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Phospholipid-transporting ATPase ABCA1 (EC 7.6.2.1) (ATP-binding cassette sub-family A member 1) (ATP-binding cassette transporter 1) (ABC-1) (ATP-binding cassette 1) (Cholesterol efflux regulatory protein)

 ABCA1_HUMAN             Reviewed;        2261 AA.
O95477; Q5VX33; Q96S56; Q96T85; Q9NQV4; Q9UN06; Q9UN07; Q9UN08; Q9UN09;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
26-FEB-2020, entry version 212.
RecName: Full=Phospholipid-transporting ATPase ABCA1 {ECO:0000305};
EC=7.6.2.1 {ECO:0000269|PubMed:24097981};
AltName: Full=ATP-binding cassette sub-family A member 1;
AltName: Full=ATP-binding cassette transporter 1;
Short=ABC-1;
Short=ATP-binding cassette 1;
AltName: Full=Cholesterol efflux regulatory protein;
Name=ABCA1 {ECO:0000312|HGNC:HGNC:29}; Synonyms=ABC1, CERP;
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 / MRNA], AND VARIANT ARG-1587.
PubMed=10884428; DOI=10.1073/pnas.97.14.7987;
Santamarina-Fojo S., Peterson K.M., Knapper C.L., Qiu Y., Freeman L.A.,
Cheng J.-F., Osorio J., Remaley A.T., Yang X.-P., Haudenschild C.C.,
Prades C., Chimini G., Blackmon E.E., Francois T.L., Duverger N.,
Rubin E.M., Rosier M., Denefle P., Fredrickson D.S., Brewer H.B. Jr.;
"Complete genomic sequence of the human ABCA1 gene: analysis of the human
and mouse ATP-binding cassette A promoter.";
Proc. Natl. Acad. Sci. U.S.A. 97:7987-7992(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-1587.
TISSUE=Skin;
Schwartz K., Lawn R.M., Wade D.P.;
"ABCA1 gene expression and apoA-I-mediated cholesterol efflux are regulated
by LXR.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-1587.
PubMed=11352567; DOI=10.1006/geno.2000.6467;
Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.;
"Human and mouse ABCA1 comparative sequencing and transgenesis studies
revealing novel regulatory sequences.";
Genomics 73:66-76(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Tanaka A.R., Abe-Dohmae S., Arakawa R., Sadanami K., Kidera A., Kioka N.,
Amachi T., Yokoyama S., Ueda K.;
"A new topological model of functional human ABCA1-signal peptide cleavage
and glycosylation of a large extracellular domain.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-2261, AND VARIANTS THR-1555; ARG-1587;
PRO-1648 AND PRO-2168.
PubMed=10092505; DOI=10.1006/bbrc.1999.0406;
Langmann T., Klucken J., Reil M., Liebisch G., Luciani M.-F., Chimini G.,
Kaminski W.E., Schmitz G.;
"Molecular cloning of the human ATP-binding cassette transporter 1 (hABC1):
evidence for sterol-dependent regulation in macrophages.";
Biochem. Biophys. Res. Commun. 257:29-33(1999).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 21-2261, AND VARIANTS THR-1555;
ARG-1587; PRO-1648 AND PRO-2168.
PubMed=10431238; DOI=10.1038/11921;
Rust S., Rosier M., Funke H., Real J., Amoura Z., Piette J.-C.,
Deleuze J.-F., Brewer H.B. Jr., Duverger N., Denefle P., Assmann G.;
"Tangier disease is caused by mutations in the gene encoding ATP-binding
cassette transporter 1.";
Nat. Genet. 22:352-355(1999).
[8]
PHOSPHORYLATION AT SER-1042 AND SER-2054.
PubMed=12196520; DOI=10.1074/jbc.m204923200;
See R.H., Caday-Malcolm R.A., Singaraja R.R., Zhou S., Silverston A.,
Huber M.T., Moran J., James E.R., Janoo R., Savill J.M., Rigot V.,
Zhang L.H., Wang M., Chimini G., Wellington C.L., Tafuri S.R., Hayden M.R.;
"Protein kinase A site-specific phosphorylation regulates ATP-binding
cassette A1 (ABCA1)-mediated phospholipid efflux.";
J. Biol. Chem. 277:41835-41842(2002).
[9]
REPRESSION BY ZNF202.
PubMed=11279031; DOI=10.1074/jbc.m100218200;
Porsch-Oezcueruemez M., Langmann T., Heimerl S., Borsukova H.,
Kaminski W.E., Drobnik W., Honer C., Schumacher C., Schmitz G.;
"The zinc finger protein 202 (ZNF202) is a transcriptional repressor of ATP
binding cassette transporter A1 (ABCA1) and ABCG1 gene expression and a
modulator of cellular lipid efflux.";
J. Biol. Chem. 276:12427-12433(2001).
[10]
INDUCTION BY LPS.
PubMed=12032171;
Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.;
"Bacterial lipopolysaccharide induces expression of ABCA1 but not ABCG1 via
an LXR-independent pathway.";
J. Lipid Res. 43:952-959(2002).
[11]
INTERACTION WITH MEGF10.
PubMed=17205124; DOI=10.1371/journal.pone.0000120;
Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
Zhou Z., Chimini G.;
"Cooperation between engulfment receptors: the case of ABCA1 and MEGF10.";
PLoS ONE 1:E120-E120(2006).
[12]
REVIEW ON VARIANTS.
PubMed=12763760; DOI=10.1161/01.atv.0000078520.89539.77;
Singaraja R.R., Brunham L.R., Visscher H., Kastelein J.J.P., Hayden M.R.;
"Efflux and atherosclerosis: the clinical and biochemical impact of
variations in the ABCA1 gene.";
Arterioscler. Thromb. Vasc. Biol. 23:1322-1332(2003).
[13]
POLYMORPHISM, AND INVOLVEMENT IN HDLCQ13.
