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Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I (Apolipoprotein A-I(1-242))]

 APOA1_HUMAN             Reviewed;         267 AA.
P02647; A8K866; Q6LDN9; Q6Q785; Q9UCS8; Q9UCT8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 229.
RecName: Full=Apolipoprotein A-I;
Short=Apo-AI;
Short=ApoA-I;
AltName: Full=Apolipoprotein A1;
Contains:
RecName: Full=Proapolipoprotein A-I;
Short=ProapoA-I;
Contains:
RecName: Full=Truncated apolipoprotein A-I;
AltName: Full=Apolipoprotein A-I(1-242);
Flags: Precursor;
Name=APOA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6406984; DOI=10.1093/nar/11.9.2827;
Shoulders C.C., Kornblihtt A.R., Munro B.S., Baralle F.E.;
"Gene structure of human apolipoprotein A1.";
Nucleic Acids Res. 11:2827-2837(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6304641; DOI=10.1093/nar/11.11.3703;
Cheung P., Chan L.;
"Nucleotide sequence of cloned cDNA of human apolipoprotein A-I.";
Nucleic Acids Res. 11:3703-3715(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6413973; DOI=10.1073/pnas.80.20.6147;
Karathanasis S.K., Zannis V.I., Breslow J.L.;
"Isolation and characterization of the human apolipoprotein A-I
gene.";
Proc. Natl. Acad. Sci. U.S.A. 80:6147-6151(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6207999; DOI=10.1089/dna.1.1984.3.309;
Seilhamer J.J., Protter A.A., Frossard P., Levy-Wilson B.;
"Isolation and DNA sequence of full-length cDNA and of the entire gene
for human apolipoprotein AI -- discovery of a new genetic polymorphism
in the apo AI gene.";
DNA 3:309-317(1984).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6328445; DOI=10.1093/nar/12.9.3917;
Sharpe C.R., Sidoli A., Shelley C.S., Lucero M.A., Shoulders C.C.,
Baralle F.E.;
"Human apolipoproteins AI, AII, CII and CIII. cDNA sequences and mRNA
abundance.";
Nucleic Acids Res. 12:3917-3932(1984).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6198645; DOI=10.1073/pnas.81.1.66;
Law S.W., Brewer H.B. Jr.;
"Nucleotide sequence and the encoded amino acids of human
apolipoprotein A-I mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 81:66-70(1984).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2995392;
Law S.W., Brewer H.B. Jr.;
"Tangier disease. The complete mRNA sequence encoding for preproapo-A-
I.";
J. Biol. Chem. 260:12810-12814(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANT TANGIER).
PubMed=3129297; DOI=10.1111/j.1432-1033.1988.tb14022.x;
Makrides S.C., Ruiz-Opazo N., Hayden M.R., Nussbaum A.L.,
Breslow J.L., Zannis V.I.;
"Sequence and expression of Tangier apoA-I gene.";
Eur. J. Biochem. 173:465-471(1988).
[9]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2673706; DOI=10.1089/dna.1.1989.8.429;
Moguilevsky N., Roobol C., Loriau R., Guillaume J.P., Jacobs P.,
Cravador A., Herzog A., Brouwers L., Scarso A., Gilles P.,
Holmquist L., Carlson L.A., Bollen A.;
"Production of human recombinant proapolipoprotein A-I in Escherichia
coli: purification and biochemical characterization.";
DNA 8:429-436(1989).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-61.
PubMed=15108119; DOI=10.1007/s00439-004-1106-x;
Fullerton S.M., Buchanan A.V., Sonpar V.A., Taylor S.L., Smith J.D.,
Carlson C.S., Salomaa V., Stengaard J.H., Boerwinkle E., Clark A.G.,
Nickerson D.A., Weiss K.M.;
"The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster.";
Hum. Genet. 115:36-56(2004).
[11]
NUCLEOTIDE SEQUENCE [MRNA].
Bollen A., Gobert J., Wuelfert E.;
"Expression of human proapolipoprotein A-1.";
Patent number EP0293357, 30-NOV-1988.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Skeletal muscle;
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).
[16]
PROTEIN SEQUENCE OF 19-27.
PubMed=6409108; DOI=10.1016/0006-291X(83)91772-2;
Brewer H.B. Jr., Fairwell T., Kay L., Meng M., Ronan R., Law S.,
Light J.A.;
"Human plasma proapoA-I: isolation and amino-terminal sequence.";
Biochem. Biophys. Res. Commun. 113:626-632(1983).
[17]
PROTEIN SEQUENCE OF 25-267.
PubMed=164450;
Baker H.N., Gotto A.M. Jr., Jackson R.L.;
"The primary structure of human plasma high density apolipoprotein
glutamine I (ApoA-I). II. The amino acid sequence and alignment of
cyanogen bromide fragments IV, III, and I.";
J. Biol. Chem. 250:2725-2738(1975).
[18]
PROTEIN SEQUENCE OF 25-267.
PubMed=204308; DOI=10.1016/0006-291X(78)91614-5;
Brewer H.B. Jr., Fairwell T., Larue A., Ronan R., Houser A.,
Bronzert T.J.;
"The amino acid sequence of human APOA-I, an apolipoprotein isolated
from high density lipoproteins.";
Biochem. Biophys. Res. Commun. 80:623-630(1978).
[19]
PROTEIN SEQUENCE OF 25-56.
