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Apolipoprotein E (Apo-E)

 APOE_HUMAN              Reviewed;         317 AA.
P02649; B2RC15; C0JYY5; Q9P2S4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
13-FEB-2019, entry version 239.
RecName: Full=Apolipoprotein E;
Short=Apo-E;
Flags: Precursor;
Name=APOE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ALLELE APOE*3).
PubMed=6325438;
Zannis V.I., McPherson J., Goldberger G., Karathanasis S.K.,
Breslow J.L.;
"Synthesis, intracellular processing, and signal peptide of human
apolipoprotein E.";
J. Biol. Chem. 259:5495-5499(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS THR-117 AND PRO-170.
PubMed=6327682;
McLean J.W., Elshourbagy N.A., Chang D.J., Mahley R.W., Taylor J.M.;
"Human apolipoprotein E mRNA. cDNA cloning and nucleotide sequencing
of a new variant.";
J. Biol. Chem. 259:6498-6504(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*4), AND VARIANT AD2
ARG-130.
PubMed=2987927; DOI=10.1073/pnas.82.10.3445;
Paik Y.-K., Chang D.J., Reardon C.A., Davies G.E., Mahley R.W.,
Taylor J.M.;
"Nucleotide sequence and structure of the human apolipoprotein E
gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:3445-3449(1985).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*2), AND VARIANT
CYS-176.
PubMed=3243553; DOI=10.1016/0888-7543(88)90130-9;
Emi M., Wu L.L., Robertson M.A., Myers R.L., Hegele R.A.,
Williams R.R., White R., Lalouel J.-M.;
"Genotyping and sequence analysis of apolipoprotein E isoforms.";
Genomics 3:373-379(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*3).
PubMed=10520737; DOI=10.3109/10425179809086433;
Freitas E.M., Zhang W.J., Lalonde J.P., Tay G.K., Gaudieri S.,
Ashworth L.K., Van Bockxmeer F.M., Dawkins R.L.;
"Sequencing of 42kb of the APO E-C2 gene cluster reveals a new gene:
PEREC1.";
DNA Seq. 9:89-100(1998).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*3), AND VARIANTS
PRO-46; ARG-130; CYS-163 AND CYS-176.
PubMed=11042151; DOI=10.1101/gr.146900;
Nickerson D.A., Taylor S.L., Fullerton S.M., Weiss K.M., Clark A.G.,
Stengard J.H., Salomaa V., Boerwinkle E., Sing C.F.;
"Sequence diversity and large-scale typing of SNPs in the human
apolipoprotein E gene.";
Genome Res. 10:1532-1545(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE APOE*3).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE APOE*3).
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE APOE*3).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-78, AND VARIANT HIS-64.
TISSUE=Blood;
Imura T., Kimura H., Kawasaki M.;
"A new apolipoprotein E variant (Gln46-->His).";
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 99-317 (ALLELE APOE*3).
PubMed=6897404;
Breslow J.L., McPherson J., Nussbaum A.L., Williams H.W.,
Lofquist-Kahl F., Karathanasis S.K., Zannis V.I.;
"Identification and DNA sequence of a human apolipoprotein E cDNA
clone.";
J. Biol. Chem. 257:14639-14641(1982).
[12]
ERRATUM.
Breslow J.L., McPherson J., Nussbaum A.L., Williams H.W.,
Lofquist-Kahl F., Karathanasis S.K., Zannis V.I.;
J. Biol. Chem. 258:11422-11422(1983).
[13]
PROTEIN SEQUENCE OF 19-317 (ALLELE APOE*2).
PubMed=7068630;
Rall S.C. Jr., Weisgraber K.H., Mahley R.W.;
"Human apolipoprotein E. The complete amino acid sequence.";
J. Biol. Chem. 257:4171-4178(1982).
[14]
FUNCTION IN LIPOPROTEINS CONVERSION.
PubMed=6860692;
Marcel Y.L., Vezina C., Milne R.W.;
"Cholesteryl ester and apolipoprotein E transfer between human high
density lipoproteins and chylomicrons.";
Biochim. Biophys. Acta 750:411-417(1983).
[15]
HEPARIN-BINDING SITES.
PubMed=3947350; DOI=10.1016/S0006-291X(86)80489-2;
Cardin A.D., Hirose N., Blankenship D.T., Jackson R.L.,
Harmony J.A.K., Sparrow D.A., Sparrow J.T.;
"Binding of a high reactive heparin to human apolipoprotein E:
identification of two heparin-binding domains.";
Biochem. Biophys. Res. Commun. 134:783-789(1986).
[16]
TISSUE SPECIFICITY.
PubMed=3115992;
Pitas R.E., Boyles J.K., Lee S.H., Hui D., Weisgraber K.H.;
"Lipoproteins and their receptors in the central nervous system.
Characterization of the lipoproteins in cerebrospinal fluid and
identification of apolipoprotein B,E(LDL) receptors in the brain.";
J. Biol. Chem. 262:14352-14360(1987).
[17]
CHARACTERIZATION OF VARIANTS SER-154 AND PRO-170, AND MUTAGENESIS OF
SER-157; HIS-158; LYS-161; LEU-162; LEU-167 AND ARG-168.
PubMed=2831187;
Lalazar A., Weisgraber K.H., Rall S.C. Jr., Giladi H.,
Innerarity T.L., Levanon A.Z., Boyles J.K., Amit B., Gorecki M.,
Mahley R.W.;
"Site-specific mutagenesis of human apolipoprotein E. Receptor binding
activity of variants with single amino acid substitutions.";
J. Biol. Chem. 263:3542-3545(1988).
[18]
SUBCELLULAR LOCATION, GLYCOSYLATION AT THR-212, AND MUTAGENESIS OF
THR-212.
PubMed=2498325;
Wernette-Hammond M.E., Lauer S.J., Corsini A., Walker D., Taylor J.M.,
Rall S.C. Jr.;
"Glycosylation of human apolipoprotein E. The carbohydrate attachment
site is threonine 194.";
J. Biol. Chem. 264:9094-9101(1989).
[19]
FUNCTION IN VLDL CLEARANCE.
PubMed=2762297;
Kowal R.C., Herz J., Goldstein J.L., Esser V., Brown M.S.;
"Low density lipoprotein receptor-related protein mediates uptake of
cholesteryl esters derived from apoprotein E-enriched lipoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 86:5810-5814(1989).
[20]
REGION, AND CHARACTERIZATION OF VARIANT ARG-130 AND ARG-176.
PubMed=2280190;
Weisgraber K.H.;
"Apolipoprotein E distribution among human plasma lipoproteins: role
of the cysteine-arginine interchange at residue 112.";
J. Lipid Res. 31:1503-1511(1990).
[21]
FUNCTION IN CHYLOMICRONS CLEARANCE, AND SUBCELLULAR LOCATION.
PubMed=1911868;
Arnon R., Sehayek E., Vogel T., Eisenberg S.;
"Effects of exogenous apo E-3 and of cholesterol-enriched meals on the
cellular metabolism of human chylomicrons and their remnants.";
Biochim. Biophys. Acta 1085:336-342(1991).
[22]
FUNCTION IN VLDL AND IDL CLEARANCE.
PubMed=1917954;
Sehayek E., Eisenberg S.;
"Mechanisms of inhibition by apolipoprotein C of apolipoprotein E-
dependent cellular metabolism of human triglyceride-rich lipoproteins
through the low density lipoprotein receptor pathway.";
J. Biol. Chem. 266:18259-18267(1991).
[23]
SUBUNIT, SUBCELLULAR LOCATION, AND REGION.
PubMed=8340399;
Westerlund J.A., Weisgraber K.H.;
"Discrete carboxyl-terminal segments of apolipoprotein E mediate
lipoprotein association and protein oligomerization.";
J. Biol. Chem. 268:15745-15750(1993).
[24]
INTERACTION WITH APP/A4 AMYLOID-BETA PEPTIDE, AND CHARACTERIZATION OF
VARIANT AD2 ARG-130.
PubMed=8367470;
Strittmatter W.J., Weisgraber K.H., Huang D.Y., Dong L.M.,
Salvesen G.S., Pericak-Vance M., Schmechel D., Saunders A.M.,
Goldgaber D., Roses A.D.;
"Binding of human apolipoprotein E to synthetic amyloid beta peptide:
isoform-specific effects and implications for late-onset Alzheimer
disease.";
Proc. Natl. Acad. Sci. U.S.A. 90:8098-8102(1993).
[25]
INTERACTION WITH MAP2, AND CHARACTERIZATION OF VARIANT AD2 ARG-130.
PubMed=7891887;
Huang D.Y., Goedert M., Jakes R., Weisgraber K.H., Garner C.C.,
Saunders A.M., Pericak-Vance M.A., Schmechel D.E., Roses A.D.,
Strittmatter W.J.;
"Isoform-specific interactions of apolipoprotein E with the
microtubule-associated protein MAP2c: implications for Alzheimer's
disease.";
Neurosci. Lett. 182:55-58(1994).
[26]
INTERACTION WITH MAPT, AND CHARACTERIZATION OF VARIANT AD2 ARG-130.
PubMed=7972031;
Strittmatter W.J., Saunders A.M., Goedert M., Weisgraber K.H.,
Dong L.M., Jakes R., Huang D.Y., Pericak-Vance M., Schmechel D.,
Roses A.D.;
"Isoform-specific interactions of apolipoprotein E with microtubule-
associated protein tau: implications for Alzheimer disease.";
Proc. Natl. Acad. Sci. U.S.A. 91:11183-11186(1994).
[27]
FUNCTION, AND LRP2-BINDING.
PubMed=7768901; DOI=10.1074/jbc.270.22.13070;
Kounnas M.Z., Loukinova E.B., Stefansson S., Harmony J.A.K.,
Brewer B.H., Strickland D.K., Argraves W.S.;
"Identification of glycoprotein 330 as an endocytic receptor for
apolipoprotein J/clusterin.";
J. Biol. Chem. 270:13070-13075(1995).
[28]
FUNCTION IN NEURITE OUTGROWTH, LRP-BINDING, AND CHARACTERIZATION OF
VARIANT AD2 ARG-130.
