OrthoDBi EOG793B87.
PhylomeDBi P08226.
TreeFami TF334458.

Enzyme and pathway databases

Reactomei REACT_196581. Scavenging by Class A Receptors.
REACT_198569. Retinoid metabolism and transport.
REACT_213857. HDL-mediated lipid transport.
REACT_216017. Chylomicron-mediated lipid transport.

Miscellaneous databases

ChiTaRSi APOE. mouse.
EvolutionaryTracei P08226.
NextBioi 279703.
PROi P08226.
SOURCEi Search...

Gene expression databases

Bgeei P08226.
CleanExi MM_APOE.
ExpressionAtlasi P08226. baseline and differential.
Genevestigatori P08226.

Family and domain databases

InterProi IPR000074. ApoA1_A4_E.
[Graphical view ]
Pfami PF01442. Apolipoprotein. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 136 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