PubMed=3047170; DOI=10.1172/JCI113682;
Yui Y., Aoyama T., Morishita H., Takahashi M., Takatsu Y., Kawai C.;
"Serum prostacyclin stabilizing factor is identical to apolipoprotein
A-I (Apo A-I). A novel function of Apo A-I.";
J. Clin. Invest. 82:803-807(1988).
[20]
PROTEIN SEQUENCE OF 25-50, FUNCTION, AND IDENTIFICATION IN THE SPAP
COMPLEX.
TISSUE=Serum;
PubMed=1909888; DOI=10.1021/bi00101a011;
Aakerloef E., Joernvall H., Slotte H., Pousette A.;
"Identification of apolipoprotein A1 and immunoglobulin as components
of a serum complex that mediates activation of human sperm motility.";
Biochemistry 30:8986-8990(1991).
[21]
PROTEIN SEQUENCE OF 25-48.
PubMed=2506184;
Manjunath P., Marcel Y.L., Uma J., Seidah N.G., Chretien M.,
Chapdelaine A.;
"Apolipoprotein A-I binds to a family of bovine seminal plasma
proteins.";
J. Biol. Chem. 264:16853-16857(1989).
[22]
PROTEIN SEQUENCE OF 25-43.
PubMed=3120314; DOI=10.1126/science.3120314;
Prioli R.P., Ordovas J.M., Rosenberg I., Schaeffer E.J.,
Pereira M.E.A.;
"Similarity of cruzin, an inhibitor of Trypanosoma cruzi
neuraminidase, to high-density lipoprotein.";
Science 238:1417-1419(1987).
[23]
PROTEIN SEQUENCE OF 25-42.
TISSUE=Heart;
PubMed=7895732; DOI=10.1002/elps.11501501209;
Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
"The human myocardial two-dimensional gel protein database: update
1994.";
Electrophoresis 15:1459-1465(1994).
[24]
PROTEIN SEQUENCE OF 25-34.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[25]
PROTEIN SEQUENCE OF 25-33, AND INTERACTION WITH APOA1BP AND CLU.
PubMed=1742316; DOI=10.1016/0005-2760(91)90167-G;
Ehnholm C., Bozas S.E., Tenkanen H., Kirszbaum L., Metso J.,
Murphy B., Walker I.D.;
"The apolipoprotein A-I binding protein of placenta and the SP-40,40
protein of human blood are different proteins which both bind to
apolipoprotein A-I.";
Biochim. Biophys. Acta 1086:255-260(1991).
[26]
PROTEIN SEQUENCE OF 35-64; 70-101; 121-140; 165-173; 185-195 AND
240-263, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[27]
NUCLEOTIDE SEQUENCE [MRNA] OF 118-267.
PubMed=6294659; DOI=10.1073/pnas.79.22.6861;
Breslow J.L., Ross D., McPherson J., Williams H.W., Kurnit D.,
Nussbaum A.L., Karathanasis S.K., Zannis V.I.;
"Isolation and characterization of cDNA clones for human
apolipoprotein A-I.";
Proc. Natl. Acad. Sci. U.S.A. 79:6861-6865(1982).
[28]
PALMITOYLATION.
PubMed=3005308;
Hoeg J.M., Meng M.S., Ronan R., Fairwell T., Brewer H.B. Jr.;
"Human apolipoprotein A-I. Post-translational modification by fatty
acid acylation.";
J. Biol. Chem. 261:3911-3914(1986).
[29]
PROTEOLYTIC PROCESSING.
PubMed=6405383; DOI=10.1073/pnas.80.9.2574;
Zannis V.I., Karathanasis S.K., Keutmann H.T., Goldberger G.,
Breslow J.L.;
"Intracellular and extracellular processing of human apolipoprotein A-
I: secreted apolipoprotein A-I isoprotein 2 is a propeptide.";
Proc. Natl. Acad. Sci. U.S.A. 80:2574-2578(1983).
[30]
GLYCATION AT LYS-263.
PubMed=8261628; DOI=10.1016/0009-8981(93)90165-Z;
Calvo C., Ulloa N., Campos M., Verdugo C., Ayrault-Jarrier M.;
"The preferential site of non-enzymatic glycation of human
apolipoprotein A-I in vivo.";
Clin. Chim. Acta 217:193-198(1993).
[31]
INTERACTION WITH APOA1BP.
PubMed=11991719; DOI=10.1006/geno.2002.6761;
Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A.,
Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G.,
Schmitz G.;
"Cloning and characterization of a novel apolipoprotein A-I-binding
protein, AI-BP, secreted by cells of the kidney proximal tubules in
response to HDL or ApoA-I.";
Genomics 79:693-702(2002).
[32]
INTERACTION WITH SCGB3A2.
PubMed=12847263;
Bin L.H., Nielson L.D., Liu X., Mason R.J., Shu H.B.;
"Identification of uteroglobin-related protein 1 and macrophage
scavenger receptor with collagenous structure as a lung-specific
ligand-receptor pair.";
J. Immunol. 171:924-930(2003).
[33]
MASS SPECTROMETRY, OXIDATION AT MET-110 AND MET-136, AND TISSUE
SPECIFICITY.
PubMed=12576517; DOI=10.1194/jlr.M200256-JLR200;
Pankhurst G., Wang X.L., Wilcken D.E., Baernthaler G., Panzenboeck U.,
Raftery M., Stocker R.;
"Characterization of specifically oxidized apolipoproteins in mildly
oxidized high density lipoprotein.";
J. Lipid Res. 44:349-355(2003).
[34]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12562854; DOI=10.1194/jlr.D200034-JLR200;
Niederkofler E.E., Tubbs K.A., Kiernan U.A., Nedelkov D., Nelson R.W.;
"Novel mass spectrometric immunoassays for the rapid structural
characterization of plasma apolipoproteins.";
J. Lipid Res. 44:630-639(2003).
[35]
INTERACTION WITH NDRG1.