PubMed=18354102; DOI=10.1056/nejmoa0706728;
Kathiresan S., Melander O., Anevski D., Guiducci C., Burtt N.P., Roos C.,
Hirschhorn J.N., Berglund G., Hedblad B., Groop L., Altshuler D.M.,
Newton-Cheh C., Orho-Melander M.;
"Polymorphisms associated with cholesterol and risk of cardiovascular
events.";
N. Engl. J. Med. 358:1240-1249(2008).
[14]
PALMITOYLATION AT CYS-3; CYS-23; CYS-1110 AND CYS-1111, AND SUBCELLULAR
LOCATION.
PubMed=19556522; DOI=10.1161/circresaha.108.193011;
Singaraja R.R., Kang M.H., Vaid K., Sanders S.S., Vilas G.L.,
Arstikaitis P., Coutinho J., Drisdel R.C., El-Husseini Ael D., Green W.N.,
Berthiaume L., Hayden M.R.;
"Palmitoylation of ATP-binding cassette transporter A1 is essential for its
trafficking and function.";
Circ. Res. 105:138-147(2009).
[15]
DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
PubMed=19258317; DOI=10.1074/jbc.m900580200;
Hozoji M., Kimura Y., Kioka N., Ueda K.;
"Formation of two intramolecular disulfide bonds is necessary for ApoA-I-
dependent cholesterol efflux mediated by ABCA1.";
J. Biol. Chem. 284:11293-11300(2009).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98 AND ASN-244.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple
enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[17]
CATALYTIC ACTIVITY, ACTIVITY REGULATION, MUTAGENESIS OF SER-100; PHE-593;
LYS-939; THR-1512 AND LYS-1952, FUNCTION, VARIANTS HDLD1 SER-590; ILE-929;
SER-935; ARG-1477 AND TRP-2081, CHARACTERIZATION OF VARIANTS HDLD1 SER-590;
ILE-929; SER-935; ARG-1477 AND TRP-2081, VARIANT HDLD2 LEU-2150,
CHARACTERIZATION OF VARIANT HDLD2 LEU-2150, AND SUBCELLULAR LOCATION.
PubMed=24097981; DOI=10.1074/jbc.m113.508812;
Quazi F., Molday R.S.;
"Differential phospholipid substrates and directional transport by ATP-
binding cassette proteins ABCA1, ABCA7, and ABCA4 and disease-causing
mutants.";
J. Biol. Chem. 288:34414-34426(2013).
[18]
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).
[19]
FUNCTION, INTERACTION WITH APOE, AND CHARACTERIZATION OF VARIANT HDLD1
ARG-1477.
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).
[20]
VARIANTS HDLD2 THR-1091 AND 1893-GLU-ASP-1894 DEL, AND FUNCTION.
PubMed=10533863; DOI=10.1016/s0140-6736(99)07026-9;
Marcil M., Brooks-Wilson A., Clee S.M., Roomp K., Zhang L.-H., Yu L.,
Collins J.A., van Dam M., Molhuizen H.O.F., Loubser O., Ouellette B.F.F.,
Sensen C.W., Fichter K., Mott S., Denis M., Boucher B., Pimstone S.,
Genest J. Jr., Kastelein J.J.P., Hayden M.R.;
"Mutations in the ABC1 gene in familial HDL deficiency with defective
cholesterol efflux.";
Lancet 354:1341-1346(1999).
[21]
VARIANTS HDLD1 ARG-597 AND ARG-1477, AND VARIANT HDLD2 LEU-693 DEL.
PubMed=10431236; DOI=10.1038/11905;
Brooks-Wilson A., Marcil M., Clee S.M., Zhang L.-H., Roomp K., van Dam M.,
Yu L., Brewer C., Collins J.A., Molhuizen H.O.F., Loubser O.,
Ouelette B.F.F., Fichter K., Ashbourne-Excoffon K.J.D., Sensen C.W.,
Scherer S., Mott S., Denis M., Martindale D., Frohlich J., Morgan K.,
Koop B., Pimstone S., Kastelein J.J.P., Hayden M.R.;
"Mutations in ABC1 in Tangier disease and familial high-density lipoprotein
deficiency.";
Nat. Genet. 22:336-345(1999).
[22]
VARIANTS HDLD1 SER-590; SER-935 AND VAL-937, AND VARIANTS ALA-399 AND
MET-883.
PubMed=10431237; DOI=10.1038/11914;
Bodzioch M., Orso E., Klucken J., Langmann T., Boettcher A., Diederich W.,
Drobnik W., Barlage S., Buechler C., Porsch-Oezcueruemez M., Kaminski W.E.,
Hahmann H.W., Oette K., Rothe G., Aslanidis C., Lackner K.J., Schmitz G.;
"The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier
disease.";
Nat. Genet. 22:347-351(1999).
[23]
VARIANTS HDLD1 ARG-597; ILE-929 AND ARG-1477, AND VARIANTS HDLD2 LEU-693
DEL; THR-1091; 1893-GLU-ASP-1894 DEL AND LEU-2150.
PubMed=11086027; DOI=10.1172/jci10727;
Clee S.M., Kastelein J.J.P., van Dam M., Marcil M., Roomp K., Zwarts K.Y.,
Collins J.A., Roelants R., Tamasawa N., Stulc T., Suda T., Ceska R.,
Boucher B., Rondeau C., DeSouich C., Brooks-Wilson A., Molhuizen H.O.F.,
Frohlich J., Genest J. Jr., Hayden M.R.;
"Age and residual cholesterol efflux affect HDL cholesterol levels and
coronary artery disease in ABCA1 heterozygotes.";
J. Clin. Invest. 106:1263-1270(2000).
[24]
VARIANTS HDLD1 ASN-1289 AND HIS-1800.