PubMed=8939961;
Fagan A.M., Bu G., Sun Y., Daugherty A., Holtzman D.M.;
"Apolipoprotein E-containing high density lipoprotein promotes neurite
outgrowth and is a ligand for the low density lipoprotein receptor-
related protein.";
J. Biol. Chem. 271:30121-30125(1996).
[29]
FUNCTION IN HDL CLEARANCE, AND HEPARAN SULFATE-BINDING.
PubMed=9395455;
Ji Z.S., Dichek H.L., Miranda R.D., Mahley R.W.;
"Heparan sulfate proteoglycans participate in hepatic lipase and
apolipoprotein E-mediated binding and uptake of plasma lipoproteins,
including high density lipoproteins.";
J. Biol. Chem. 272:31285-31292(1997).
[30]
FUNCTION, HEPARAN-SULFATE-BINDING, AND SUBCELLULAR LOCATION.
PubMed=9488694;
Burgess J.W., Gould D.R., Marcel Y.L.;
"The HepG2 extracellular matrix contains separate heparinase- and
lipid-releasable pools of ApoE. Implications for hepatic lipoprotein
metabolism.";
J. Biol. Chem. 273:5645-5654(1998).
[31]
TISSUE SPECIFICITY.
PubMed=10027417; DOI=10.1016/S0002-9440(10)65305-9;
Xu P.T., Gilbert J.R., Qiu H.L., Ervin J., Rothrock-Christian T.R.,
Hulette C., Schmechel D.E.;
"Specific regional transcription of apolipoprotein E in human brain
neurons.";
Am. J. Pathol. 154:601-611(1999).
[32]
GLYCATION AT LYS-93, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10452964; DOI=10.1016/S0925-4439(99)00047-2;
Shuvaev V.V., Fujii J., Kawasaki Y., Itoh H., Hamaoka R., Barbier A.,
Ziegler O., Siest G., Taniguchi N.;
"Glycation of apolipoprotein E impairs its binding to heparin:
identification of the major glycation site.";
Biochim. Biophys. Acta 1454:296-308(1999).
[33]
PTM, AND CHARACTERIZATION OF VARIANT AD2 ARG-130.
PubMed=11447277; DOI=10.1073/pnas.151254698;
Huang Y., Liu X.Q., Wyss-Coray T., Brecht W.J., Sanan D.A.,
Mahley R.W.;
"Apolipoprotein E fragments present in Alzheimer's disease brains
induce neurofibrillary tangle-like intracellular inclusions in
neurons.";
Proc. Natl. Acad. Sci. U.S.A. 98:8838-8843(2001).
[34]
FUNCTION, LRP8-BINDING, AND CHARACTERIZATION OF VARIANT CYS-176.
PubMed=12950167; DOI=10.1021/bi027093c;
Li X., Kypreos K., Zanni E.E., Zannis V.;
"Domains of apoE required for binding to apoE receptor 2 and to
phospholipids: implications for the functions of apoE in the brain.";
Biochemistry 42:10406-10417(2003).
[35]
FUNCTION IN REVERSE CHOLESTEROL TRANSPORT, AND INTERACTION WITH ABCA1.
PubMed=14754908; DOI=10.1194/jlr.M300418-JLR200;
Krimbou L., Denis M., Haidar B., Carrier M., Marcil M., Genest J. Jr.;
"Molecular interactions between apoE and ABCA1: impact on apoE
lipidation.";
J. Lipid Res. 45:839-848(2004).
[36]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-212; THR-307 AND SER-308,
AND STRUCTURE OF CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[37]
FUNCTION, LRP1-BINDING, AND REGION.
PubMed=20030366; DOI=10.1021/bi9017208;
Guttman M., Prieto J.H., Croy J.E., Komives E.A.;
"Decoding of lipoprotein-receptor interactions: properties of ligand
binding modules governing interactions with apolipoprotein E.";
Biochemistry 49:1207-1216(2010).
[38]
GLYCOSYLATION AT SER-308.
PubMed=20511397; DOI=10.1074/mcp.M900430-MCP200;
Lee Y., Kockx M., Raftery M.J., Jessup W., Griffith R.,
Kritharides L.;
"Glycosylation and sialylation of macrophage-derived human
apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence
for a novel site of glycosylation on Ser290.";
Mol. Cell. Proteomics 9:1968-1981(2010).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[41]
FUNCTION IN LIPOPROTEIN CLEARANCE, AND HEPARAN-SULFATE PROTEOGLYCANS
BINDING.
PubMed=23676495; DOI=10.1172/JCI67398;
Gonzales J.C., Gordts P.L., Foley E.M., Esko J.D.;
"Apolipoproteins E and AV mediate lipoprotein clearance by hepatic
proteoglycans.";
J. Clin. Invest. 123:2742-2751(2013).
[42]
GLYCOSYLATION AT THR-26; THR-36 AND SER-314, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=23234360; DOI=10.1021/pr300963h;
Halim A., Ruetschi U., Larson G., Nilsson J.;
"LC-MS/MS characterization of O-glycosylation sites and glycan
structures of human cerebrospinal fluid glycoproteins.";
J. Proteome Res. 12:573-584(2013).
[43]
FUNCTION IN CHOLESTEROL EFFLUX, AND INTERACTION WITH APP/A4
AMYLOID-BETA PEPTIDE.
PubMed=23620513; DOI=10.1073/pnas.1220484110;
Verghese P.B., Castellano J.M., Garai K., Wang Y., Jiang H., Shah A.,
Bu G., Frieden C., Holtzman D.M.;
"ApoE influences amyloid-beta (Abeta) clearance despite minimal
apoE/Abeta association in physiological conditions.";
Proc. Natl. Acad. Sci. U.S.A. 110:E1807-E1816(2013).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[45]
PHOSPHORYLATION AT SER-147.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[46]
FUNCTION IN APP TRANSCRIPTION, AND CHARACTERIZATION OF VARIANT AD2
ARG-130.
PubMed=28111074; DOI=10.1016/j.cell.2016.12.044;
Huang Y.A., Zhou B., Wernig M., Suedhof T.C.;
"ApoE2, ApoE3, and ApoE4 Differentially Stimulate APP Transcription
and Abeta Secretion.";
Cell 168:427-441(2017).
[47] {ECO:0000244|PDB:1LPE}
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 41-184, FUNCTION, AND
REGION.
PubMed=2063194; DOI=10.1126/science.2063194;
Wilson C., Wardell M.R., Weisgraber K.H., Mahley R.W., Agard D.A.;
"Three-dimensional structure of the LDL receptor-binding domain of
human apolipoprotein E.";
Science 252:1817-1822(1991).
[48] {ECO:0000244|PDB:1LE4}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 41-184 OF VARIANT AD2
ARG-130, CHARACTERIZATION OF VARIANT AD2 ARG-130, MUTAGENESIS OF
ARG-79 AND GLU-127, AND REGION.
PubMed=8071364;
Dong L.M., Wilson C., Wardell M.R., Simmons T., Mahley R.W.,
Weisgraber K.H., Agard D.A.;
"Human apolipoprotein E. Role of arginine 61 in mediating the
lipoprotein preferences of the E3 and E4 isoforms.";
J. Biol. Chem. 269:22358-22365(1994).
[49] {ECO:0000244|PDB:1LE2}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 41-184 OF VARIANT CYS-176,
AND CHARACTERIZATION OF VARIANT CYS-176.
PubMed=7994571; DOI=10.1016/S0969-2126(00)00072-1;
Wilson C., Mau T., Weisgraber K.H., Wardell M.R., Mahley R.W.,
Agard D.A.;
"Salt bridge relay triggers defective LDL receptor binding by a mutant
apolipoprotein.";
Structure 2:713-718(1994).
[50] {ECO:0000244|PDB:1NFN, ECO:0000244|PDB:1NFO}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-209 OF VARIANT CYS-176,
MUTAGENESIS OF ASP-172, CHARACTERIZATION OF VARIANT CYS-176, FUNCTION,
AND LDLR-BINDING.
PubMed=8756331; DOI=10.1038/nsb0896-718;
Dong L.-M., Parkin S., Trakhanov S.D., Rupp B., Simmons T.,
Arnold K.S., Newhouse Y.M., Innerarity T.L., Weisgraber K.H.;
"Novel mechanism for defective receptor binding of apolipoprotein E2
in type III hyperlipoproteinemia.";
Nat. Struct. Biol. 3:718-722(1996).
[51] {ECO:0000244|PDB:1BZ4, ECO:0000244|PDB:1OR2, ECO:0000244|PDB:1OR3}
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-183.
PubMed=10850798; DOI=10.1110/ps.9.5.886;
Segelke B.W., Forstner M., Knapp M., Trakhanov S.D., Parkin S.,
Newhouse Y.M., Bellamy H.D., Weisgraber K.H., Rupp B.;
"Conformational flexibility in the apolipoprotein E amino-terminal
domain structure determined from three new crystal forms: implications
for lipid binding.";
Protein Sci. 9:886-897(2000).
[52] {ECO:0000244|PDB:1B68}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 19-209 OF VARIANT AD2
ARG-130.
PubMed=11258893; DOI=10.1021/bi002417n;
Dong J., Peters-Libeu C.A., Weisgraber K.H., Segelke B.W., Rupp B.,
Capila I., Hernaiz M.J., LeBrun L.A., Linhardt R.J.;
"Interaction of the N-terminal domain of apolipoprotein E4 with
heparin.";
Biochemistry 40:2826-2834(2001).
[53] {ECO:0000244|PDB:2KNY}
STRUCTURE BY NMR OF 147-167 IN COMPLEX WITH LRP1, FUNCTION, AND
LRP1-BINDING.
PubMed=20303980; DOI=10.1016/j.jmb.2010.03.022;
Guttman M., Prieto J.H., Handel T.M., Domaille P.J., Komives E.A.;
"Structure of the minimal interface between ApoE and LRP.";
J. Mol. Biol. 398:306-319(2010).
[54]
VARIANT HLPP3 262-GLU-GLU-263 DELINS LYS-LYS.