PubMed=15922294; DOI=10.1016/j.bbrc.2005.05.050;
Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C.,
Watts G.F., Kremensky I., Kalaydjieva L.;
"NDRG1 interacts with APO A-I and A-II and is a functional candidate
for the HDL-C QTL on 8q24.";
Biochem. Biophys. Res. Commun. 332:982-992(2005).
[36]
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).
[37]
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).
[38]
CHARACTERIZATION OF VARIANT MILANO CYS-197.
PubMed=24755625; DOI=10.1371/journal.pone.0096150;
Petrlova J., Dalla-Riva J., Morgelin M., Lindahl M., Krupinska E.,
Stenkula K.G., Voss J.C., Lagerstedt J.O.;
"Secondary structure changes in ApoA-I Milano (R173C) are not
accompanied by a decrease in protein stability or solubility.";
PLoS ONE 9:E96150-E96150(2014).
[39]
STRUCTURE BY NMR OF 190-209.
PubMed=8664326; DOI=10.1016/0005-2760(96)00037-9;
Wang G., Treleaven W.D., Cushley R.J.;
"Conformation of human serum apolipoprotein A-I(166-185) in the
presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR
and CD. Evidence for specific peptide-SDS interactions.";
Biochim. Biophys. Acta 1301:174-184(1996).
[40]
X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 67-267.
PubMed=9356442; DOI=10.1073/pnas.94.23.12291;
Borhani D.W., Rogers D.P., Engler J.A., Brouillette C.G.;
"Crystal structure of truncated human apolipoprotein A-I suggests a
lipid-bound conformation.";
Proc. Natl. Acad. Sci. U.S.A. 94:12291-12296(1997).
[41]
DISEASE.
PubMed=8240372; DOI=10.1006/bbrc.1993.2341;
Nakata K., Kobayashi K., Yanagi H., Shimakura Y., Tsuchiya S.,
Arinami T., Hamaguchi H.;
"Autosomal dominant hypoalphalipoproteinemia due to a completely
defective apolipoprotein A-I gene.";
Biochem. Biophys. Res. Commun. 196:950-955(1993).
[42]
DISEASE.
PubMed=8282791; DOI=10.1172/JCI116949;
Ng D.S., Leiter L.A., Vezina C., Connelly P.W., Hegele R.A.;
"Apolipoprotein A-I Q[-2]X causing isolated apolipoprotein A-I
deficiency in a family with analphalipoproteinemia.";
J. Clin. Invest. 93:223-229(1994).
[43]
VARIANT MILANO CYS-197.
PubMed=6401735;
Weisgraber K.H., Rall S.C. Jr., Bersot T.P., Mahley R.W.,
Franceschini G., Sirtori C.R.;
"Apolipoprotein A-IMilano. Detection of normal A-I in affected
subjects and evidence for a cysteine for arginine substitution in the
variant A-I.";
J. Biol. Chem. 258:2508-2513(1983).
[44]
VARIANT TANGIER.
PubMed=6412234; DOI=10.1073/pnas.80.19.6081;
Schmitz G., Assmann G., Rall S.C. Jr., Mahley R.W.;
"Tangier disease: defective recombination of a specific Tangier
apolipoprotein A-I isoform (pro-apo A-I) with high density
lipoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 80:6081-6085(1983).
[45]
VARIANT GIESSEN ARG-167.
PubMed=6489332; DOI=10.1111/j.1432-1033.1984.tb08467.x;
Utermann G., Haas J., Steinmetz A., Paetzold R., Rall S.C. Jr.,
Weisgraber K.H., Mahley R.W.;
"Apolipoprotein A-IGiessen (Pro143-->Arg). A mutant that is defective
in activating lecithin:cholesterol acyltransferase.";
Eur. J. Biochem. 144:325-331(1984).
[46]
VARIANT NORWAY LYS-160.
PubMed=6432779;
Rall S.C. Jr., Weisgraber K.H., Mahley R.W., Ogawa Y., Fielding C.J.,
Utermann G., Haas J., Steinmetz A., Menzel H.J., Assmann G.;
"Abnormal lecithin:cholesterol acyltransferase activation by a human
apolipoprotein A-I variant in which a single lysine residue is
deleted.";
J. Biol. Chem. 259:10063-10070(1984).
[47]
PROTEIN SEQUENCE OF 25-107, AND VARIANT AMYL8 ARG-50.
PubMed=3142462; DOI=10.1016/S0006-291X(88)80909-4;
Nichols W.C., Dwulet F.E., Liepnieks J., Benson M.D.;
"Variant apolipoprotein AI as a major constituent of a human
hereditary amyloid.";
Biochem. Biophys. Res. Commun. 156:762-768(1988).
[48]
VARIANT AMYL8 ARG-50.
PubMed=2123470; DOI=10.1016/0888-7543(90)90288-6;
Nichols W.C., Gregg R.E., Brewer H.B. Jr., Benson M.D.;
"A mutation in apolipoprotein A-I in the Iowa type of familial
amyloidotic polyneuropathy.";
Genomics 8:318-323(1990).
[49]
PROTEIN SEQUENCE OF 25-267, AND VARIANT FUKUOKA LYS-134.