PubMed=10706591;
Brousseau M.E., Schaefer E.J., Dupuis J., Eustace B., Van Eerdewegh P.,
Goldkamp A.L., Thurston L.M., FitzGerald M.G., Yasek-McKenna D.,
O'Neill G., Eberhart G.P., Weiffenbach B., Ordovas J.M., Freeman M.W.,
Brown R.H. Jr., Gu J.Z.;
"Novel mutations in the gene encoding ATP-binding cassette 1 in four
tangier disease kindreds.";
J. Lipid Res. 41:433-441(2000).
[25]
VARIANT HDLD1 ASP-1046, AND VARIANTS LYS-219; CYS-230; ILE-825; MET-883 AND
ARG-1587.
PubMed=10938021; DOI=10.1161/01.atv.20.8.1983;
Wang J., Burnett J.R., Near S., Young K., Zinman B., Hanley A.J.G.,
Connelly P.W., Harris S.B., Hegele R.A.;
"Common and rare ABCA1 variants affecting plasma HDL cholesterol.";
Arterioscler. Thromb. Vasc. Biol. 20:1983-1989(2000).
[26]
VARIANT HDLD1 TRP-587, AND VARIANT PRO-2168.
PubMed=11257260; DOI=10.1016/s0021-9150(00)00587-6;
Bertolini S., Pisciotta L., Seri M., Cusano R., Cantafora A., Calabresi L.,
Franceschini G., Ravazzolo R., Calandra S.;
"A point mutation in ABC1 gene in a patient with severe premature coronary
heart disease and mild clinical phenotype of Tangier disease.";
Atherosclerosis 154:599-605(2001).
[27]
VARIANTS LYS-219; MET-883 AND ASP-1172.
PubMed=11257261; DOI=10.1016/s0021-9150(00)00722-x;
Brousseau M.E., Bodzioch M., Schaefer E.J., Goldkamp A.L., Kielar D.,
Probst M., Ordovas J.M., Aslanidis C., Lackner K.J., Bloomfield Rubins H.,
Collins D., Robins S.J., Wilson P.W.F., Schmitz G.;
"Common variants in the gene encoding ATP-binding cassette transporter 1 in
men with low HDL cholesterol levels and coronary heart disease.";
Atherosclerosis 154:607-611(2001).
[28]
VARIANT HDLD1 LEU-1506.
PubMed=11476961; DOI=10.1016/s0925-4439(01)00053-9;
Lapicka-Bodzioch K., Bodzioch M., Kruell M., Kielar D., Probst M., Kiec B.,
Andrikovics H., Boettcher A., Hubacek J., Aslanidis C., Suttorp N.,
Schmitz G.;
"Homogeneous assay based on 52 primer sets to scan for mutations of the
ABCA1 gene and its application in genetic analysis of a new patient with
familial high-density lipoprotein deficiency syndrome.";
Biochim. Biophys. Acta 1537:42-48(2001).
[29]
VARIANTS HDLD1 ASN-1289 AND TRP-2081, AND VARIANT LYS-219.
PubMed=11476965; DOI=10.1016/s0925-4439(01)00058-8;
Huang W., Moriyama K., Koga T., Hua H., Ageta M., Kawabata S., Mawatari K.,
Imamura T., Eto T., Kawamura M., Teramoto T., Sasaki J.;
"Novel mutations in ABCA1 gene in Japanese patients with Tangier disease
and familial high density lipoprotein deficiency with coronary heart
disease.";
Biochim. Biophys. Acta 1537:71-78(2001).
[30]
VARIANTS LYS-219; ALA-399; MET-771; PRO-774; ASN-776; ILE-825; MET-883;
ASP-1172; ARG-1587 AND CYS-1731.
PubMed=11238261; DOI=10.1161/01.cir.103.9.1198;
Clee S.M., Zwinderman A.H., Engert J.C., Zwarts K.Y., Molhuizen H.O.F.,
Roomp K., Jukema J.W., van Wijland M., van Dam M., Hudson T.J.,
Brooks-Wilson A., Genest J. Jr., Kastelein J.J.P., Hayden M.R.;
"Common genetic variation in ABCA1 is associated with altered lipoprotein
levels and a modified risk for coronary artery disease.";
Circulation 103:1198-1205(2001).
[31]
VARIANT HDLD2 LEU-85.
PubMed=12204794; DOI=10.1016/s0021-9150(02)00106-5;
Hong S.H., Rhyne J., Zeller K., Miller M.;
"ABCA1(Alabama): a novel variant associated with HDL deficiency and
premature coronary artery disease.";
Atherosclerosis 164:245-250(2002).
[32]
VARIANTS HDLD2 TYR-1099 AND SER-2009.
PubMed=12009425; DOI=10.1016/s0925-4439(02)00066-2;
Hong S.H., Rhyne J., Zeller K., Miller M.;
"Novel ABCA1 compound variant associated with HDL cholesterol deficiency.";
Biochim. Biophys. Acta 1587:60-64(2002).
[33]
VARIANT HDLD1 THR-255, AND VARIANT ATHEROSCLEROSIS ASP-1611.
PubMed=11785958; DOI=10.1006/bbrc.2001.6219;
Nishida Y., Hirano K., Tsukamoto K., Nagano M., Ikegami C., Roomp K.,
Ishihara M., Sakane N., Zhang Z., Tsujii K., Matsuyama A., Ohama T.,
Matsuura F., Ishigami M., Sakai N., Hiraoka H., Hattori H., Wellington C.,
Yoshida Y., Misugi S., Hayden M.R., Egashira T., Yamashita S.,
Matsuzawa Y.;
"Expression and functional analyses of novel mutations of ATP-binding
cassette transporter-1 in Japanese patients with high-density lipoprotein
deficiency.";
Biochem. Biophys. Res. Commun. 290:713-721(2002).
[34]
VARIANT HDLD1 LEU-590.