PubMed=2738044;
Maeda H., Nakamura H., Kobori S., Okada M., Mori H., Niki H.,
Ogura T., Hiraga S.;
"Identification of human apolipoprotein E variant gene: apolipoprotein
E7 (Glu244,245----Lys244,245).";
J. Biochem. 105:51-54(1989).
[55]
VARIANT LYS-21.
PubMed=2760009; DOI=10.1093/oxfordjournals.jbchem.a122692;
Maeda H., Nakamura H., Kobori S., Okada M., Niki H., Ogura T.,
Hiraga S.;
"Molecular cloning of a human apolipoprotein E variant: E5 (Glu-
3-->Lys).";
J. Biochem. 105:491-493(1989).
[56]
VARIANTS HLPP3 ARG-130 AND GLU-VAL-GLN-ALA-MET-LEU-GLY-145 INS.
PubMed=2556398;
Wardell M.R., Weisgraber K.H., Havekes L.M., Rall S.C. Jr.;
"Apolipoprotein E3-Leiden contains a seven-amino acid insertion that
is a tandem repeat of residues 121-127.";
J. Biol. Chem. 264:21205-21210(1989).
[57]
VARIANT HLPP3 HIS-163.
PubMed=2101409;
Suehiro T., Yoshida K., Yamano T., Ohno F.;
"Identification and characterization of a new variant of
apolipoprotein E (apo E-Kochi).";
Jpn. J. Med. 29:587-594(1990).
[58]
VARIANT CYS-246.
PubMed=2341812;
Wardell M.R., Rall S.C. Jr., Brennan S.O., Nye E.R., George P.M.,
Janus E.D., Weisgraber K.H.;
"Apolipoprotein E2-Dunedin (228 Arg replaced by Cys): an
apolipoprotein E2 variant with normal receptor-binding activity.";
J. Lipid Res. 31:535-543(1990).
[59]
VARIANTS HLPP3 LYS-31 AND CYS-163.
PubMed=1674745;
Lohse P., Mann W.A., Stein E.A., Brewer H.B. Jr.;
"Apolipoprotein E-4 Philadelphia (Glu-13-->Lys,Arg-145-->Cys).
Homozygosity for two rare point mutations in the apolipoprotein E gene
combined with severe type III hyperlipoproteinemia.";
J. Biol. Chem. 266:10479-10484(1991).
[60]
VARIANT APOE5 FRENCH-CANADIAN LYS-31.
PubMed=1713245;
Mailly F., Xu C.F., Xhignesse M., Lussier-Cacan S., Talmud P.J.,
Davignon J., Humphries S.E., Nestruck A.C.;
"Characterization of a new apolipoprotein E5 variant detected in two
French-Canadian subjects.";
J. Lipid Res. 32:613-620(1991).
[61]
CHARACTERIZATION OF VARIANT LYS-21, FUNCTION, AND LDLR-BINDING.
PubMed=1530612;
Dong L.M., Yamamura T., Tajima S., Yamamoto A.;
"Site-directed mutagenesis of an apolipoprotein E mutant, apo
E5(Glu3----Lys) and its binding to low density lipoprotein
receptors.";
Biochem. Biophys. Res. Commun. 187:1180-1186(1992).
[62]
VARIANT HLPP3 228-TRP--HIS-317 DEL.
PubMed=1361196;
Lohse P., Brewer H.B. III, Meng M.S., Skarlatos S.I., LaRosa J.C.,
Brewer H.B. Jr.;
"Familial apolipoprotein E deficiency and type III
hyperlipoproteinemia due to a premature stop codon in the
apolipoprotein E gene.";
J. Lipid Res. 33:1583-1590(1992).
[63]
VARIANTS GLU-254; GLY-269; GLU-270; HIS-292 AND ARG-314.
PubMed=8488843;
van den Maagdenberg A.M.J.M., Weng W., de Bruijn I.H., de Knijff P.,
Funke H., Smelt A.H.M., Leuven J.A.G., van 't Hooft F.M., Assmann G.,
Hofker M.H., Havekes L.M., Frants R.R.;
"Characterization of five new mutants in the carboxyl-terminal domain
of human apolipoprotein E: no cosegregation with severe
hyperlipidemia.";
Am. J. Hum. Genet. 52:937-946(1993).
[64]
VARIANTS LYS-99 AND ARG-130.
PubMed=8125051;
Ruzicka V., Maerz W., Russ A., Fisher E., Mondorf W., Gross W.;
"Characterization of the gene for apolipoprotein E5-Frankfurt
(Gln81->Lys, Cys112->Arg) by polymerase chain reaction, restriction
isotyping, and temperature gradient gel electrophoresis.";
Electrophoresis 14:1032-1037(1993).
[65]
CHARACTERIZATION OF VARIANT GLU-VAL-GLN-ALA-MET-LEU-GLY-145 INS.
PubMed=8468528;
Fazio S., Horie Y., Weisgraber K.H., Havekes L.M., Rall S.C. Jr.;
"Preferential association of apolipoprotein E Leiden with very low
density lipoproteins of human plasma.";
J. Lipid Res. 34:447-453(1993).
[66]
INVOLVEMENT IN AD2, AND VARIANT AD2 ARG-130.
PubMed=8346443; DOI=10.1126/science.8346443;
Corder E.H., Saunders A.M., Strittmatter W.J., Schmechel D.E.,
Gaskell P.C., Small G.W., Roses A.D., Haines J.L., Pericak-Vance M.A.;
"Gene dose of apolipoprotein E type 4 allele and the risk of
Alzheimer's disease in late onset families.";
Science 261:921-923(1993).
[67]
VARIANTS HLPP3 ARG-130; ASP-145; SER-154; CYS-160 AND CYS-176.
PubMed=8287539;
Richard P., Thomas G., de Zulueta M.P., de Gennes J.-L., Thomas M.,
Cassaigne A., Bereziat G., Iron A.;
"Common and rare genotypes of human apolipoprotein E determined by
specific restriction profiles of polymerase chain reaction-amplified
DNA.";
Clin. Chem. 40:24-29(1994).
[68]
VARIANT HLPP3 GLU-164, CHARACTERIZATION OF VARIANT HLPP3 GLU-164 AND
CYS-176, FUNCTION, LDLR-BINDING, AND HEPARIN-BINDING.
PubMed=7635945; DOI=10.1172/JCI118096;
Mann W.A., Lohse P., Gregg R.E., Ronan R., Hoeg J.M., Zech L.A.,
Brewer H.B. Jr.;
"Dominant expression of type III hyperlipoproteinemia.
Pathophysiological insights derived from the structural and kinetic
characteristics of ApoE-1 (Lys146-->Glu).";
J. Clin. Invest. 96:1100-1107(1995).
[69]
VARIANT GLN-242.
PubMed=8664327;
Moriyama K., Sasaki J., Takada Y., Arakawa F., Matsunaga A., Ito Y.,
Arakawa K.;
"Characterization of a novel variant of apolipoprotein E, E2 Fukuoka
(Arg-224 --> Gln) in a hyperlipidemic patient with xanthomatosis.";
Biochim. Biophys. Acta 1301:185-190(1996).
[70]
VARIANT LPG PRO-163.
PubMed=9176854;
Oikawa S., Matsunaga A., Saito T., Sato H., Seki T., Hoshi K.,
Hayasaka K., Kotake H., Midorikawa H., Sekikawa A., Hara S., Abe K.,
Toyota T., Jingami H., Nakamura H., Sasaki J.;
"Apolipoprotein E Sendai (arginine 145-->proline): a new variant
associated with lipoprotein glomerulopathy.";
J. Am. Soc. Nephrol. 8:820-823(1997).
[71]
VARIANTS ARG-130 AND GLY-269.
PubMed=9360638; DOI=10.1016/S1383-5726(97)00009-5;
Kang A.K., Jenkins D.J.A., Wolever T.M.S., Huff M.W., Maguire G.F.,
Connelly P.W., Hegele R.A.;
"Apolipoprotein E R112; R251G: a carboxy-terminal variant found in
patients with hyperlipidemia and coronary heart disease.";
Mutat. Res. 382:57-65(1997).
[72]
VARIANT LPG CYS-43.
PubMed=10432380; DOI=10.1046/j.1523-1755.1999.00572.x;
Matsunaga A., Sasaki J., Komatsu T., Kanatsu K., Tsuji E.,
Moriyama K., Koga T., Arakawa K., Oikawa S., Saito T., Kita T.,
Doi T.;
"A novel apolipoprotein E mutation, E2 (Arg25Cys), in lipoprotein
glomerulopathy.";
Kidney Int. 56:421-427(1999).
[73]
CHARACTERIZATION OF VARIANT LPG PRO-163, AND CHARACTERIZATION OF
VARIANT AD2 ARG-130.
PubMed=10903326; DOI=10.1074/jbc.M005906200;
Ishigaki Y., Oikawa S., Suzuki T., Usui S., Magoori K., Kim D.H.,
Suzuki H., Sasaki J., Sasano H., Okazaki M., Toyota T., Saito T.,
Yamamoto T.T.;
"Virus-mediated transduction of apolipoprotein E (ApoE)-sendai
develops lipoprotein glomerulopathy in ApoE-deficient mice.";
J. Biol. Chem. 275:31269-31273(2000).
[74]
VARIANT SBHD LEU-167 DEL.
PubMed=11095479; DOI=10.1210/jcem.85.11.6981;
Nguyen T.T., Kruckeberg K.E., O'Brien J.F., Ji Z.-S., Karnes P.S.,
Crotty T.B., Hay I.D., Mahley R.W., O'Brien T.;
"Familial splenomegaly: macrophage hypercatabolism of lipoproteins
associated with apolipoprotein E mutation [apolipoprotein E (delta149
Leu)].";
J. Clin. Endocrinol. Metab. 85:4354-4358(2000).
[75]
VARIANT VAL-124.
PubMed=12864777; DOI=10.1046/j.1365-2362.2003.01180.x;
Miserez A.R., Scharnagl H., Muller P.Y., Mirsaidi R., Stahelin H.B.,
Monsch A., Marz W., Hoffmann M.M.;
"Apolipoprotein E3Basel: new insights into a highly conserved protein
region.";
Eur. J. Clin. Invest. 33:677-685(2003).