PubMed=2107878; DOI=10.1016/0005-2760(90)90292-6;
Takada Y., Sasaki J., Ogata S., Nakanishi T., Ikehara Y., Arakawa K.;
"Isolation and characterization of human apolipoprotein A-I Fukuoka
(110 Glu-->Lys). A novel apolipoprotein variant.";
Biochim. Biophys. Acta 1043:169-176(1990).
[50]
PROTEIN SEQUENCE OF 25-112, AND VARIANT AMYL8 ARG-84.
PubMed=1502149; DOI=10.1073/pnas.89.16.7389;
Soutar A.K., Hawkins P.N., Vigushin D.M., Tennent G.A., Booth S.E.,
Hutton T., Nguyen O., Totty N.F., Feest T.G., Hsuan J.J., Pepys M.B.;
"Apolipoprotein AI mutation Arg-60 causes autosomal dominant
amyloidosis.";
Proc. Natl. Acad. Sci. U.S.A. 89:7389-7393(1992).
[51]
VARIANT BALTIMORE LEU-34.
PubMed=2108924; DOI=10.1007/BF00195816;
Ladias J.A.A., Kwiterovich P.O. Jr., Smith H.H., Karathanasis S.K.,
Antonarakis S.E.;
"Apolipoprotein A1 Baltimore (Arg-10-->Leu), a new ApoA1 variant.";
Hum. Genet. 84:439-445(1990).
[52]
VARIANTS ARG-27; ARG-28 AND ARG-189.
PubMed=2512329; DOI=10.1172/JCI114355;
von Eckardstein A., Funke H., Henke A., Altland K., Benninghoven A.,
Assmann G., Welp S., Roetrige A., Kock R.;
"Apolipoprotein A-I variants. Naturally occurring substitutions of
proline residues affect plasma concentration of apolipoprotein A-I.";
J. Clin. Invest. 84:1722-1730(1989).
[53]
VARIANTS GLU-113; MET-131; GLY-163; VAL-171 AND LYS-222.
PubMed=2111322;
von Eckardstein A., Funke H., Walter M., Altland K., Benninghoven A.,
Assmann G.;
"Structural analysis of human apolipoprotein A-I variants. Amino acid
substitutions are nonrandomly distributed throughout the
apolipoprotein A-I primary structure.";
J. Biol. Chem. 265:8610-8617(1990).
[54]
VARIANTS HITA AND TSUSHIMA.
PubMed=7918609;
Araki K., Sasaki J., Matsunaga A., Takada Y., Moriyama K., Hidaka K.,
Arakawa K.;
"Characterization of two new human apolipoprotein A-I variants:
apolipoprotein A-I Tsushima (Trp-108-->Arg) and A-I Hita (Ala-
95-->Asp).";
Biochim. Biophys. Acta 1214:272-278(1994).
[55]
VARIANT AMYL8 ARG-50.
PubMed=8208902;
Vigushin D.M., Gough J., Allan D., Alguacil A., Penner B.,
Pettigrew N.M., Quinonez G., Bernstein K., Booth S.E., Booth D.R.,
Soutar A.K., Hawkins P.N., Pepys M.B.;
"Familial nephropathic systemic amyloidosis caused by apolipoprotein
AI variant Arg26.";
Q. J. Med. 87:149-154(1994).
[56]
VARIANT AOITA GLU-180.
PubMed=9514407; DOI=10.1161/01.ATV.18.3.389;
Huang W., Sasaki J., Matsunaga A., Nanimatsu H., Moriyama K., Han H.,
Kugi M., Koga T., Yamaguchi K., Arakawa K.;
"A novel homozygous missense mutation in the apo A-I gene with apo A-I
deficiency.";
Arterioscler. Thromb. Vasc. Biol. 18:389-396(1998).
[57]
VARIANT ZARAGOZA ARG-168.
Recalde D., Cenarro A., Civeira F., Pocovi M.;
"Apo A-I Zaragoza(L144R): a novel mutation in the apolipoprotein A-I
gene associated with familial hypoalphalipoproteinemia.";
Hum. Mutat. 11:416-416(1998).
[58]
VARIANT ILE-92.
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).
[59]
VARIANT ILE-92, 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).
[60]
VARIANT BOSTON SER-173.
PubMed=26073399; DOI=10.1016/j.jacl.2015.02.005;
Anthanont P., Asztalos B.F., Polisecki E., Zachariah B.,
Schaefer E.J.;
"Case report: A novel apolipoprotein A-I missense mutation apoA-I
(Arg149Ser)Boston associated with decreased lecithin-cholesterol
acyltransferase activation and cellular cholesterol efflux.";
J. Clin. Lipidol. 9:390-395(2015).
-!- FUNCTION: Participates in the reverse transport of cholesterol
from tissues to the liver for excretion by promoting cholesterol
efflux from tissues and by acting as a cofactor for the lecithin
cholesterol acyltransferase (LCAT). As part of the SPAP complex,
activates spermatozoa motility. {ECO:0000269|PubMed:1909888}.
-!- SUBUNIT: Interacts with APOA1BP and CLU (PubMed:1742316,
PubMed:11991719). Component of a sperm activating protein complex
(SPAP), consisting of APOA1, an immunoglobulin heavy chain, an
immunoglobulin light chain and albumin (PubMed:1909888). Interacts
with NDRG1 (PubMed:15922294). Interacts with SCGB3A2
(PubMed:12847263). {ECO:0000269|PubMed:11991719,
ECO:0000269|PubMed:12847263, ECO:0000269|PubMed:15922294,
ECO:0000269|PubMed:1742316, ECO:0000269|PubMed:1909888}.
