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P08226

- APOE_MOUSE

UniProt

P08226 - APOE_MOUSE

Protein

Apolipoprotein E

Gene

Apoe

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      Previous versions | rss
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    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
    10. protein binding Source: MGI

    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. G-protein coupled receptor signaling pathway Source: Ensembl
    15. high-density lipoprotein particle assembly Source: Ensembl
    16. high-density lipoprotein particle clearance Source: Ensembl
    17. high-density lipoprotein particle remodeling Source: Ensembl
    18. lipid homeostasis Source: MGI
    19. lipid metabolic process Source: MGI
    20. lipoprotein biosynthetic process Source: MGI
    21. lipoprotein catabolic process Source: MGI
    22. lipoprotein metabolic process Source: MGI
    23. low-density lipoprotein particle remodeling Source: BHF-UCL
    24. maintenance of location in cell Source: MGI
    25. negative regulation of blood vessel endothelial cell migration Source: Ensembl
    26. negative regulation of cholesterol biosynthetic process Source: Ensembl
    27. negative regulation of endothelial cell proliferation Source: Ensembl
    28. negative regulation of inflammatory response Source: UniProtKB
    29. negative regulation of MAP kinase activity Source: Ensembl
    30. negative regulation of neuron apoptotic process Source: Ensembl
    31. negative regulation of platelet activation Source: Ensembl
    32. nitric oxide mediated signal transduction Source: Ensembl
    33. oligodendrocyte differentiation Source: Ensembl
    34. phospholipid efflux Source: Ensembl
    35. positive regulation of axon extension Source: Ensembl
    36. positive regulation of cGMP biosynthetic process Source: Ensembl
    37. positive regulation of cholesterol efflux Source: Ensembl
    38. positive regulation of cholesterol esterification Source: BHF-UCL
    39. positive regulation of low-density lipoprotein particle receptor catabolic process Source: Ensembl
    40. positive regulation of membrane protein ectodomain proteolysis Source: Ensembl
    41. positive regulation of nitric-oxide synthase activity Source: Ensembl
    42. receptor-mediated endocytosis Source: Ensembl
    43. regulation of Cdc42 protein signal transduction Source: Ensembl
    44. regulation of gene expression Source: MGI
    45. response to dietary excess Source: MGI
    46. response to ethanol Source: Ensembl
    47. response to insulin Source: Ensembl
    48. response to oxidative stress Source: MGI
    49. response to retinoic acid Source: Ensembl
    50. reverse cholesterol transport Source: Ensembl
    51. triglyceride metabolic process Source: Ensembl
    52. vasodilation Source: MGI
    53. very-low-density lipoprotein particle clearance Source: Ensembl
    54. very-low-density lipoprotein particle remodeling Source: BHF-UCL

    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. chylomicron Source: UniProtKB-KW
    2. cytosol Source: Reactome
    3. dendrite Source: Ensembl
    4. extracellular region Source: Reactome
    5. extracellular space Source: MGI
    6. extrinsic component of external side of plasma membrane Source: Ensembl
    7. Golgi apparatus Source: Ensembl
    8. high-density lipoprotein particle Source: UniProtKB-KW
    9. intermediate-density lipoprotein particle Source: Ensembl
    10. late endosome Source: Ensembl
    11. low-density lipoprotein particle Source: BHF-UCL
    12. neuronal cell body Source: Ensembl
    13. very-low-density lipoprotein particle Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chylomicron, HDL, Secreted, VLDL

    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

    ArrayExpressiP08226.
    BgeeiP08226.
    CleanExiMM_APOE.
    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

    MKALWAVLLV TLLTGCLAEG EPEVTDQLEW QSNQPWEQAL NRFWDYLRWV    50
    QTLSDQVQEE LQSSQVTQEL TALMEDTMTE VKAYKKELEE QLGPVAEETR 100
    ARLGKEVQAA QARLGADMED LRNRLGQYRN EVHTMLGQST EEIRARLSTH 150
    LRKMRKRLMR DAEDLQKRLA VYKAGAREGA ERGVSAIRER LGPLVEQGRQ 200
    RTANLGAGAA QPLRDRAQAF GDRIRGRLEE VGNQARDRLE EVREHMEEVR 250
    SKMEEQTQQI RLQAEIFQAR LKGWFEPIVE DMHRQWANLM EKIQASVATN 300
    PIITPVAQEN Q 311
    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

    ArrayExpressi P08226.
    Bgeei P08226.
    CleanExi MM_APOE.
    Genevestigatori P08226.

    Family and domain databases

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

    Publicationsi

    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.

    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 1, 2014
    This is version 135 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