Primary Information |
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BoMiProt ID | Bomi223 |
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Protein Name | Apolipoprotein E |
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Organism | Bos taurus |
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Uniprot ID | Q03247 |
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Milk Fraction | Whey, MFGM, Exosome |
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Ref Sequence ID | NP_776416.1 |
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Aminoacid Length | 316 |
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Molecular Weight | 35980 |
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FASTA Sequence |
Download |
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Gene Name | APOE |
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Gene ID | 281004 |
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Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | the liver, brain, spleen,
lungs, adrenal gland, ovaries, kidneys, and muscles as found in humans |
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Protein Function | Component of plasma lipoproteins in the transport of lipids among cells of
different organs and within specific tissues; Mediate the
binding of lipoproteins or lipid complexes in the plasma or interstitial fluids to specific cell-surface
receptors; participates in
the distribution/redistribution of lipids among various tissues and cells of the body; plays a key role in regulating the clearance of these lipoproteins from the plasma |
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Biochemical Properties | associated with very low density lipoproteins; intermediate
density lipoproteins, chylomicron remnants, and certain subclasses of high-density lipoproteins; ApoE mediates the
interaction of apoE-containing lipoproteins and lipid complexes to the LDL receptor, the LDL receptor related
protein (LRP), the VLDL receptor, the apoE receptor-2, and gp330; Arginine 158 appears to be involved in modulating the conformation of the
136–150 region and is involved only indirectly in receptor binding activity. ApoE3 and apoE4, which
display normal receptor binding activity, have arginine at residue 158, whereas apoE2, which is
defective in receptor binding activity, has cysteine. |
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Significance in milk | Related to lipid transport; expression decreases over lactation period |
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PTMs | Glycosylated: human mature apolipoprotein E (ApoE) is a 299-amino acid glycoprotein
(34–37 kDa); various other PTMs include methylation, Dihydroxylation, dimethylation; four glycosylation sites (T194, T289, S290, and S296 residues) on
secreted and cellular human ApoE |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q03247|APOE_BOVIN Apolipoprotein E OS=Bos taurus OX=9913 GN=APOE PE=1 SV=1
MKVLWVAVVVALLAGCQADMEGELGPEEPLTT*32QQPRGKDSQPWEQALGRFWDYLRWVQTL
SDQVQEELLNTQVIQELTALMEETMKEVKAYKEELEGQLGPMAQETQARVSKELQAAQAR
LGSDMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLPKRLLRDADDLKKRLAVYQ
AGASEGAERSLSAIRERFGPLVEQGQSRAAT*211LSTLAGQPLLERAEAWRQKLHGRLEEVGV
RAQDRLDKIRQQLEEVHAKVEEQGNQMRLQAEAFQARLRSWFEPLVEDMQRQWAGLVEKV
QLALRPSPT*309S*310PPSENH |
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | serves as a ligand for the low-density lipoprotein
(LDL) receptor (LDLR), that is involved in lipid metabolism; alter the
domain interactions, functions, binding affinities, hydrophobicity, and
structural stability of ApoE; glycation at the K75 position may impair lipoprotein-cell interactions
through heparan sulfate proteoglycans, andmay lead to enhancement
of lipid abnormalities in diabetic patients |
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Bibliography | 1. Chartier-Hariln, M.-C. et al. (1994) ‘Apolipoprotein E, ɛ4 allele as a major risk factor for sporadic early and late-onset forms of Alzheimer’s disease: analysis of the 19q13.2 chromosomal region’, Human Molecular Genetics, 3(4), pp. 569–574. doi: 10.1093/hmg/3.4.569. 2. Uen, Y.-H. et al. (2015) ‘Analysis of differentially expressed novel post-translational modifications of plasma apolipoprotein E in Taiwanese females with breast cancer’, Journal of Proteomics, 126, pp. 252–262. doi: 10.1016/j.jprot.2015.05.038. 3. Mahley, R. W. (2016) ‘Apolipoprotein E: from cardiovascular disease to neurodegenerative disorders’, Journal of Molecular Medicine, 94(7), pp. 739–746. doi: 10.1007/s00109-016-1427-y. |