PubMed=12407001;
Hong S.H., Riley W., Rhyne J., Friel G., Miller M.;
"Lack of association between increased carotid intima-media thickening and
decreased HDL-cholesterol in a family with a novel ABCA1 variant, G2265T.";
Clin. Chem. 48:2066-2070(2002).
[35]
VARIANTS HDLD1 HIS-935 AND SER-935.
PubMed=12111381; DOI=10.1007/s100380200044;
Guo Z., Inazu A., Yu W., Suzumura T., Okamoto M., Nohara A.,
Higashikata T., Sano R., Wakasugi K., Hayakawa T., Yoshida K., Suehiro T.,
Schmitz G., Mabuchi H.;
"Double deletions and missense mutations in the first nucleotide-binding
fold of the ATP-binding cassette transporter A1 (ABCA1) gene in Japanese
patients with Tangier disease.";
J. Hum. Genet. 47:325-329(2002).
[36]
VARIANT HDLD1 TRP-1680.
PubMed=12111371; DOI=10.1007/s100380200051;
Ishii J., Nagano M., Kujiraoka T., Ishihara M., Egashira T., Takada D.,
Tsuji M., Hattori H., Emi M.;
"Clinical variant of Tangier disease in Japan: mutation of the ABCA1 gene
in hypoalphalipoproteinemia with corneal lipidosis.";
J. Hum. Genet. 47:366-369(2002).
[37]
VARIANT HDLD1 GLN-1851.
PubMed=14576201; DOI=10.1161/01.res.0000102957.84247.8f;
Hong S.H., Rhyne J., Miller M.;
"Novel polypyrimidine variation (IVS46: del T -39._.-46) in ABCA1 causes
exon skipping and contributes to HDL cholesterol deficiency in a family
with premature coronary disease.";
Circ. Res. 93:1006-1012(2003).
[38]
VARIANTS ILE-825 AND MET-883, AND ASSOCIATION OF VARIANTS ILE-825 AND
MET-883 WITH HIGHER PLASMA HDL CHOLESTEROL.
PubMed=12709788; DOI=10.1007/s00439-003-0943-3;
Tan J.H., Low P.S., Tan Y.S., Tong M.C., Saha N., Yang H., Heng C.K.;
"ABCA1 gene polymorphisms and their associations with coronary artery
disease and plasma lipids in males from three ethnic populations in
Singapore.";
Hum. Genet. 113:106-117(2003).
[39]
VARIANTS LYS-219; MET-771; ILE-825; MET-883; ASP-1172; PHE-1181 AND
ARG-1587.
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).
[40]
VARIANT LYS-219.
PubMed=12624133; DOI=10.1136/jmg.40.3.163;
Cenarro A., Artieda M., Castillo S., Mozas P., Reyes G., Tejedor D.,
Alonso R., Mata P., Pocovi M., Civeira F.;
"A common variant in the ABCA1 gene is associated with a lower risk for
premature coronary heart disease in familial hypercholesterolaemia.";
J. Med. Genet. 40:163-168(2003).
[41]
VARIANTS HDLD1 LEU-590; ARG-840 AND CYS-1068, AND VARIANTS MET-771;
SER-2163 AND ILE-2244.
PubMed=15262183; DOI=10.1016/j.atherosclerosis.2004.02.019;
Probst M.C., Thumann H., Aslanidis C., Langmann T., Buechler C., Patsch W.,
Baralle F.E., Dallinga-Thie G.M., Geisel J., Keller C., Menys V.C.,
Schmitz G.;
"Screening for functional sequence variations and mutations in ABCA1.";
Atherosclerosis 175:269-279(2004).
[42]
VARIANTS HDLD1 LYS-284; CYS-482; HIS-1800; SER-1901 AND HIS-2196.
PubMed=15019541; DOI=10.1016/j.atherosclerosis.2003.11.009;
Pisciotta L., Hamilton-Craig I., Tarugi P., Bellocchio A., Fasano T.,
Alessandrini P., Bon G.B., Siepi D., Mannarino E., Cattin L., Averna M.,
Cefalu A.B., Cantafora A., Calandra S., Bertolini S.;
"Familial HDL deficiency due to ABCA1 gene mutations with or without other
genetic lipoprotein disorders.";
Atherosclerosis 172:309-320(2004).
[43]
VARIANTS HDLD1 PHE-1379 AND ASP-1704, AND CHARACTERIZATION OF VARIANTS
HDLD1 PHE-1379 AND ASP-1704.
PubMed=15158913; DOI=10.1016/j.bbadis.2004.01.007;
Albrecht C., Baynes K., Sardini A., Schepelmann S., Eden E.R., Davies S.W.,
Higgins C.F., Feher M.D., Owen J.S., Soutar A.K.;
"Two novel missense mutations in ABCA1 result in altered trafficking and
cause severe autosomal recessive HDL deficiency.";
Biochim. Biophys. Acta 1689:47-57(2004).
[44]
VARIANT HDLD1 HIS-1800, AND VARIANTS LYS-219; CYS-364; MET-771; PRO-774;
ASN-776; ILE-825; MET-883; SER-1065; ASP-1172; VAL-1216 AND ARG-1587.
PubMed=15520867; DOI=10.1172/jci200420361;
Frikke-Schmidt R., Nordestgaard B.G., Jensen G.B., Tybjaerg-Hansen A.;
"Genetic variation in ABC transporter A1 contributes to HDL cholesterol in
the general population.";
J. Clin. Invest. 114:1343-1353(2004).
[45]
VARIANT HDLD1 HIS-1800, AND VARIANTS ALA-248; GLN-401; TRP-496; SER-590;
GLN-638; SER-774; GLY-815; PHE-1181; THR-1341; GLY-1376; GLN-1615;
THR-1670; GLN-1680 AND GLU-2243.
PubMed=15297675; DOI=10.1126/science.1099870;
Cohen J.C., Kiss R.S., Pertsemlidis A., Marcel Y.L., McPherson R.,
Hobbs H.H.;
"Multiple rare alleles contribute to low plasma levels of HDL
cholesterol.";
Science 305:869-872(2004).