-!- INTERACTION:
Self; NbExp=21; IntAct=EBI-701692, EBI-701692;
O95477:ABCA1; NbExp=4; IntAct=EBI-701692, EBI-784112;
P05067:APP; NbExp=5; IntAct=EBI-701692, EBI-77613;
Q96DZ9:CMTM5; NbExp=3; IntAct=EBI-701692, EBI-2548702;
Q96DZ9-2:CMTM5; NbExp=7; IntAct=EBI-701692, EBI-11522780;
P02671:FGA; NbExp=2; IntAct=EBI-701692, EBI-348571;
P00738:HP; NbExp=3; IntAct=EBI-701692, EBI-1220767;
P04180:LCAT; NbExp=2; IntAct=EBI-701692, EBI-9104464;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Major protein of plasma HDL, also found in
chylomicrons. Synthesized in the liver and small intestine. The
oxidized form at Met-110 and Met-136 is increased in individuals
with increased risk for coronary artery disease, such as in
carrier of the eNOSa/b genotype and exposure to cigarette smoking.
It is also present in increased levels in aortic lesions relative
to native ApoA-I and increased levels are seen with increasing
severity of disease. {ECO:0000269|PubMed:12576517}.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- PTM: Palmitoylated. {ECO:0000269|PubMed:3005308}.
-!- PTM: Phosphorylation sites are present in the extracellular
medium.
-!- MASS SPECTROMETRY: Mass=28081; Method=Electrospray; Range=25-267;
Note=Without methionine sulfoxide.;
Evidence={ECO:0000269|PubMed:12576517};
-!- MASS SPECTROMETRY: Mass=28098; Method=Electrospray; Range=25-267;
Note=With 1 methionine sulfoxide, oxidation at Met-110.;
Evidence={ECO:0000269|PubMed:12576517};
-!- MASS SPECTROMETRY: Mass=28095; Method=Electrospray; Range=25-267;
Note=With 1 methionine sulfoxide, oxidation at Met-136.;
Evidence={ECO:0000269|PubMed:12576517};
-!- MASS SPECTROMETRY: Mass=28114; Method=Electrospray; Range=25-267;
Note=With 2 methionine sulfoxides, oxidation at Met-110 and Met-
136.; Evidence={ECO:0000269|PubMed:12576517};
-!- POLYMORPHISM: Genetic variations in APOA1 can result in APOA1
deficiency and are associated with low levels of HDL cholesterol
[MIM:107680]. {ECO:0000305}.
-!- DISEASE: High density lipoprotein deficiency 2 (HDLD2)
[MIM:604091]: Inherited as autosomal dominant trait. It is
characterized by moderately low HDL cholesterol, predilection
toward premature coronary artery disease (CAD) and a reduction in
cellular cholesterol efflux. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: High density lipoprotein deficiency 1 (HDLD1)
[MIM:205400]: Recessive disorder characterized by absence of high
density lipoprotein (HDL) cholesterol from plasma, accumulation of
cholesteryl esters, premature coronary artery disease (CAD),
hepatosplenomegaly, recurrent peripheral neuropathy and
progressive muscle wasting and weakness. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Note=APOA1 mutations may be involved in the pathogenesis
of amyloid polyneuropathy-nephropathy Iowa type, also known as
amyloidosis van Allen type or familial amyloid polyneuropathy type
III (PubMed:3142462 and PubMed:2123470). The clinical picture is
dominated by neuropathy in the early stages of the disease and
nephropathy late in the course. Death is due in most cases to
renal amyloidosis.
-!- DISEASE: Amyloidosis 8 (AMYL8) [MIM:105200]: A form of hereditary
generalized amyloidosis. Clinical features include extensive
visceral amyloid deposits, renal amyloidosis resulting in
nephrotic syndrome, arterial hypertension, hepatosplenomegaly,
cholestasis, petechial skin rash. There is no involvement of the
nervous system. {ECO:0000269|PubMed:1502149,
ECO:0000269|PubMed:2123470, ECO:0000269|PubMed:3142462,
ECO:0000269|PubMed:8208902}. Note=The disease is 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=APOA1";
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EMBL; J00098; AAB59514.1; -; Genomic_DNA.
EMBL; X01038; CAA25519.1; -; Genomic_DNA.
EMBL; X02162; CAA26097.1; -; mRNA.
EMBL; X00566; CAA25232.1; -; mRNA.
EMBL; M11791; AAA35545.1; -; mRNA.
EMBL; X07496; CAA30377.1; -; Genomic_DNA.
EMBL; M27875; AAA62829.1; -; mRNA.
EMBL; M29068; AAA51747.1; -; mRNA.
EMBL; AY422952; AAQ91811.1; -; Genomic_DNA.
EMBL; AY555191; AAS68227.1; -; Genomic_DNA.
EMBL; A14829; CAA01198.1; -; mRNA.
EMBL; AK292231; BAF84920.1; -; mRNA.
EMBL; EF444948; ACA05932.1; -; Genomic_DNA.
EMBL; EF444948; ACA05933.1; -; Genomic_DNA.
EMBL; EF444948; ACA05934.1; -; Genomic_DNA.
EMBL; EF444948; ACA05935.1; -; Genomic_DNA.
EMBL; EF444948; ACA05936.1; -; Genomic_DNA.
EMBL; CH471065; EAW67274.1; -; Genomic_DNA.
EMBL; BC005380; AAH05380.1; -; mRNA.
EMBL; BC110286; AAI10287.1; -; mRNA.
CCDS; CCDS8378.1; -.
PIR; A90947; LPHUA1.
RefSeq; NP_000030.1; NM_000039.2.