[76]
VARIANTS ARG-130 AND CYS-176.
PubMed=12966036; DOI=10.1093/hmg/ddg314;
Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S.,
Alvin G.B., Das K., Gilliam T.C.;
"Association of extreme blood lipid profile phenotypic variation with
11 reverse cholesterol transport genes and 10 non-genetic
cardiovascular disease risk factors.";
Hum. Mol. Genet. 12:2733-2743(2003).
[77]
VARIANT SBHD LEU-167 DEL.
PubMed=16094309; DOI=10.1038/sj.ejhg.5201480;
Faivre L., Saugier-Veber P., Pais de Barros J.-P., Verges B.,
Couret B., Lorcerie B., Thauvin C., Charbonnier F., Huet F.,
Gambert P., Frebourg T., Duvillard L.;
"Variable expressivity of the clinical and biochemical phenotype
associated with the apolipoprotein E p.Leu149del mutation.";
Eur. J. Hum. Genet. 13:1186-1191(2005).
[78]
VARIANT LPG CYS-43.
PubMed=18077821; DOI=10.1056/NEJMc072088;
Rovin B.H., Roncone D., McKinley A., Nadasdy T., Korbet S.M.,
Schwartz M.M.;
"APOE Kyoto mutation in European Americans with lipoprotein
glomerulopathy.";
N. Engl. J. Med. 357:2522-2524(2007).
[79]
VARIANT HIS-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22028381; DOI=10.1093/jmcb/mjr024;
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
Lin X., Zeng R., Wu J.R.;
"Quantitative detection of single amino acid polymorphisms by targeted
proteomics.";
J. Mol. Cell Biol. 3:309-315(2011).
[80]
VARIANT HLPP3 SER-154, AND VARIANT LEU-167 DEL.
PubMed=22481068; DOI=10.1016/j.atherosclerosis.2012.03.011;
Solanas-Barca M., de Castro-Oros I., Mateo-Gallego R., Cofan M.,
Plana N., Puzo J., Burillo E., Martin-Fuentes P., Ros E., Masana L.,
Pocovi M., Civeira F., Cenarro A.;
"Apolipoprotein E gene mutations in subjects with mixed hyperlipidemia
and a clinical diagnosis of familial combined hyperlipidemia.";
Atherosclerosis 222:449-455(2012).
[81]
POSSIBLE INVOLVEMENT IN FH, AND VARIANT FH LEU-167 DEL.
PubMed=24267230; DOI=10.1016/j.atherosclerosis.2013.09.007;
Awan Z., Choi H.Y., Stitziel N., Ruel I., Bamimore M.A., Husa R.,
Gagnon M.H., Wang R.H., Peloso G.M., Hegele R.A., Seidah N.G.,
Kathiresan S., Genest J.;
"APOE p.Leu167del mutation in familial hypercholesterolemia.";
Atherosclerosis 231:218-222(2013).
[82]
POSSIBLE INVOLVEMENT IN FH, AND VARIANT FH LEU-167 DEL.
PubMed=22949395; DOI=10.1002/humu.22215;
Marduel M., Ouguerram K., Serre V., Bonnefont-Rousselot D.,
Marques-Pinheiro A., Erik Berge K., Devillers M., Luc G., Lecerf J.M.,
Tosolini L., Erlich D., Peloso G.M., Stitziel N., Nitchke P.,
Jais J.P., Abifadel M., Kathiresan S., Leren T.P., Rabes J.P.,
Boileau C., Varret M.;
"Description of a large family with autosomal dominant
hypercholesterolemia associated with the APOE p.Leu167del mutation.";
Hum. Mutat. 34:83-87(2013).
[83]
POSSIBLE INVOLVEMENT IN FH, AND VARIANTS FH PRO-46; ASP-145; CYS-163
AND LEU-167 DEL.
PubMed=26802169; DOI=10.1194/jlr.P055699;
Wintjens R., Bozon D., Belabbas K., Mbou F., Girardet J.P.,
Tounian P., Jolly M., Boccara F., Cohen A., Karsenty A., Dubern B.,
Carel J.C., Azar-Kolakez A., Feillet F., Labarthe F., Gorsky A.M.,
Horovitz A., Tamarindi C., Kieffer P., Lienhardt A., Lascols O.,
Di Filippo M., Dufernez F.;
"Global molecular analysis and APOE mutations in a cohort of autosomal
dominant hypercholesterolemia patients in France.";
J. Lipid Res. 57:482-491(2016).
[84]
REVIEW, AND VARIANTS LYS-31; ARG-102; ARG-130; GLN-152 AND CYS-154.
PubMed=7833947; DOI=10.1002/humu.1380040303;
de Knijff P., van den Maagdenberg A.M.J.M., Frants R.R., Havekes L.M.;
"Genetic heterogeneity of apolipoprotein E and its influence on plasma
lipid and lipoprotein levels.";
Hum. Mutat. 4:178-194(1994).
[85]
REVIEW, POLYMORPHISM, AND TISSUE SPECIFICITY.
PubMed=25173806; DOI=10.1016/j.nbd.2014.08.025;
Huang Y., Mahley R.W.;
"Apolipoprotein E: structure and function in lipid metabolism,
neurobiology, and Alzheimer's diseases.";
Neurobiol. Dis. 72:3-12(2014).
[86]
REVIEW, FUNCTION, AND PTM.
PubMed=29516132; DOI=10.1007/s00109-018-1632-y;
Kockx M., Traini M., Kritharides L.;
"Cell-specific production, secretion, and function of apolipoprotein
E.";
J. Mol. Med. 96:361-371(2018).
-!- FUNCTION: APOE is an apolipoprotein, a protein associating with
lipid particles, that mainly functions in lipoprotein-mediated
lipid transport between organs via the plasma and interstitial
fluids (PubMed:6860692, PubMed:1911868, PubMed:14754908). APOE is
a core component of plasma lipoproteins and is involved in their
production, conversion and clearance (PubMed:6860692,
PubMed:2762297, PubMed:1911868, PubMed:1917954, PubMed:9395455,
PubMed:14754908, PubMed:23620513). Apoliproteins are amphipathic
molecules that interact both with lipids of the lipoprotein
particle core and the aqueous environment of the plasma
(PubMed:6860692, PubMed:2762297, PubMed:9395455). As such, APOE
associates with chylomicrons, chylomicron remnants, very low
density lipoproteins (VLDL) and intermediate density lipoproteins
(IDL) but shows a preferential binding to high-density
lipoproteins (HDL) (PubMed:6860692, PubMed:1911868). It also binds
a wide range of cellular receptors including the LDL
receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and
LRP8 and the very low-density lipoprotein receptor/VLDLR that
mediate the cellular uptake of the APOE-containing lipoprotein
particles (PubMed:2762297, PubMed:1917954, PubMed:7768901,
PubMed:8939961, PubMed:12950167, PubMed:20030366, PubMed:2063194,
PubMed:8756331, PubMed:20303980, PubMed:1530612, PubMed:7635945).
Finally, APOE has also a heparin-binding activity and binds
heparan-sulfate proteoglycans on the surface of cells, a property
that supports the capture and the receptor-mediated uptake of
APOE-containing lipoproteins by cells (PubMed:9395455,
PubMed:9488694, PubMed:23676495, PubMed:7635945). A main function
of APOE is to mediate lipoprotein clearance through the uptake of
chylomicrons, VLDLs, and HDLs by hepatocytes (PubMed:1911868,
PubMed:1917954, PubMed:9395455, PubMed:23676495, PubMed:29516132).
APOE is also involved in the biosynthesis by the liver of VLDLs as
well as their uptake by peripheral tissues ensuring the delivery
of triglycerides and energy storage in muscle, heart and adipose
tissues (PubMed:2762297, PubMed:29516132). By participating to the
lipoprotein-mediated distribution of lipids among tissues, APOE
plays a critical role in plasma and tissues lipid homeostasis
(PubMed:2762297, PubMed:1917954, PubMed:29516132). APOE is also
involved in two steps of reverse cholesterol transport, the HDLs-
mediated transport of cholesterol from peripheral tissues to the
liver, and thereby plays an important role in cholesterol
homeostasis (PubMed:9395455, PubMed:14754908, PubMed:23620513).
First, it is functionally associated with ABCA1 in the biogenesis
of HDLs in tissues (PubMed:14754908, PubMed:23620513). Second, it
is enriched in circulating HDLs and mediates their uptake by
hepatocytes (PubMed:9395455). APOE also plays an important role in
lipid transport in the central nervous system, regulating neuron
survival and sprouting (PubMed:8939961, PubMed:25173806). APOE in
also involved in innate and adaptive immune responses, controlling
for instance the survival of myeloid-derived suppressor cells (By
similarity). APOE, may also play a role in transcription
regulation through a receptor-dependent and cholesterol-
independent mechanism, that activates MAP3K12 and a non-canonical
MAPK signal transduction pathway that results in enhanced AP-1-
mediated transcription of APP (PubMed:28111074).
{ECO:0000250|UniProtKB:P08226, ECO:0000269|PubMed:12950167,
ECO:0000269|PubMed:14754908, ECO:0000269|PubMed:1530612,
ECO:0000269|PubMed:1911868, ECO:0000269|PubMed:1917954,
ECO:0000269|PubMed:20030366, ECO:0000269|PubMed:20303980,
ECO:0000269|PubMed:2063194, ECO:0000269|PubMed:23620513,
ECO:0000269|PubMed:23676495, ECO:0000269|PubMed:2762297,
ECO:0000269|PubMed:28111074, ECO:0000269|PubMed:6860692,
ECO:0000269|PubMed:7635945, ECO:0000269|PubMed:7768901,
ECO:0000269|PubMed:8756331, ECO:0000269|PubMed:8939961,
ECO:0000269|PubMed:9395455, ECO:0000269|PubMed:9488694,
ECO:0000303|PubMed:25173806, ECO:0000303|PubMed:29516132}.