[46]
VARIANT SCOTT SYNDROME GLN-1925, AND CHARACTERIZATION OF VARIANT SCOTT
SYNDROME GLN-1925.
PubMed=15790791; DOI=10.1182/blood-2004-05-2056;
Albrecht C., McVey J.H., Elliott J.I., Sardini A., Kasza I., Mumford A.D.,
Naoumova R.P., Tuddenham E.G., Szabo K., Higgins C.F.;
"A novel missense mutation in ABCA1 results in altered protein trafficking
and reduced phosphatidylserine translocation in a patient with Scott
syndrome.";
Blood 106:542-549(2005).
[47]
VARIANT ASN-776, AND ASSOCIATION OF VARIANT ASN-776 WITH INCREASED RISK OF
ISCHEMIC HEART DISEASE.
PubMed=16226177; DOI=10.1016/j.jacc.2005.06.066;
Frikke-Schmidt R., Nordestgaard B.G., Schnohr P., Steffensen R.,
Tybjaerg-Hansen A.;
"Mutation in ABCA1 predicted risk of ischemic heart disease in the
Copenhagen City Heart Study Population.";
J. Am. Coll. Cardiol. 46:1516-1520(2005).
[48]
VARIANT HDLD2 TRP-1897.
PubMed=15722566; DOI=10.1194/jlr.d400038-jlr200;
Fasano T., Bocchi L., Pisciotta L., Bertolini S., Calandra S.;
"Denaturing high-performance liquid chromatography in the detection of
ABCA1 gene mutations in familial HDL deficiency.";
J. Lipid Res. 46:817-822(2005).
[49]
VARIANTS [LARGE SCALE ANALYSIS] ASP-210; TYR-917; THR-1407 AND THR-2109.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
[50]
VARIANT CYS-230.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Catalyzes the translocation of specific phospholipids from
the cytoplasmic to the extracellular/lumenal leaflet of membrane
coupled to the hydrolysis of ATP (PubMed:24097981). Thereby,
participates to phospholipids transfer to apoliproteins to form nascent
high density lipoproteins/HDLs (PubMed:14754908). Transports
preferentially phosphatidylcholine over phosphatidylserine
(PubMed:24097981). May play a similar role in the efflux of
intracellular cholesterol to apoliproteins and the formation of nascent
high density lipoproteins/HDLs (PubMed:10533863, PubMed:14754908,
PubMed:24097981). {ECO:0000269|PubMed:10533863,
ECO:0000269|PubMed:14754908, ECO:0000269|PubMed:24097981}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H(2)O + phospholipid(Side 1) = ADP + phosphate +
phospholipid(Side 2).; EC=7.6.2.1;
Evidence={ECO:0000269|PubMed:24097981};
-!- CATALYTIC ACTIVITY:
Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a
1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate;
Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643,
ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24097981};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38584;
Evidence={ECO:0000269|PubMed:24097981};
-!- CATALYTIC ACTIVITY:
Reaction=1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
Evidence={ECO:0000269|PubMed:24097981};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
Evidence={ECO:0000269|PubMed:24097981};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O + sphingomyelin(in) = ADP + H(+) + phosphate +
sphingomyelin(out); Xref=Rhea:RHEA:38903, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
Evidence={ECO:0000269|PubMed:24097981};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38904;
Evidence={ECO:0000269|PubMed:24097981};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
Evidence={ECO:0000305|PubMed:10533863, ECO:0000305|PubMed:14754908,
ECO:0000305|PubMed:24097981};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
Evidence={ECO:0000305|PubMed:10533863, ECO:0000305|PubMed:14754908,
ECO:0000305|PubMed:24097981};
-!- ACTIVITY REGULATION: ATPase activity is decreased by cholesterol and
ceramide. ATPase activity is stimulated by phosphatidylcholine and to a
lesser degree by phosphatidylserine and sphingomyelin. Phospholipid
translocase activity is highly reduced by berylium fluoride and
aluminum flouride and reduced by N-ethylmaleimide.
{ECO:0000269|PubMed:24097981}.
-!- SUBUNIT: Interacts with MEGF10 (PubMed:17205124). May interact with
APOE1; functionally associated with APOE1 in the biogenesis of HDLs
(PubMed:14754908). {ECO:0000269|PubMed:14754908,
ECO:0000269|PubMed:17205124}.
-!- INTERACTION:
Q86UK0:ABCA12; NbExp=4; IntAct=EBI-784112, EBI-9541582;
P02647:APOA1; NbExp=4; IntAct=EBI-784112, EBI-701692;
P27824:CANX; NbExp=8; IntAct=EBI-784112, EBI-355947;
P60953:CDC42; NbExp=2; IntAct=EBI-784112, EBI-81752;
P55055:NR1H2; NbExp=2; IntAct=EBI-784112, EBI-745354;
Q13424:SNTA1; NbExp=2; IntAct=EBI-784112, EBI-717191;
Q13884:SNTB1; NbExp=3; IntAct=EBI-784112, EBI-295843;
Q86Y82:STX12; NbExp=9; IntAct=EBI-784112, EBI-2691717;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19258317,
ECO:0000269|PubMed:19556522}; Multi-pass membrane protein
{ECO:0000269|PubMed:19258317, ECO:0000269|PubMed:19556522}. Cell
membrane {ECO:0000269|PubMed:24097981}. Endosome
{ECO:0000269|PubMed:24097981}.
-!- TISSUE SPECIFICITY: Widely expressed, but most abundant in macrophages.
-!- INDUCTION: By bacterial lipopolysaccharides (LPS). LPS regulates
expression through a liver X receptor (LXR) -independent mechanism.
Repressed by ZNF202. {ECO:0000269|PubMed:11279031,
ECO:0000269|PubMed:12032171}.