RefSeq; NP_001304946.1; NM_001318017.1.
RefSeq; NP_001304947.1; NM_001318018.1.
RefSeq; NP_001304950.1; NM_001318021.1.
UniGene; Hs.93194; -.
PDB; 1AV1; X-ray; 4.00 A; A/B/C/D=68-267.
PDB; 1GW3; NMR; -; A=166-211.
PDB; 1GW4; NMR; -; A=166-211.
PDB; 1ODP; NMR; -; A=190-209.
PDB; 1ODQ; NMR; -; A=190-209.
PDB; 1ODR; NMR; -; A=190-209.
PDB; 2A01; X-ray; 2.40 A; A/B/C=25-267.
PDB; 2MSC; NMR; -; A/C=68-265.
PDB; 2MSD; NMR; -; A/C=68-265.
PDB; 2MSE; NMR; -; A/C=68-265.
PDB; 2N5E; NMR; -; A/B=79-267.
PDB; 3K2S; X-ray; -; A/B=25-267.
PDB; 3R2P; X-ray; 2.20 A; A=25-208.
PDB; 4V6M; EM; 7.10 A; A0/A1=68-267.
PDBsum; 1AV1; -.
PDBsum; 1GW3; -.
PDBsum; 1GW4; -.
PDBsum; 1ODP; -.
PDBsum; 1ODQ; -.
PDBsum; 1ODR; -.
PDBsum; 2A01; -.
PDBsum; 2MSC; -.
PDBsum; 2MSD; -.
PDBsum; 2MSE; -.
PDBsum; 2N5E; -.
PDBsum; 3K2S; -.
PDBsum; 3R2P; -.
PDBsum; 4V6M; -.
ProteinModelPortal; P02647; -.
SMR; P02647; -.
BioGrid; 106832; 90.
CORUM; P02647; -.
DIP; DIP-29619N; -.
IntAct; P02647; 70.
MINT; MINT-5000866; -.
STRING; 9606.ENSP00000236850; -.
ChEMBL; CHEMBL5984; -.
iPTMnet; P02647; -.
PhosphoSitePlus; P02647; -.
BioMuta; APOA1; -.
DMDM; 113992; -.
DOSAC-COBS-2DPAGE; P02647; -.
OGP; P02647; -.
REPRODUCTION-2DPAGE; IPI00021841; -.
REPRODUCTION-2DPAGE; P02647; -.
SWISS-2DPAGE; P02647; -.
UCD-2DPAGE; P02647; -.
EPD; P02647; -.
MaxQB; P02647; -.
PaxDb; P02647; -.
PeptideAtlas; P02647; -.
PRIDE; P02647; -.
DNASU; 335; -.
Ensembl; ENST00000236850; ENSP00000236850; ENSG00000118137.
Ensembl; ENST00000359492; ENSP00000352471; ENSG00000118137.
Ensembl; ENST00000375320; ENSP00000364469; ENSG00000118137.
Ensembl; ENST00000375323; ENSP00000364472; ENSG00000118137.
GeneID; 335; -.
KEGG; hsa:335; -.
UCSC; uc001ppv.2; human.
CTD; 335; -.
DisGeNET; 335; -.
EuPathDB; HostDB:ENSG00000118137.9; -.
GeneCards; APOA1; -.
HGNC; HGNC:600; APOA1.
HPA; CAB016778; -.
HPA; HPA046715; -.
MalaCards; APOA1; -.
MIM; 105200; phenotype.
MIM; 107680; gene+phenotype.
MIM; 205400; phenotype.
MIM; 604091; phenotype.
neXtProt; NX_P02647; -.
OpenTargets; ENSG00000118137; -.
Orphanet; 425; Apolipoprotein A-I deficiency.
Orphanet; 93560; Familial renal amyloidosis due to Apolipoprotein AI variant.
Orphanet; 314701; Primary systemic amyloidosis.
PharmGKB; PA49; -.
eggNOG; ENOG410IWKR; Eukaryota.
eggNOG; ENOG410YGQ6; LUCA.
GeneTree; ENSGT00530000063081; -.
HOGENOM; HOG000033998; -.
HOVERGEN; HBG105708; -.
InParanoid; P02647; -.
KO; K08757; -.
OMA; KDFATVY; -.
OrthoDB; EOG091G0IA5; -.
PhylomeDB; P02647; -.
TreeFam; TF334458; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
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-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-8963888; Chylomicron assembly.
Reactome; R-HSA-8963896; HDL assembly.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-8964011; HDL clearance.
Reactome; R-HSA-8964058; HDL remodeling.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
Reactome; R-HSA-977225; Amyloid fiber formation.
SIGNOR; P02647; -.
ChiTaRS; APOA1; human.
EvolutionaryTrace; P02647; -.
GeneWiki; Apolipoprotein_A1; -.
GenomeRNAi; 335; -.
PMAP-CutDB; P02647; -.
PRO; PR:P02647; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000118137; -.
CleanEx; HS_APOA1; -.
ExpressionAtlas; P02647; baseline and differential.
Genevisible; P02647; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0042627; C:chylomicron; IBA:GO_Central.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0034365; C:discoidal high-density lipoprotein particle; IEA:Ensembl.
GO; GO:0005769; C:early endosome; TAS:Reactome.
GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
GO; GO:0034362; C:low-density lipoprotein particle; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0001540; F:amyloid-beta binding; IDA:BHF-UCL.
GO; GO:0034191; F:apolipoprotein A-I receptor binding; IPI:BHF-UCL.
GO; GO:0034190; F:apolipoprotein receptor binding; IPI:BHF-UCL.