-!- SUBUNIT: Homotetramer (PubMed:8340399). May interact with ABCA1;
functionally associated with ABCA1 in the biogenesis of HDLs
(PubMed:14754908). May interact with APP/A4 amyloid-beta peptide;
the interaction is extremely stable in vitro but its physiological
significance is unclear (PubMed:8367470, PubMed:23620513). May
interact with MAPT (PubMed:7972031). May interact with MAP2
(PubMed:7891887). {ECO:0000269|PubMed:14754908,
ECO:0000269|PubMed:23620513, ECO:0000269|PubMed:7891887,
ECO:0000269|PubMed:7972031, ECO:0000269|PubMed:8340399,
ECO:0000269|PubMed:8367470}.
-!- INTERACTION:
P27958:- (xeno); NbExp=4; IntAct=EBI-1222467, EBI-6904269;
P05067:APP; NbExp=3; IntAct=EBI-1222467, EBI-2431589;
Q16543:CDC37; NbExp=3; IntAct=EBI-1222467, EBI-295634;
Q9BQ95:ECSIT; NbExp=4; IntAct=EBI-1222467, EBI-712452;
P00738:HP; NbExp=7; IntAct=EBI-1222467, EBI-1220767;
P01130:LDLR; NbExp=2; IntAct=EBI-1222467, EBI-988319;
Q14114:LRP8; NbExp=2; IntAct=EBI-1222467, EBI-2681187;
P10636:MAPT; NbExp=3; IntAct=EBI-9209835, EBI-366182;
Q53EL6:PDCD4; NbExp=3; IntAct=EBI-1222467, EBI-935824;
P50502:ST13; NbExp=3; IntAct=EBI-1222467, EBI-357285;
O75069:TMCC2; NbExp=5; IntAct=EBI-1222467, EBI-726731;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2498325}.
Secreted, extracellular space {ECO:0000269|PubMed:8340399}.
Secreted, extracellular space, extracellular matrix
{ECO:0000269|PubMed:9488694}. Note=In the plasma, APOE is
associated with chylomicrons, chylomicrons remnants, VLDL, LDL and
HDL lipoproteins (PubMed:1911868, PubMed:8340399). Lipid poor
oligomeric APOE is associated with the extracellular matrix in a
calcium- and heparan-sulfate proteoglycans-dependent manner
(PubMed:9488694). Lipidation induces the release from the
extracellular matrix (PubMed:9488694).
{ECO:0000269|PubMed:1911868, ECO:0000269|PubMed:8340399,
ECO:0000269|PubMed:9488694}.
-!- TISSUE SPECIFICITY: Produced by several tissues and cell types and
mainly found associated with lipid particles in the plasma, the
interstitial fluid and lymph (PubMed:25173806). Mainly synthesized
by liver hepatocytes (PubMed:25173806). Significant quantities are
also produced in brain, mainly by astrocytes and glial cells in
the cerebral cortex, but also by neurons in frontal cortex and
hippocampus (PubMed:3115992, PubMed:10027417). It is also
expressed by cells of the peripheral nervous system
(PubMed:10027417, PubMed:25173806). Also expressed by adrenal
gland, testis, ovary, skin, kidney, spleen and adipose tissue and
macrophages in various tissues (PubMed:25173806).
{ECO:0000269|PubMed:10027417, ECO:0000269|PubMed:3115992,
ECO:0000303|PubMed:25173806}.
-!- PTM: APOE exists as multiple glycosylated and sialylated
glycoforms within cells and in plasma (PubMed:29516132). The
extent of glycosylation and sialylation are tissue and context
specific (PubMed:29516132). Plasma APOE undergoes desialylation
and is less glycosylated and sialylated than the cellular form
(PubMed:2498325, PubMed:19838169, PubMed:20511397,
PubMed:23234360). Glycosylation is not required for proper
expression and secretion (PubMed:2498325). O-glycosylated with
core 1 or possibly core 8 glycans. Thr-307 and Ser-314 are minor
glycosylation sites compared to Ser-308 (PubMed:19838169,
PubMed:23234360). {ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:20511397, ECO:0000269|PubMed:23234360,
ECO:0000269|PubMed:2498325, ECO:0000303|PubMed:29516132}.
-!- PTM: Glycated in plasma VLDL of normal subjects, and of
hyperglycemic diabetic patients at a higher level (2-3 fold).
{ECO:0000269|PubMed:10452964}.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- PTM: Undergoes C-terminal proteolytic processing in neurons. C-
terminally truncated APOE has a tendency to form neurotoxic
intracellular neurofibrillary tangle-like inclusions in neurons.
{ECO:0000269|PubMed:11447277}.
-!- POLYMORPHISM: There are three common APOE alleles identified:
APOE*2/APOE-epsilon2/E2, APOE*3/APOE-epsilon3/E3, and APOE*4/APOE-
epsilon4/E4. The corresponding ApoE2, ApoE3 and ApoE4 isoforms
differentially present Cys and Arg residues at positions 130 and
176. The most common allele in the human population is APOE*3
which sequence is the one displayed in that entry with a Cys at
position 130 and an Arg at position 176. Common APOE variants
influence lipoprotein metabolism in healthy individuals.
Additional variants have been described and are described relative
to the three common alleles. {ECO:0000269|PubMed:2987927,
ECO:0000269|PubMed:3243553, ECO:0000269|PubMed:6325438,
ECO:0000303|PubMed:25173806}.
-!- DISEASE: Hyperlipoproteinemia 3 (HLPP3) [MIM:617347]: A disorder
characterized by the accumulation of intermediate-density
lipoprotein particles (IDL or broad-beta-lipoprotein) rich in
cholesterol. Clinical features include xanthomas, yellowish lipid
deposits in the palmar crease, or less specific on tendons and on
elbows. The disorder rarely manifests before the third decade in
men. In women, it is usually expressed only after the menopause.
{ECO:0000269|PubMed:1361196, ECO:0000269|PubMed:1674745,
ECO:0000269|PubMed:2101409, ECO:0000269|PubMed:22481068,
ECO:0000269|PubMed:2556398, ECO:0000269|PubMed:2738044,
ECO:0000269|PubMed:7635945, ECO:0000269|PubMed:8287539}. Note=The
disease is caused by mutations affecting the gene represented in
this entry. The vast majority of the patients are homozygous for
APOE*2 alleles. More severe cases of HLPP3 have also been observed
in individuals heterozygous for rare APOE variants. The influence
of APOE on lipid levels is often suggested to have major
implications for the risk of coronary artery disease (CAD).
Individuals carrying the common APOE*4 variant are at higher risk
of CAD.
-!- DISEASE: Alzheimer disease 2 (AD2) [MIM:104310]: A late-onset form
of Alzheimer disease. Alzheimer disease is a neurodegenerative
disorder characterized by progressive dementia, loss of cognitive
abilities, and deposition of fibrillar amyloid proteins as
intraneuronal neurofibrillary tangles, extracellular amyloid
plaques and vascular amyloid deposits. The major constituents of
these plaques are neurotoxic amyloid-beta protein 40 and amyloid-
beta protein 42, that are produced by the proteolysis of the
transmembrane APP protein. The cytotoxic C-terminal fragments
(CTFs) and the caspase-cleaved products, such as C31, are also
implicated in neuronal death. {ECO:0000269|PubMed:10903326,
ECO:0000269|PubMed:11258893, ECO:0000269|PubMed:11447277,
ECO:0000269|PubMed:28111074, ECO:0000269|PubMed:2987927,
ECO:0000269|PubMed:7891887, ECO:0000269|PubMed:7972031,
ECO:0000269|PubMed:8071364, ECO:0000269|PubMed:8346443,
ECO:0000269|PubMed:8367470, ECO:0000269|PubMed:8939961}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry. The APOE*4 allele
(APOE form E4) is genetically associated with the common late
onset familial and sporadic forms of Alzheimer disease. Risk for
AD increased from 20% to 90% and mean age at onset decreased from
84 to 68 years with increasing number of APOE*4 alleles in 42
families with late onset AD. Thus APOE*4 gene dose is a major risk
factor for late onset AD and, in these families, homozygosity for
APOE*4 was virtually sufficient to cause AD by age 80. The
mechanism by which APOE*4 participates in pathogenesis is not
known. {ECO:0000269|PubMed:8346443}.
-!- DISEASE: Sea-blue histiocyte disease (SBHD) [MIM:269600]:
Characterized by splenomegaly, mild thrombocytopenia and, in the
bone marrow, numerous histiocytes containing cytoplasmic granules
which stain bright blue with the usual hematologic stains. The
syndrome is the consequence of an inherited metabolic defect
analogous to Gaucher disease and other sphingolipidoses.
{ECO:0000269|PubMed:11095479, ECO:0000269|PubMed:16094309}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Lipoprotein glomerulopathy (LPG) [MIM:611771]: Uncommon
kidney disease characterized by proteinuria, progressive kidney
failure, and distinctive lipoprotein thrombi in glomerular
capillaries. {ECO:0000269|PubMed:10432380,
ECO:0000269|PubMed:10903326, ECO:0000269|PubMed:18077821,
ECO:0000269|PubMed:9176854}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Familial hypercholesterolemia (FH) [MIM:143890]: A common
autosomal dominant disorder characterized by elevated serum low-
density lipoprotein (LDL) cholesterol levels, which result in
excess deposition of cholesterol in tissues and leads to
xanthelasma, xanthomas, accelerated atherosclerosis and increased
risk of premature coronary heart disease. The disorder occurs in 2
clinical forms: a mild form that becomes evident in the fourth or
fifth decade in individuals carrying heterozygous LDLR mutations;
a more severe form that usually manifests in the first two decades
of life in individuals with homozygous LDLR mutations.
{ECO:0000269|PubMed:22949395, ECO:0000269|PubMed:24267230,
ECO:0000269|PubMed:26802169}. Note=The disease may be caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOE";
-!- WEB RESOURCE: Name=Wikipedia; Note=Apolipoprotein E entry;
URL="https://en.wikipedia.org/wiki/Apolipoprotein_E";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Tangled - Issue 83 of
June 2007;
URL="https://web.expasy.org/spotlight/back_issues/083";
-----------------------------------------------------------------------
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EMBL; M12529; AAB59518.1; -; mRNA.
