Human apolipoprotein E. The complete amino acid sequence

Rall, S C; Weisgraber, K H; Mahley, R W

doi:10.1016/s0021-9258(18)34702-1

Cited by 741Alzheimer's disease research and treatmentsLipoproteins and Cardiovascular HealthLipid metabolism and disorders

Human apolipoprotein E. The complete amino acid sequence

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Rall, S C, Weisgraber, K H, Mahley, R W·1982·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)34702-1

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Abstract

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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The most common apo E2 has a 158 Arg-to-Cys mutation, while 145 Arg-to-Cys and 146 Lys-to-Gln mutations have also been reported in type III hyperlipoproteinemia.
“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]
Three apo E2 variants have been described, each differing from apo E3 by a single amino acid substitution.
“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]
Secondary structure predictions suggest that position 136 lies in an alpha-helix from residues 130 to 150, which includes the receptor-binding domain from 140 to 150.
“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]
The mature apoE protein consists of 299 amino acids, and an 18-amino acid signal peptide is removed post-translationally.
“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]
The LDL receptor binding region is situated in helix four between amino acids 136 and 150.
“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]

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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)
DOI: 10.1016/s0021-9258(18)34702-1
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 14090 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Surgery › 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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Human apolipoprotein E. The complete amino acid sequence

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