-!- DOMAIN: Multifunctional polypeptide with two homologous halves, each
containing a hydrophobic membrane-anchoring domain and an ATP binding
cassette (ABC) domain.
-!- PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux.
{ECO:0000269|PubMed:12196520}.
-!- PTM: Palmitoylation by DHHC8 is essential for membrane localization.
{ECO:0000269|PubMed:19556522}.
-!- POLYMORPHISM: Genetic variations in ABCA1 define the high density
lipoprotein cholesterol level quantitative trait locus 13 (HDLCQ13)
[MIM:600046]. {ECO:0000269|PubMed:18354102}.
-!- 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.
{ECO:0000269|PubMed:10431236, ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:10706591, ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:11086027, ECO:0000269|PubMed:11257260,
ECO:0000269|PubMed:11476961, ECO:0000269|PubMed:11476965,
ECO:0000269|PubMed:11785958, ECO:0000269|PubMed:12111371,
ECO:0000269|PubMed:12111381, ECO:0000269|PubMed:12407001,
ECO:0000269|PubMed:14576201, ECO:0000269|PubMed:14754908,
ECO:0000269|PubMed:15019541, ECO:0000269|PubMed:15158913,
ECO:0000269|PubMed:15262183, ECO:0000269|PubMed:15297675,
ECO:0000269|PubMed:15520867, ECO:0000269|PubMed:24097981}. Note=The
disease is caused by mutations affecting the gene represented in this
entry.
-!- 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.
{ECO:0000269|PubMed:10431236, ECO:0000269|PubMed:10533863,
ECO:0000269|PubMed:11086027, ECO:0000269|PubMed:12009425,
ECO:0000269|PubMed:12204794, ECO:0000269|PubMed:15722566,
ECO:0000269|PubMed:24097981}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD49849.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=CAA10005.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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=ABCA1";
-!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=O95477";
---------------------------------------------------------------------------
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EMBL; AF275948; AAF86276.1; -; Genomic_DNA.
EMBL; AL353685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL359846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF285167; AAF98175.1; -; mRNA.
EMBL; AF287262; AAK43526.1; -; Genomic_DNA.
EMBL; AB055982; BAB63210.1; -; mRNA.
EMBL; AJ012376; CAA10005.1; ALT_INIT; mRNA.
EMBL; AF165281; AAD49849.1; ALT_INIT; mRNA.
EMBL; AF165286; AAD49851.1; -; Genomic_DNA.
EMBL; AF165282; AAD49851.1; JOINED; Genomic_DNA.
EMBL; AF165283; AAD49851.1; JOINED; Genomic_DNA.
EMBL; AF165284; AAD49851.1; JOINED; Genomic_DNA.
EMBL; AF165285; AAD49851.1; JOINED; Genomic_DNA.
EMBL; AF165306; AAD49852.1; -; Genomic_DNA.
EMBL; AF165287; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165288; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165289; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165290; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165291; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165292; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165293; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165294; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165295; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165296; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165297; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165298; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165299; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165300; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165301; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165302; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165303; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165304; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165305; AAD49852.1; JOINED; Genomic_DNA.
EMBL; AF165309; AAD49854.1; -; Genomic_DNA.
EMBL; AF165307; AAD49854.1; JOINED; Genomic_DNA.
EMBL; AF165308; AAD49854.1; JOINED; Genomic_DNA.
EMBL; AF165310; AAD49853.1; -; Genomic_DNA.
CCDS; CCDS6762.1; -.
RefSeq; NP_005493.2; NM_005502.3.
PDB; 5XJY; EM; 4.10 A; A=1-2261.
PDBsum; 5XJY; -.
SMR; O95477; -.
BioGrid; 106537; 25.
DIP; DIP-29211N; -.
IntAct; O95477; 32.
MINT; O95477; -.
STRING; 9606.ENSP00000363868; -.
ChEMBL; CHEMBL2362986; -.
DrugBank; DB00171; ATP.
DrugBank; DB01016; Glyburide.
DrugBank; DB01599; Probucol.
DrugBank; DB11635; Tocofersolan.
DrugBank; DB00163; Vitamin E.
DrugCentral; O95477; -.
SwissLipids; SLP:000000345; -.
TCDB; 3.A.1.211.14; the atp-binding cassette (abc) superfamily.
GlyConnect; 1020; -.
iPTMnet; O95477; -.
PhosphoSitePlus; O95477; -.
SwissPalm; O95477; -.
BioMuta; ABCA1; -.
EPD; O95477; -.
jPOST; O95477; -.
MassIVE; O95477; -.
MaxQB; O95477; -.
PaxDb; O95477; -.
PeptideAtlas; O95477; -.
PRIDE; O95477; -.
ProteomicsDB; 50908; -.
Ensembl; ENST00000374736; ENSP00000363868; ENSG00000165029.
GeneID; 19; -.
KEGG; hsa:19; -.
UCSC; uc004bcl.4; human.
CTD; 19; -.
DisGeNET; 19; -.
GeneCards; ABCA1; -.
HGNC; HGNC:29; ABCA1.
HPA; CAB069889; -.
HPA; HPA057283; -.
MalaCards; ABCA1; -.
MIM; 205400; phenotype.
MIM; 600046; gene+phenotype.
MIM; 604091; phenotype.
neXtProt; NX_O95477; -.
OpenTargets; ENSG00000165029; -.
Orphanet; 425; Apolipoprotein A-I deficiency.
Orphanet; 31150; Tangier disease.
PharmGKB; PA24373; -.
eggNOG; KOG0059; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00940000154658; -.
HOGENOM; CLU_000604_19_0_1; -.
InParanoid; O95477; -.
KO; K05641; -.
OMA; PEKEVCK; -.
OrthoDB; 131191at2759; -.
PhylomeDB; O95477; -.
TreeFam; TF105191; -.
Reactome; R-HSA-1989781; PPARA activates gene expression.