EMBL; K00396; AAB59546.1; -; mRNA.
EMBL; M10065; AAB59397.1; -; Genomic_DNA.
EMBL; AF050154; AAD02505.1; -; Genomic_DNA.
EMBL; AF261279; AAG27089.1; -; Genomic_DNA.
EMBL; AK314898; BAG37412.1; -; mRNA.
EMBL; FJ525876; ACN81314.1; -; Genomic_DNA.
EMBL; BC003557; AAH03557.1; -; mRNA.
EMBL; AB035149; BAA96080.1; -; Genomic_DNA.
CCDS; CCDS12647.1; -.
PIR; A92478; LPHUE.
RefSeq; NP_000032.1; NM_000041.3.
RefSeq; NP_001289617.1; NM_001302688.1.
RefSeq; NP_001289618.1; NM_001302689.1.
RefSeq; NP_001289619.1; NM_001302690.1.
RefSeq; NP_001289620.1; NM_001302691.1.
UniGene; Hs.654439; -.
PDB; 1B68; X-ray; 2.00 A; A=19-209.
PDB; 1BZ4; X-ray; 1.85 A; A=40-183.
PDB; 1EA8; X-ray; 1.95 A; A=19-209.
PDB; 1GS9; X-ray; 1.70 A; A=19-183.
PDB; 1H7I; X-ray; 1.90 A; A=19-209.
PDB; 1LE2; X-ray; 3.00 A; A=41-184.
PDB; 1LE4; X-ray; 2.50 A; A=41-184.
PDB; 1LPE; X-ray; 2.25 A; A=41-184.
PDB; 1NFN; X-ray; 1.80 A; A=19-209.
PDB; 1NFO; X-ray; 2.00 A; A=19-209.
PDB; 1OEF; NMR; -; A=281-304.
PDB; 1OEG; NMR; -; A=285-307.
PDB; 1OR2; X-ray; 2.50 A; A=19-183.
PDB; 1OR3; X-ray; 1.73 A; A=19-183.
PDB; 2KC3; NMR; -; A=19-201.
PDB; 2KNY; NMR; -; A=147-167.
PDB; 2L7B; NMR; -; A=19-317.
PDBsum; 1B68; -.
PDBsum; 1BZ4; -.
PDBsum; 1EA8; -.
PDBsum; 1GS9; -.
PDBsum; 1H7I; -.
PDBsum; 1LE2; -.
PDBsum; 1LE4; -.
PDBsum; 1LPE; -.
PDBsum; 1NFN; -.
PDBsum; 1NFO; -.
PDBsum; 1OEF; -.
PDBsum; 1OEG; -.
PDBsum; 1OR2; -.
PDBsum; 1OR3; -.
PDBsum; 2KC3; -.
PDBsum; 2KNY; -.
PDBsum; 2L7B; -.
ProteinModelPortal; P02649; -.
SMR; P02649; -.
BioGrid; 106845; 77.
DIP; DIP-1120N; -.
IntAct; P02649; 34.
MINT; P02649; -.
STRING; 9606.ENSP00000252486; -.
DrugBank; DB00062; Human Serum Albumin.
DrugBank; DB00064; Serum albumin iodonated.
MoonDB; P02649; Predicted.
CarbonylDB; P02649; -.
GlyConnect; 648; -.
iPTMnet; P02649; -.
PhosphoSitePlus; P02649; -.
SwissPalm; P02649; -.
UniCarbKB; P02649; -.
BioMuta; APOE; -.
DMDM; 114039; -.
DOSAC-COBS-2DPAGE; P02649; -.
SWISS-2DPAGE; P02649; -.
EPD; P02649; -.
jPOST; P02649; -.
MaxQB; P02649; -.
PaxDb; P02649; -.
PeptideAtlas; P02649; -.
PRIDE; P02649; -.
ProteomicsDB; 51537; -.
DNASU; 348; -.
Ensembl; ENST00000252486; ENSP00000252486; ENSG00000130203.
GeneID; 348; -.
KEGG; hsa:348; -.
UCSC; uc002pab.4; human.
CTD; 348; -.
DisGeNET; 348; -.
EuPathDB; HostDB:ENSG00000130203.9; -.
GeneCards; APOE; -.
GeneReviews; APOE; -.
HGNC; HGNC:613; APOE.
HPA; CAB008363; -.
HPA; CAB069921; -.
HPA; HPA065539; -.
HPA; HPA068768; -.
MalaCards; APOE; -.
MIM; 104310; phenotype.
MIM; 107741; gene.
MIM; 143890; phenotype.
MIM; 269600; phenotype.
MIM; 611771; phenotype.
MIM; 617347; phenotype.
neXtProt; NX_P02649; -.
OpenTargets; ENSG00000130203; -.
Orphanet; 412; Hyperlipoproteinemia type 3.
Orphanet; 329481; Lipoprotein glomerulopathy.
Orphanet; 238616; NON RARE IN EUROPE: Alzheimer disease.
Orphanet; 1648; NON RARE IN EUROPE: Dementia with Lewy body.
Orphanet; 406; NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia.
Orphanet; 158029; Sea-blue histiocytosis.
PharmGKB; PA55; -.
eggNOG; ENOG410IVK0; Eukaryota.
eggNOG; ENOG4111MYC; LUCA.
GeneTree; ENSGT00730000111315; -.
HOGENOM; HOG000034006; -.
HOVERGEN; HBG010582; -.
InParanoid; P02649; -.
KO; K04524; -.
OMA; ARLKGWF; -.
OrthoDB; 1344247at2759; -.
PhylomeDB; P02649; -.
TreeFam; TF334458; -.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8864260; Transcriptional regulation by the AP-2 (TFAP2) family of transcription factors.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-8963888; Chylomicron assembly.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-8964026; Chylomicron clearance.
Reactome; R-HSA-8964058; HDL remodeling.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
SIGNOR; P02649; -.
ChiTaRS; APOE; human.
EvolutionaryTrace; P02649; -.
GeneWiki; Apolipoprotein_E; -.
GenomeRNAi; 348; -.
PMAP-CutDB; P02649; -.
PRO; PR:P02649; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130203; Expressed in 224 organ(s), highest expression level in left adrenal gland.
ExpressionAtlas; P02649; baseline and differential.
Genevisible; P02649; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0030425; C:dendrite; NAS:BHF-UCL.
GO; GO:0034365; C:discoidal high-density lipoprotein particle; TAS:ARUK-UCL.
GO; GO:0005769; C:early endosome; TAS:Reactome.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:AgBase.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:ARUK-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0005794; C:Golgi apparatus; IDA:AgBase.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:UniProtKB.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:UniProtKB.
GO; GO:1990777; C:lipoprotein particle; IDA:ARUK-UCL.
GO; GO:0034362; C:low-density lipoprotein particle; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; NAS:BHF-UCL.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043083; C:synaptic cleft; IDA:SynGO.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IDA:UniProtKB.
GO; GO:0016209; F:antioxidant activity; IDA:BHF-UCL.
GO; GO:0015485; F:cholesterol binding; IBA:GO_Central.
GO; GO:0017127; F:cholesterol transporter activity; IBA:GO_Central.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
GO; GO:0005319; F:lipid transporter activity; IDA:BHF-UCL.
GO; GO:0071813; F:lipoprotein particle binding; IEA:Ensembl.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:UniProtKB.
GO; GO:0046911; F:metal chelating activity; IDA:BHF-UCL.
GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IDA:BHF-UCL.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0046983; F:protein dimerization activity; IDA:ARUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:ARUK-UCL.
GO; GO:0044877; F:protein-containing complex binding; IDA:ARUK-UCL.
GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
GO; GO:0005198; F:structural molecule activity; TAS:ARUK-UCL.
GO; GO:0048156; F:tau protein binding; IPI:BHF-UCL.
GO; GO:0070326; F:very-low-density lipoprotein particle receptor binding; IDA:BHF-UCL.
GO; GO:0097113; P:AMPA glutamate receptor clustering; IDA:Alzheimers_University_of_Toronto.
GO; GO:0042982; P:amyloid precursor protein metabolic process; IDA:UniProtKB.
GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0019934; P:cGMP-mediated signaling; IDA:BHF-UCL.
GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
GO; GO:0033344; P:cholesterol efflux; IDA:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0034378; P:chylomicron assembly; TAS:Reactome.
GO; GO:0034382; P:chylomicron remnant clearance; IDA:UniProtKB.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB.
GO; GO:0055089; P:fatty acid homeostasis; IDA:Alzheimers_University_of_Toronto.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IDA:UniProtKB.
GO; GO:0034384; P:high-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IGI:BHF-UCL.
GO; GO:0071831; P:intermediate-density lipoprotein particle clearance; IDA:UniProtKB.
GO; GO:0046907; P:intracellular transport; TAS:UniProtKB.
GO; GO:0010877; P:lipid transport involved in lipid storage; ISS:BHF-UCL.
GO; GO:0042158; P:lipoprotein biosynthetic process; IDA:UniProtKB.
GO; GO:0042159; P:lipoprotein catabolic process; IBA:GO_Central.
GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
GO; GO:0035641; P:locomotory exploration behavior; IMP:ARUK-UCL.
GO; GO:0015909; P:long-chain fatty acid transport; IDA:Alzheimers_University_of_Toronto.
GO; GO:0007616; P:long-term memory; IGI:ARUK-UCL.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
GO; GO:0051651; P:maintenance of location in cell; IEA:Ensembl.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030195; P:negative regulation of blood coagulation; IDA:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:ARUK-UCL.
GO; GO:0032269; P:negative regulation of cellular protein metabolic process; IGI:ARUK-UCL.
GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:BHF-UCL.
GO; GO:0090370; P:negative regulation of cholesterol efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0061000; P:negative regulation of dendritic spine development; IDA:Alzheimers_University_of_Toronto.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IDA:Alzheimers_University_of_Toronto.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:0010629; P:negative regulation of gene expression; ISS:ARUK-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IDA:Alzheimers_University_of_Toronto.