GO; GO:0045499; F:chemorepellent activity; IDA:UniProtKB.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0017127; F:cholesterol transporter activity; IMP:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0031072; F:heat shock protein binding; IPI:CAFA.
GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0070653; F:high-density lipoprotein particle receptor binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0055102; F:lipase inhibitor activity; IEA:Ensembl.
GO; GO:0031210; F:phosphatidylcholine binding; IBA:GO_Central.
GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IDA:BHF-UCL.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0005548; F:phospholipid transporter activity; IEA:Ensembl.
GO; GO:0030325; P:adrenal gland development; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0043534; P:blood vessel endothelial cell migration; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0006695; P:cholesterol biosynthetic process; IBA:GO_Central.
GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0070508; P:cholesterol import; IMP:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IMP:BHF-UCL.
GO; GO:0030301; P:cholesterol transport; IDA:MGI.
GO; GO:0034378; P:chylomicron assembly; TAS:Reactome.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0008211; P:glucocorticoid metabolic process; IEA:Ensembl.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IDA:BHF-UCL.
GO; GO:0034384; P:high-density lipoprotein particle clearance; TAS:Reactome.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:BHF-UCL.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0019915; P:lipid storage; IEA:Ensembl.
GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0042157; P:lipoprotein metabolic process; IBA:GO_Central.
GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
GO; GO:0060354; P:negative regulation of cell adhesion molecule production; IDA:BHF-UCL.
GO; GO:0002740; P:negative regulation of cytokine secretion involved in immune response; IDA:BHF-UCL.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IDA:BHF-UCL.
GO; GO:0050713; P:negative regulation of interleukin-1 beta secretion; IDA:BHF-UCL.
GO; GO:0060192; P:negative regulation of lipase activity; IEA:Ensembl.
GO; GO:0060761; P:negative regulation of response to cytokine stimulus; IDA:BHF-UCL.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0010903; P:negative regulation of very-low-density lipoprotein particle remodeling; IDA:BHF-UCL.
GO; GO:0031102; P:neuron projection regeneration; IBA:GO_Central.
GO; GO:0018206; P:peptidyl-methionine modification; IDA:UniProtKB.
GO; GO:0014012; P:peripheral nervous system axon regeneration; IEA:Ensembl.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:BHF-UCL.
GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
GO; GO:0055091; P:phospholipid homeostasis; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0010873; P:positive regulation of cholesterol esterification; IDA:BHF-UCL.
GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IBA:GO_Central.
GO; GO:0051345; P:positive regulation of hydrolase activity; IDA:BHF-UCL.
GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IBA:GO_Central.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IBA:GO_Central.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0018158; P:protein oxidation; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IDA:BHF-UCL.
GO; GO:0030300; P:regulation of intestinal cholesterol absorption; IBA:GO_Central.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0019433; P:triglyceride catabolic process; IBA:GO_Central.
GO; GO:0070328; P:triglyceride homeostasis; IDA:BHF-UCL.
GO; GO:0051180; P:vitamin transport; IMP:AgBase.
InterPro; IPR000074; ApoA_E.
Pfam; PF01442; Apolipoprotein; 1.
1: Evidence at protein level;
3D-structure; Amyloid; Amyloidosis; Atherosclerosis;
Cholesterol metabolism; Complete proteome; Direct protein sequencing;
Disease mutation; Glycation; Glycoprotein; HDL; Lipid metabolism;
Lipid transport; Lipoprotein; Neuropathy; Oxidation; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
Signal; Steroid metabolism; Sterol metabolism; Transport.
SIGNAL 1 18 {ECO:0000269|PubMed:6328445,
ECO:0000269|PubMed:6409108}.
CHAIN 19 267 Proapolipoprotein A-I.
/FTId=PRO_0000425323.
CHAIN 25 267 Apolipoprotein A-I.
/FTId=PRO_0000001939.
CHAIN 25 266 Truncated apolipoprotein A-I.
/FTId=PRO_0000001940.
REPEAT 68 89 1.
REPEAT 90 111 2.
REPEAT 112 122 3; half-length.
REPEAT 123 144 4.
REPEAT 145 166 5.
REPEAT 167 188 6.
REPEAT 189 210 7.
REPEAT 211 232 8.
REPEAT 233 243 9; half-length.
REPEAT 244 267 10.
REGION 68 267 10 X approximate tandem repeats.
MOD_RES 110 110 Methionine sulfoxide.
{ECO:0000269|PubMed:12576517}.
MOD_RES 136 136 Methionine sulfoxide.
{ECO:0000269|PubMed:12576517}.
CARBOHYD 263 263 N-linked (Glc) (glycation) lysine.
VARIANT 27 27 P -> H (in Munster-3C;
dbSNP:rs121912720).
/FTId=VAR_000605.
VARIANT 27 27 P -> R (in dbSNP:rs121912720).
{ECO:0000269|PubMed:2512329}.
/FTId=VAR_000606.
VARIANT 28 28 P -> R (in Munster-3B;
dbSNP:rs121912721).
{ECO:0000269|PubMed:2512329}.
/FTId=VAR_000607.
VARIANT 34 34 R -> L (in Baltimore; dbSNP:rs28929476).
{ECO:0000269|PubMed:2108924}.
/FTId=VAR_000608.
VARIANT 50 50 G -> R (in AMYL8; also found in a family
with amyloid polyneuropathy-nephropathy
Iowa; dbSNP:rs28931574).
{ECO:0000269|PubMed:2123470,
ECO:0000269|PubMed:3142462,
ECO:0000269|PubMed:8208902}.