Reactome; R-HSA-5682113; Defective ABCA1 causes Tangier disease.
Reactome; R-HSA-8963896; HDL assembly.
Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
SignaLink; O95477; -.
SIGNOR; O95477; -.
ChiTaRS; ABCA1; human.
GeneWiki; ABCA1; -.
GenomeRNAi; 19; -.
Pharos; O95477; Tclin.
PRO; PR:O95477; -.
Proteomes; UP000005640; Chromosome 9.
RNAct; O95477; protein.
Bgee; ENSG00000165029; Expressed in liver and 221 other tissues.
ExpressionAtlas; O95477; baseline and differential.
Genevisible; O95477; HS.
GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0045335; C:phagocytic vesicle; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0034186; F:apolipoprotein A-I binding; IPI:BHF-UCL.
GO; GO:0034188; F:apolipoprotein A-I receptor activity; IDA:BHF-UCL.
GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
GO; GO:0016887; F:ATPase activity; IDA:BHF-UCL.
GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015485; F:cholesterol binding; IC:BHF-UCL.
GO; GO:0120020; F:cholesterol transfer activity; IDA:BHF-UCL.
GO; GO:0140328; F:floppase activity; IDA:UniProtKB.
GO; GO:0008035; F:high-density lipoprotein particle binding; IEA:Ensembl.
GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
GO; GO:0090554; F:phosphatidylcholine floppase activity; IDA:BHF-UCL.
GO; GO:0090556; F:phosphatidylserine floppase activity; IDA:BHF-UCL.
GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL.
GO; GO:0019905; F:syntaxin binding; IPI:BHF-UCL.
GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEP:BHF-UCL.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO; GO:0016197; P:endosomal transport; IDA:BHF-UCL.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0034380; P:high-density lipoprotein particle assembly; IMP:UniProtKB.
GO; GO:0050702; P:interleukin-1 beta secretion; IMP:BHF-UCL.
GO; GO:0032367; P:intracellular cholesterol transport; IMP:BHF-UCL.
GO; GO:0006869; P:lipid transport; IBA:GO_Central.
GO; GO:0007040; P:lysosome organization; IDA:BHF-UCL.
GO; GO:0010887; P:negative regulation of cholesterol storage; TAS:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; TAS:BHF-UCL.
GO; GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl.
GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL.
GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL.
GO; GO:0045332; P:phospholipid translocation; IDA:BHF-UCL.
GO; GO:0060155; P:platelet dense granule organization; IMP:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
GO; GO:0090108; P:positive regulation of high-density lipoprotein particle assembly; ISS:UniProtKB.
GO; GO:0006497; P:protein lipidation; IEA:Ensembl.
GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL.
GO; GO:0090107; P:regulation of high-density lipoprotein particle assembly; TAS:BHF-UCL.
GO; GO:0019216; P:regulation of lipid metabolic process; TAS:Reactome.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0034616; P:response to laminar fluid shear stress; IEP:BHF-UCL.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR026082; ABCA.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR19229; PTHR19229; 1.
Pfam; PF00005; ABC_tran; 2.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
3D-structure; Atherosclerosis; ATP-binding; Cell membrane;
Cholesterol metabolism; Disease mutation; Disulfide bond; Endosome;
Glycoprotein; Lipid metabolism; Lipoprotein; Membrane; Nucleotide-binding;
Palmitate; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Steroid metabolism; Sterol metabolism; Translocase; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1..2261
/note="Phospholipid-transporting ATPase ABCA1"
/id="PRO_0000093288"
TRANSMEM 22..42
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 43..639
/note="Extracellular"
TRANSMEM 640..660
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 683..703
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 716..736
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 745..765
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 777..797
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 827..847
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 1041..1057
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 1351..1371
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 1372..1656
/note="Extracellular"
TRANSMEM 1657..1677
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 1703..1723
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 1735..1755
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 1768..1788
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 1802..1822
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 1852..1872
/note="Helical"
/evidence="ECO:0000255"
DOMAIN 899..1131
/note="ABC transporter 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
DOMAIN 1912..2144
/note="ABC transporter 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
NP_BIND 933..940
/note="ATP 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
NP_BIND 1946..1953
/note="ATP 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
MOD_RES 1042
/note="Phosphoserine; by PKA"
/evidence="ECO:0000269|PubMed:12196520"
MOD_RES 1296
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P41233"
MOD_RES 2054
/note="Phosphoserine; by PKA"
/evidence="ECO:0000269|PubMed:12196520"
LIPID 3
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:19556522"
LIPID 23
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:19556522"
LIPID 1110
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:19556522"
LIPID 1111
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:19556522"
CARBOHYD 14
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 98
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 151
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 161
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 196
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 244
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:19159218"
CARBOHYD 292
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 337
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 349
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 400
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 478
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 489
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 521
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 820