GO; GO:1903001; P:negative regulation of lipid transport across blood-brain barrier; IDA:Alzheimers_University_of_Toronto.
GO; GO:1900272; P:negative regulation of long-term synaptic potentiation; IDA:ARUK-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IBA:GO_Central.
GO; GO:1901215; P:negative regulation of neuron death; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ARUK-UCL.
GO; GO:1902999; P:negative regulation of phospholipid efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010544; P:negative regulation of platelet activation; IDA:BHF-UCL.
GO; GO:1901627; P:negative regulation of postsynaptic membrane organization; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901630; P:negative regulation of presynaptic membrane organization; IDA:Alzheimers_University_of_Toronto.
GO; GO:0090209; P:negative regulation of triglyceride metabolic process; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
GO; GO:0007263; P:nitric oxide mediated signal transduction; IDA:BHF-UCL.
GO; GO:0097114; P:NMDA glutamate receptor clustering; IDA:Alzheimers_University_of_Toronto.
GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
GO; GO:0044794; P:positive regulation by host of viral process; IMP:AgBase.
GO; GO:1905908; P:positive regulation of amyloid fibril formation; TAS:ARUK-UCL.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010873; P:positive regulation of cholesterol esterification; IDA:BHF-UCL.
GO; GO:0060999; P:positive regulation of dendritic spine development; IDA:Alzheimers_University_of_Toronto.
GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IDA:Alzheimers_University_of_Toronto.
GO; GO:0045807; P:positive regulation of endocytosis; IDA:ARUK-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:1905855; P:positive regulation of heparan sulfate binding; IDA:ARUK-UCL.
GO; GO:1905860; P:positive regulation of heparan sulfate proteoglycan binding; IDA:ARUK-UCL.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IDA:Alzheimers_University_of_Toronto.
GO; GO:1903002; P:positive regulation of lipid transport across blood-brain barrier; IDA:Alzheimers_University_of_Toronto.
GO; GO:0032805; P:positive regulation of low-density lipoprotein particle receptor catabolic process; IDA:BHF-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:1902998; P:positive regulation of neurofibrillary tangle assembly; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901216; P:positive regulation of neuron death; IDA:Alzheimers_University_of_Toronto.
GO; GO:0010976; P:positive regulation of neuron projection development; IDA:ARUK-UCL.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:BHF-UCL.
GO; GO:1902995; P:positive regulation of phospholipid efflux; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901628; P:positive regulation of postsynaptic membrane organization; IDA:Alzheimers_University_of_Toronto.
GO; GO:1901631; P:positive regulation of presynaptic membrane organization; IDA:Alzheimers_University_of_Toronto.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0017038; P:protein import; IDA:Alzheimers_University_of_Toronto.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:1905906; P:regulation of amyloid fibril formation; IDA:ARUK-UCL.
GO; GO:1900221; P:regulation of amyloid-beta clearance; IDA:Alzheimers_University_of_Toronto.
GO; GO:0030516; P:regulation of axon extension; TAS:UniProtKB.
GO; GO:2000822; P:regulation of behavioral fear response; IMP:ARUK-UCL.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IDA:BHF-UCL.
GO; GO:1905890; P:regulation of cellular response to very-low-density lipoprotein particle stimulus; IDA:ARUK-UCL.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IGI:ARUK-UCL.
GO; GO:0032374; P:regulation of cholesterol transport; IBA:GO_Central.
GO; GO:0045088; P:regulation of innate immune response; IEA:Ensembl.
GO; GO:1901214; P:regulation of neuron death; IDA:Alzheimers_University_of_Toronto.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; TAS:UniProtKB.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:0032462; P:regulation of protein homooligomerization; IDA:ARUK-UCL.
GO; GO:0051246; P:regulation of protein metabolic process; IGI:ARUK-UCL.
GO; GO:1902947; P:regulation of tau-protein kinase activity; IDA:Alzheimers_University_of_Toronto.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0061771; P:response to caloric restriction; IGI:ARUK-UCL.
GO; GO:0002021; P:response to dietary excess; IEA:Ensembl.
GO; GO:0000302; P:response to reactive oxygen species; NAS:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0043691; P:reverse cholesterol transport; IDA:BHF-UCL.
GO; GO:0007271; P:synaptic transmission, cholinergic; TAS:UniProtKB.
GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
GO; GO:0070328; P:triglyceride homeostasis; ISS:BHF-UCL.
GO; GO:0006641; P:triglyceride metabolic process; IDA:BHF-UCL.
GO; GO:0071830; P:triglyceride-rich lipoprotein particle clearance; IMP:UniProtKB.
GO; GO:0042311; P:vasodilation; IEA:Ensembl.
GO; GO:0034447; P:very-low-density lipoprotein particle clearance; IDA:UniProtKB.
GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
GO; GO:0019068; P:virion assembly; IMP:AgBase.
InterPro; IPR000074; ApoA_E.
Pfam; PF01442; Apolipoprotein; 1.
1: Evidence at protein level;
3D-structure; Alzheimer disease; Amyloidosis; Cholesterol metabolism;
Chylomicron; Complete proteome; Direct protein sequencing;
Disease mutation; Extracellular matrix; Glycation; Glycoprotein; HDL;
Heparin-binding; Hyperlipidemia; Lipid metabolism; Lipid transport;
Lipid-binding; Neurodegeneration; Oxidation; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Secreted; Signal;
Steroid metabolism; Sterol metabolism; Transport; VLDL.
SIGNAL 1 18 {ECO:0000269|PubMed:7068630}.
CHAIN 19 317 Apolipoprotein E.
/FTId=PRO_0000001987.
REPEAT 80 101 1.
REPEAT 102 123 2.
REPEAT 124 145 3.
REPEAT 146 167 4.
REPEAT 168 189 5.
REPEAT 190 211 6.
REPEAT 212 233 7.
REPEAT 234 255 8.
REGION 80 255 8 X 22 AA approximate tandem repeats.
REGION 158 168 LDL and other lipoprotein receptors
binding. {ECO:0000269|PubMed:20030366,
ECO:0000269|PubMed:2063194}.
REGION 162 165 Heparin-binding.
{ECO:0000269|PubMed:3947350}.
REGION 210 290 Lipid-binding and lipoprotein
association. {ECO:0000269|PubMed:2280190,
ECO:0000269|PubMed:8071364}.
REGION 229 236 Heparin-binding.
{ECO:0000269|PubMed:3947350}.
REGION 266 317 Homooligomerization.
{ECO:0000269|PubMed:8340399}.
REGION 278 290 Specificity for association with VLDL.
{ECO:0000269|PubMed:8071364}.
MOD_RES 143 143 Methionine sulfoxide.
{ECO:0000250|UniProtKB:P08226}.
MOD_RES 147 147 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
CARBOHYD 26 26 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23234360}.
CARBOHYD 36 36 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:23234360}.
CARBOHYD 93 93 N-linked (Glc) (glycation) lysine.
{ECO:0000269|PubMed:10452964}.
CARBOHYD 212 212 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:2498325}.
CARBOHYD 307 307 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:19838169}.
CARBOHYD 308 308 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:19838169,
ECO:0000269|PubMed:20511397}.
CARBOHYD 314 314 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:23234360}.
VARIANT 21 21 E -> K (in ApoE5; associated with
hyperlipoproteinemia and atherosclerosis;
increased binding to LDL receptor;
dbSNP:rs121918392).
{ECO:0000269|PubMed:1530612,
ECO:0000269|PubMed:2760009}.
/FTId=VAR_000645.
VARIANT 31 31 E -> K (in HLPP3; ApoE4 Philadelphia,
ApoE5 French-Canadian and ApoE5-type;
only ApoE4 Philadelphia is associated
with HLPP3; dbSNP:rs201672011).
{ECO:0000269|PubMed:1674745,
ECO:0000269|PubMed:1713245,
ECO:0000303|PubMed:7833947}.
/FTId=VAR_000646.
VARIANT 43 43 R -> C (in LPG; ApoE2 Kyoto;
dbSNP:rs121918399).
{ECO:0000269|PubMed:10432380,
ECO:0000269|PubMed:18077821}.
/FTId=VAR_042734.
VARIANT 46 46 L -> P (in FH; unknown pathological
significance; ApoE4 Freiburg;
dbSNP:rs769452).
{ECO:0000269|PubMed:11042151,
ECO:0000269|PubMed:26802169}.
/FTId=VAR_000647.
VARIANT 60 60 T -> A (in ApoE3 Freiburg;
dbSNP:rs28931576).
/FTId=VAR_000648.
VARIANT 64 64 Q -> H (polymorphism; confirmed at
protein level; dbSNP:rs370594287).
{ECO:0000269|PubMed:22028381,
ECO:0000269|Ref.10}.
/FTId=VAR_014114.
VARIANT 99 99 Q -> K (in ApoE5 Frankfurt;
dbSNP:rs1180612218).
{ECO:0000269|PubMed:8125051}.
/FTId=VAR_000649.
VARIANT 102 102 P -> R (in ApoE5-type; no hyperlipidemia;
dbSNP:rs11083750).
{ECO:0000303|PubMed:7833947}.
/FTId=VAR_000650.
VARIANT 117 117 A -> T (in ApoE3*; dbSNP:rs28931577).
{ECO:0000269|PubMed:6327682}.
/FTId=VAR_000651.
VARIANT 124 124 A -> V (in ApoE3 Basel;
dbSNP:rs937063425).
{ECO:0000269|PubMed:12864777}.
/FTId=VAR_016789.
VARIANT 130 130 C -> R (in HLPP3 and AD2; ApoE4, ApoE3
Leiden, ApoE3**, ApoE5-Frankfurt and
ApoE5-type; ApoE3 Leiden and ApoE3** are
associated with HLPP3; ApoE4 is
associated with AD2; changed protein
structure; no effect on binding to LDL
receptor; decreased association with HDL
and enrichment in VLDL and IDL; may
prevent the interaction with MAP2 and
MAPT; changed interaction with APP/A4
amyloid-beta peptide; increased ability
to induce APP transcription; increased C-
terminal proteolytic processing in
neurons; decreased function in neurite
outgrowth; dbSNP:rs429358).