/FTId=VAR_000609.
VARIANT 61 61 A -> T (in dbSNP:rs12718465).
{ECO:0000269|PubMed:15108119}.
/FTId=VAR_025445.
VARIANT 84 84 L -> R (in AMYL8; dbSNP:rs121912724).
{ECO:0000269|PubMed:1502149}.
/FTId=VAR_000610.
VARIANT 92 92 T -> I (polymorphism; confirmed at
protein level; dbSNP:rs766422306).
{ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:22028381}.
/FTId=VAR_017017.
VARIANT 113 113 D -> E (in dbSNP:rs150243849).
{ECO:0000269|PubMed:2111322}.
/FTId=VAR_000611.
VARIANT 119 119 A -> D (in Hita).
/FTId=VAR_000612.
VARIANT 126 126 D -> H (in dbSNP:rs5077).
/FTId=VAR_016189.
VARIANT 127 127 D -> N (in Munster-3A).
/FTId=VAR_000613.
VARIANT 131 131 K -> M (in dbSNP:rs4882).
{ECO:0000269|PubMed:2111322}.
/FTId=VAR_000615.
VARIANT 131 131 Missing (in Marburg/Munster-2).
/FTId=VAR_000614.
VARIANT 132 132 W -> R (in Tsushima).
/FTId=VAR_000616.
VARIANT 134 134 E -> K (in Fukuoka).
{ECO:0000269|PubMed:2107878}.
/FTId=VAR_000617.
VARIANT 160 160 E -> K (in Norway; dbSNP:rs121912718).
{ECO:0000269|PubMed:6432779}.
/FTId=VAR_000618.
VARIANT 163 163 E -> G (in dbSNP:rs758509542).
{ECO:0000269|PubMed:2111322}.
/FTId=VAR_000619.
VARIANT 167 167 P -> R (in Giessen; dbSNP:rs121912719).
{ECO:0000269|PubMed:6489332}.
/FTId=VAR_000620.
VARIANT 168 168 L -> R (in Zaragoza).
{ECO:0000269|Ref.57}.
/FTId=VAR_000621.
VARIANT 171 171 E -> V. {ECO:0000269|PubMed:2111322}.
/FTId=VAR_000622.
VARIANT 173 173 R -> S (in Boston; no evidence of
association with premature coronary heart
disease; associated with decreased levels
of HDL cholesterol; associated with
decreased serum cellular cholesterol
efflux; associated with decreased
lecithin-cholesterol acyltransferase
(LCAT) activity).
{ECO:0000269|PubMed:26073399}.
/FTId=VAR_074073.
VARIANT 180 180 V -> E (in Oita; 60% of normal apoA-I and
normal HDL cholesterol levels; rapidly
cleared from plasma; dbSNP:rs121912727).
{ECO:0000269|PubMed:9514407}.
/FTId=VAR_021362.
VARIANT 184 184 R -> P (in dbSNP:rs5078).
/FTId=VAR_014609.
VARIANT 189 189 P -> R (in dbSNP:rs121912722).
{ECO:0000269|PubMed:2512329}.
/FTId=VAR_000623.
VARIANT 197 197 R -> C (in Milano; no evidence of
association with premature vascular
disease; associated with decreased HDL
levels and moderate increase in
triglycerides; allows the formation of
disulfide-linked homodimers via the
introduced cysteine; assembles properly
in HDL; alters protein structure; has no
tendency to form fibrils and aggregates;
dbSNP:rs28931573).
{ECO:0000269|PubMed:24755625,
ECO:0000269|PubMed:6401735}.
/FTId=VAR_000624.
VARIANT 222 222 E -> K (in Munster-4; dbSNP:rs121912717).
{ECO:0000269|PubMed:2111322}.
/FTId=VAR_000625.
CONFLICT 32 32 W -> P (in Ref. 25; AA sequence).
{ECO:0000305}.
HELIX 33 42 {ECO:0000244|PDB:3R2P}.
HELIX 45 59 {ECO:0000244|PDB:3R2P}.
HELIX 61 65 {ECO:0000244|PDB:3R2P}.
STRAND 69 73 {ECO:0000244|PDB:2A01}.
HELIX 80 88 {ECO:0000244|PDB:3R2P}.
HELIX 93 158 {ECO:0000244|PDB:3R2P}.
TURN 159 164 {ECO:0000244|PDB:3R2P}.
HELIX 166 203 {ECO:0000244|PDB:3R2P}.
TURN 212 214 {ECO:0000244|PDB:2A01}.
STRAND 215 217 {ECO:0000244|PDB:2A01}.
HELIX 220 237 {ECO:0000244|PDB:2A01}.
STRAND 238 240 {ECO:0000244|PDB:2A01}.
HELIX 243 266 {ECO:0000244|PDB:2A01}.
SEQUENCE 267 AA; 30778 MW; 1A28B8366E620310 CRC64;
MKAAVLTLAV LFLTGSQARH FWQQDEPPQS PWDRVKDLAT VYVDVLKDSG RDYVSQFEGS
ALGKQLNLKL LDNWDSVTST FSKLREQLGP VTQEFWDNLE KETEGLRQEM SKDLEEVKAK
VQPYLDDFQK KWQEEMELYR QKVEPLRAEL QEGARQKLHE LQEKLSPLGE EMRDRARAHV
DALRTHLAPY SDELRQRLAA RLEALKENGG ARLAEYHAKA TEHLSTLSEK AKPALEDLRQ
GLLPVLESFK VSFLSALEEY TKKLNTQ


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