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Human apolipoprotein E. The complete amino acid sequence
Open accessAbstract
The amino acid sequence of human apolipoprotein E (apo-E) has been determined.Apo-E2, one of the major isoforms of apolipoprotein E, is a polypeptide of 299 amino acids having a calculated molecular weight of 34,145.The isoform apo-E3 differs from apo-E2 by a single amino acid substitution of arginine for cysteine at residue 158 (italicized).The sequqnce of apo-E2 is:HzN-Lys-Val-Glu-Gln-Ala-Val-Glu-Thr-Glu-Pro-Glu-Pro-Glu-Leu-Arg-Gln-Gln-Thr-Glu-Trp-Gln-Ser-Gly-Gln-Arg-Trp-Glu-Leu-Ala-Leu-Gly-Arg-Phe-Trp-Asp-Tyr-Leu-Arg-Trp-Val-Gln-%-Leu-Ser-Glu-Gln-Val-Gln-Glu-Glu-Leu-Leu-Ser-Ser-Gln-Val-Thr-Gln-Glu-Leu-Arg-Ala-Leu-Met-Asp-Glu-Thr-Met-Lys-Glu-Leu-Lys-Ala-Tyr-Lys-Ser-Glu-Leu-Glu-Glu-Gln-Leu-Thr-Pro-Val-Ala-Glu-Glu-Thr-Arg-Ala-Arg-Leu-Ser-Lys-Glu-Leu-Gln-Ala-Ala-Gln-Ala-Arg-Leu-Gly-Ala-Asp-Met-Glu-Asp-Val-Cys-Gly-Arg-Leu-Val-Gln-Tyr-Arg-Gly-Glu-Val-Gln-Ala-Met-Leu-Gly-Gln-Ser-Thr-Glu-Glu-Leu-Arg-Val-Arg-Leu-Ala-Ser-His-Leu-Arg-Lys-Leu-Arg-Lys-Arg-Leu-Leu-Arg-Asp-Ala-Asp-Asp-Leu-Gln-Lys-Cys-Leu-Ala-Val-Tyr-Gln-Ala-Gly-Ala-Arg-Glu-Gly-Ala-Glu-Arg-Gly-Leu-Ser-Ala-Ile-Arg-Glu-Arg-Leu-Gly-Pro-Leu-Val-Glu-Gln-Gly-Arg-Val-Arg-Ala-Ala-%-Val-Gly-Ser-Leu-Ala-Gly-Gln-Pro-Leu-Gln-Glu-Arg-Ala-Gln-Ala-Trp-Gly-Glu-Arg-Leu-Arg-Ala-Arg
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In the citing paper
“The most common has a mutation of 158 Arg --Cys (13), but mutations of 145 Arg -* Cys (14) and 146 Lys --Gln (6) have also been reported in individuals with type III hyperlipoproteinemia.”
From Apolipoprotein E2-Christchurch (136 Arg----Ser). New variant of human apolipoprotein E in a patient with type III hyperlipoproteinemia. (1987) · cites this paper as [13]
In the citing paper
“Three variants ofapo E2 have been described.Each ofthese differs from apo E3 by a single amino acid substitution (6, 12- 14).”
From Apolipoprotein E2-Christchurch (136 Arg----Ser). New variant of human apolipoprotein E in a patient with type III hyperlipoproteinemia. (1987) · cites this paper as [13]
In the citing paper
“Secondary structure predictions (54,55) suggest that position 136 is part of an a-helix that extends between residues 130 and 150 (13,24), encompassing the receptor-binding domain from 140 to 150 (22).”
From Apolipoprotein E2-Christchurch (136 Arg----Ser). New variant of human apolipoprotein E in a patient with type III hyperlipoproteinemia. (1987) · cites this paper as [13]
In the citing paper
“The mature apoE protein consists of 299 amino acids and an 18amino acid signal peptide is removed post-translationally [17,28].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [17]
In the citing paper
“The low density lipoprotein (LDL) receptor binding region is situated in helix four between amino acids 136 and 150 [17,28].”
From Plasma levels of apolipoprotein E, APOE genotype and risk of dementia and ischemic heart disease: A review (2016) · cites this paper as [17]
In the citing paper
“Both codons 112 and 158 showed the amino acid cysteine (Cys) (shown in Fig. 3), which indicated that the isoform of apoE was apoE2/E2 [8, 9].”
In the citing paper
“In normal apoE3, peptide T15 is a 15-residue peptide encompassing residues 120-134 (23).”
From Apolipoprotein E3-Leiden contains a seven-amino acid insertion that is a tandem repeat of residues 121–127 (1989) · cites this paper as [23]
In the citing paper
“This profile is similar to that for normal apoE3 (17, 23) except for the presence of a new peak (CBX) eluting at the column volume.”
From Apolipoprotein E3-Leiden contains a seven-amino acid insertion that is a tandem repeat of residues 121–127 (1989) · cites this paper as [23]
Citations
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Apolipoprotein E: Cholesterol Transport Protein with Expanding Role in Cell Biology
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Self-citation
Metadata
- Authors
- Rall, S. C., Weisgraber, K. H., & Mahley, R. W.
- ORCID
- Mahley, R W
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1982-04
- Volume
- 257
- Issue
- 8
- Pages
- 4171-4178
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1736154854
- Cited by
- 741
- References
- 38
- Citations by year
- 2026: 7 · 2025: 13 · 2024: 9 · 2023: 13 · 2022: 16 · 2021: 17 · 2020: 12 · 2019: 14 · 2018: 11 · 2017: 7 · 2016: 10 · 2015: 11 · 2014: 21 · 2013: 19 · 2012: 10
- FWCI
- 40.41
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipid metabolism and disorders
- Keywords
- apolipoprotein E, amino acid sequence, apolipoprotein E isoforms, single amino acid substitution, protein sequences
- MeSH terms
- Amino Acid Sequence, Apolipoproteins, Apolipoproteins E, Carboxypeptidases, Cyanogen Bromide, Humans, Lipoproteins, LDL, Models, Molecular, Molecular Weight, Peptide Fragments, Protein Conformation, Carboxypeptidases A
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