{ECO:0000269|PubMed:10903326,
ECO:0000269|PubMed:11042151,
ECO:0000269|PubMed:11447277,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:2280190,
ECO:0000269|PubMed:2556398,
ECO:0000269|PubMed:28111074,
ECO:0000269|PubMed:2987927,
ECO:0000269|PubMed:7891887,
ECO:0000269|PubMed:7972031,
ECO:0000269|PubMed:8071364,
ECO:0000269|PubMed:8125051,
ECO:0000269|PubMed:8287539,
ECO:0000269|PubMed:8346443,
ECO:0000269|PubMed:8367470,
ECO:0000269|PubMed:8939961,
ECO:0000269|PubMed:9360638,
ECO:0000303|PubMed:7833947}.
/FTId=VAR_000652.
VARIANT 145 145 G -> D (in FH; unknown pathological
significance; ApoE1 Weisgraber;
dbSNP:rs267606664).
{ECO:0000269|PubMed:26802169,
ECO:0000269|PubMed:8287539}.
/FTId=VAR_000653.
VARIANT 145 145 G -> GEVQAMLG (in HLPP3; ApoE3 Leiden; no
effect on glycosylation).
{ECO:0000269|PubMed:2556398,
ECO:0000269|PubMed:8468528}.
/FTId=VAR_000654.
VARIANT 152 152 R -> Q (in ApoE2-type; no hyperlipidemia;
dbSNP:rs28931578).
{ECO:0000303|PubMed:7833947}.
/FTId=VAR_000655.
VARIANT 154 154 R -> C (in HLPP3; ApoE2-type;
dbSNP:rs121918393).
{ECO:0000303|PubMed:7833947}.
/FTId=VAR_000657.
VARIANT 154 154 R -> S (in HLPP3; ApoE2 Christchurch;
decreased binding to LDL receptor;
dbSNP:rs121918393).
{ECO:0000269|PubMed:22481068,
ECO:0000269|PubMed:2831187,
ECO:0000269|PubMed:8287539}.
/FTId=VAR_000656.
VARIANT 160 160 R -> C (in HLPP3; ApoE3**;
dbSNP:rs387906567).
{ECO:0000269|PubMed:8287539}.
/FTId=VAR_000658.
VARIANT 163 163 R -> C (in HLPP3 and FH; ApoE4
Philadelphia and ApoE2-type;
dbSNP:rs769455).
{ECO:0000269|PubMed:11042151,
ECO:0000269|PubMed:1674745,
ECO:0000269|PubMed:26802169}.
/FTId=VAR_000659.
VARIANT 163 163 R -> H (in HLPP3; unknown pathological
significance; ApoE Kochi;
dbSNP:rs121918397).
{ECO:0000269|PubMed:2101409}.
/FTId=VAR_000660.
VARIANT 163 163 R -> P (in LPG; ApoE2 Sendai; decreased
binding to LDL receptor; induces
intraglomerular deposition of ApoE-
containing lipoproteins;
dbSNP:rs121918397).
{ECO:0000269|PubMed:10903326,
ECO:0000269|PubMed:9176854}.
/FTId=VAR_042735.
VARIANT 164 164 K -> E (in HLPP3; ApoE1 Harrisburg;
decreased binding to LDL receptor;
probable dominant negative effect;
decreased in vitro binding to heparin;
dbSNP:rs121918394).
{ECO:0000269|PubMed:7635945}.
/FTId=VAR_000662.
VARIANT 164 164 K -> Q (in HLPP3; ApoE2**;
dbSNP:rs121918394).
/FTId=VAR_000661.
VARIANT 167 167 Missing (in SBHD and FH; also found in
patients with a diagnosis of familial
combined hyperlipidemia).
{ECO:0000269|PubMed:11095479,
ECO:0000269|PubMed:16094309,
ECO:0000269|PubMed:22481068,
ECO:0000269|PubMed:22949395,
ECO:0000269|PubMed:24267230,
ECO:0000269|PubMed:26802169}.
/FTId=VAR_035015.
VARIANT 170 170 A -> P (in ApoE3*; decreased binding to
LDL receptor; dbSNP:rs267606662).
{ECO:0000269|PubMed:2831187,
ECO:0000269|PubMed:6327682}.
/FTId=VAR_000663.
VARIANT 176 176 R -> C (in HLPP3; ApoE2, ApoE2 Fukuoka,
ApoE1 Weisgraber and ApoE3**; ApoE3** is
associated with HLPP3; changed protein
structure; decreased binding to LDLR and
other lipoprotein receptors; decreased in
vitro binding to heparin; no effect on
distribution among plasma lipoproteins;
dbSNP:rs7412).
{ECO:0000269|PubMed:11042151,
ECO:0000269|PubMed:12950167,
ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:2280190,
ECO:0000269|PubMed:3243553,
ECO:0000269|PubMed:7635945,
ECO:0000269|PubMed:7994571,
ECO:0000269|PubMed:8287539,
ECO:0000269|PubMed:8756331}.
/FTId=VAR_000664.
VARIANT 228 317 Missing (in HLPP3; ApoE3 Washington).
{ECO:0000269|PubMed:1361196}.
/FTId=VAR_081136.
VARIANT 242 242 R -> Q (in ApoE2 Fukuoka;
dbSNP:rs267606663).
{ECO:0000269|PubMed:8664327}.
/FTId=VAR_000665.
VARIANT 246 246 R -> C (in ApoE2 Dunedin;
dbSNP:rs121918395).
{ECO:0000269|PubMed:2341812}.
/FTId=VAR_000666.
VARIANT 254 254 V -> E (in ApoE2 WG; dbSNP:rs199768005).
{ECO:0000269|PubMed:8488843}.
/FTId=VAR_000667.
VARIANT 262 263 EE -> KK (in HLPP3; ApoE7 Suita).
{ECO:0000269|PubMed:2738044}.
/FTId=VAR_000668.
VARIANT 269 269 R -> G (in ApoE3 HB; dbSNP:rs267606661).
{ECO:0000269|PubMed:8488843,
ECO:0000269|PubMed:9360638}.
/FTId=VAR_000669.
VARIANT 270 270 L -> E (in ApoE1 HE; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:8488843}.
/FTId=VAR_000670.
VARIANT 292 292 R -> H (in ApoE4 PD; dbSNP:rs121918398).
{ECO:0000269|PubMed:8488843}.
/FTId=VAR_000671.
VARIANT 314 314 S -> R (in ApoE4 HG; dbSNP:rs28931579).
{ECO:0000269|PubMed:8488843}.
/FTId=VAR_000672.
MUTAGEN 79 79 R->T: Changes the plasma lipoprotein
distribution of ApoE4 to the HDL.
{ECO:0000269|PubMed:8071364}.
MUTAGEN 127 127 E->A: No effect on plasma lipoprotein
distribution.
{ECO:0000269|PubMed:8071364}.
MUTAGEN 157 157 S->R: Increased binding to LDL receptor;
when associated with A-167.
{ECO:0000269|PubMed:2831187}.
MUTAGEN 158 158 H->A: Decreased binding to LDL receptor.
{ECO:0000269|PubMed:2831187}.
MUTAGEN 161 161 K->A: Decreased binding to LDL receptor.
{ECO:0000269|PubMed:2831187}.
MUTAGEN 162 162 L->P: Decreased binding to LDL receptor.
{ECO:0000269|PubMed:2831187}.
MUTAGEN 167 167 L->A: Increased binding to LDL receptor;
when associated with R-157.
{ECO:0000269|PubMed:2831187}.
MUTAGEN 168 168 R->A: Decreased binding to LDL receptor.
{ECO:0000269|PubMed:2831187}.
MUTAGEN 172 172 D->A: Restores the LDL receptor binding
activity of ApoE2.
{ECO:0000269|PubMed:8756331}.
MUTAGEN 212 212 T->A: Loss of O-glycosylation.
{ECO:0000269|PubMed:2498325}.
STRAND 22 24 {ECO:0000244|PDB:2KC3}.
HELIX 31 39 {ECO:0000244|PDB:2KC3}.
TURN 40 42 {ECO:0000244|PDB:2KC3}.
HELIX 43 60 {ECO:0000244|PDB:1GS9}.
HELIX 63 70 {ECO:0000244|PDB:1GS9}.
HELIX 73 96 {ECO:0000244|PDB:1GS9}.
TURN 97 99 {ECO:0000244|PDB:1LE4}.
HELIX 106 141 {ECO:0000244|PDB:1GS9}.
TURN 143 145 {ECO:0000244|PDB:1NFN}.
HELIX 149 179 {ECO:0000244|PDB:1GS9}.
TURN 180 182 {ECO:0000244|PDB:1BZ4}.
TURN 187 190 {ECO:0000244|PDB:2KC3}.
HELIX 193 198 {ECO:0000244|PDB:2KC3}.
STRAND 200 202 {ECO:0000244|PDB:2L7B}.
HELIX 209 217 {ECO:0000244|PDB:2L7B}.
HELIX 228 241 {ECO:0000244|PDB:2L7B}.
HELIX 257 283 {ECO:0000244|PDB:2L7B}.
HELIX 286 303 {ECO:0000244|PDB:1OEF}.
STRAND 307 309 {ECO:0000244|PDB:2L7B}.
SEQUENCE 317 AA; 36154 MW; 91AFC04210A30689 CRC64;
MKVLWAALLV TFLAGCQAKV EQAVETEPEP ELRQQTEWQS GQRWELALGR FWDYLRWVQT
LSEQVQEELL SSQVTQELRA LMDETMKELK AYKSELEEQL TPVAEETRAR LSKELQAAQA
RLGADMEDVC GRLVQYRGEV QAMLGQSTEE LRVRLASHLR KLRKRLLRDA DDLQKRLAVY
QAGAREGAER GLSAIRERLG PLVEQGRVRA ATVGSLAGQP LQERAQAWGE RLRARMEEMG
SRTRDRLDEV KEQVAEVRAK LEEQAQQIRL QAEAFQARLK SWFEPLVEDM QRQWAGLVEK
VQAAVGTSAA PVPSDNH


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