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1144
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1294
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1453
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1504
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 1637
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2044
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 2238
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 75..309
/evidence="ECO:0000269|PubMed:19258317"
DISULFID 1463..1477
/evidence="ECO:0000269|PubMed:19258317"
VARIANT 85
/note="P -> L (in HDLD2; Alabama; dbSNP:rs145183203)"
/evidence="ECO:0000269|PubMed:12204794"
/id="VAR_017529"
VARIANT 210
/note="E -> D (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_035724"
VARIANT 219
/note="R -> K (common polymorphism; associated with a
decreased severity of CAD; dbSNP:rs2230806)"
/evidence="ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:11238261, ECO:0000269|PubMed:11257261,
ECO:0000269|PubMed:11476965, ECO:0000269|PubMed:12624133,
ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:15520867"
/id="VAR_012618"
VARIANT 230
/note="R -> C (in dbSNP:rs9282541)"
/evidence="ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:27535533"
/id="VAR_012619"
VARIANT 248
/note="P -> A (in dbSNP:rs142625938)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062481"
VARIANT 255
/note="A -> T (in HDLD1; deficient cellular cholesterol
efflux; dbSNP:rs758100110)"
/evidence="ECO:0000269|PubMed:11785958"
/id="VAR_012620"
VARIANT 284
/note="E -> K (in HDLD1)"
/evidence="ECO:0000269|PubMed:15019541"
/id="VAR_062482"
VARIANT 364
/note="S -> C (in dbSNP:rs775035559)"
/evidence="ECO:0000269|PubMed:15520867"
/id="VAR_062483"
VARIANT 399
/note="V -> A (in dbSNP:rs9282543)"
/evidence="ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:11238261"
/id="VAR_009145"
VARIANT 401
/note="K -> Q (in dbSNP:rs138487227)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062484"
VARIANT 482
/note="Y -> C (in HDLD1)"
/evidence="ECO:0000269|PubMed:15019541"
/id="VAR_062485"
VARIANT 496
/note="R -> W (associated with increased plasma HDL
cholesterol; dbSNP:rs147675550)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062486"
VARIANT 587
/note="R -> W (in HDLD1; dbSNP:rs2853574)"
/evidence="ECO:0000269|PubMed:11257260"
/id="VAR_009146"
VARIANT 590
/note="W -> L (in HDLD1; dbSNP:rs137854496)"
/evidence="ECO:0000269|PubMed:12407001,
ECO:0000269|PubMed:15262183"
/id="VAR_062487"
VARIANT 590
/note="W -> S (in HDLD1; moderately decreased protein
abundance; highly decreased ATPase activity; highly
decreased phospholipid translocase activity;
dbSNP:rs137854496)"
/evidence="ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:15297675, ECO:0000269|PubMed:24097981"
/id="VAR_009147"
VARIANT 597
/note="Q -> R (in HDLD1; dbSNP:rs2853578)"
/evidence="ECO:0000269|PubMed:10431236,
ECO:0000269|PubMed:11086027"
/id="VAR_009148"
VARIANT 638
/note="R -> Q (associated with reduced plasma HDL
cholesterol; dbSNP:rs374190304)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062488"
VARIANT 693
/note="Missing (in HDLD2)"
/evidence="ECO:0000269|PubMed:10431236,
ECO:0000269|PubMed:11086027"
/id="VAR_009149"
VARIANT 771
/note="V -> M (associated with HDL cholesterol;
dbSNP:rs2066718)"
/evidence="ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:15262183,
ECO:0000269|PubMed:15520867"
/id="VAR_012621"
VARIANT 774
/note="T -> P (in dbSNP:rs35819696)"
/evidence="ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:15520867"
/id="VAR_012622"
VARIANT 774
/note="T -> S"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062489"
VARIANT 776
/note="K -> N (may be associated with increased risk of
ischemic heart disease; dbSNP:rs138880920)"
/evidence="ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:15520867, ECO:0000269|PubMed:16226177"
/id="VAR_012623"
VARIANT 815
/note="E -> G (associated with reduced plasma HDL
cholesterol; dbSNP:rs145582736)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062490"
VARIANT 825
/note="V -> I (associated with higher plasma cholesterol;
dbSNP:rs2066715)"
/evidence="ECO:0000269|PubMed:10938021,
ECO:0000269|PubMed:11238261, ECO:0000269|PubMed:12709788,
ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:15520867"
/id="VAR_012624"
VARIANT 840
/note="W -> R (in HDLD1; dbSNP:rs1322998567)"
/evidence="ECO:0000269|PubMed:15262183"
/id="VAR_062491"
VARIANT 883
/note="I -> M (associated with higher plasma cholesterol;
dbSNP:rs2066714)"
/evidence="ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:10938021, ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:11257261, ECO:0000269|PubMed:12709788,
ECO:0000269|PubMed:12966036, ECO:0000269|PubMed:15520867"
/id="VAR_012625"
VARIANT 917
/note="D -> Y (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_035725"
VARIANT 929
/note="T -> I (in HDLD1; moderately decreased protein
abundance; highly decreased ATPase activity; highly
decreased phospholipid translocase activity; loss protein
subcellular localization to the plasma membrane)"
/evidence="ECO:0000269|PubMed:11086027,
ECO:0000269|PubMed:24097981"
/id="VAR_012626"
VARIANT 935
/note="N -> H (in HDLD1; dbSNP:rs28937314)"
/evidence="ECO:0000269|PubMed:12111381"
/id="VAR_037968"
VARIANT 935
/note="N -> S (in HDLD1; moderately decreased protein
abundance; highly decreased ATPase activity; highly
decreased phospholipid translocase activity;
dbSNP:rs28937313)"
/evidence="ECO:0000269|PubMed:10431237,
ECO:0000269|PubMed:12111381, ECO:0000269|PubMed:24097981"
/id="VAR_009150"
VARIANT 937
/note="A -> V (in HDLD1; dbSNP:rs137854495)"
/evidence="ECO:0000269|PubMed:10431237"
/id="VAR_009151"
VARIANT 1046
/note="A -> D (in HDLD1; dbSNP:rs141021096)"
/evidence="ECO:0000269|PubMed:10938021"
/id="VAR_012627"
VARIANT 1054
/note="V -> I (in dbSNP:rs13306072)"
/id="VAR_037969"
VARIANT 1065
/note="P -> S"
/evidence="ECO:0000269|PubMed:15520867"
/id="VAR_062492"
VARIANT 1068
/note="R -> C (in HDLD1; dbSNP:rs745593394)"
/evidence="ECO:0000269|PubMed:15262183"
/id="VAR_062493"
VARIANT 1091
/note="M -> T (in HDLD2)"
/evidence="ECO:0000269|PubMed:10533863,
ECO:0000269|PubMed:11086027"
/id="VAR_012628"
VARIANT 1099
/note="D -> Y (in HDLD2; dbSNP:rs28933692)"
/evidence="ECO:0000269|PubMed:12009425"
/id="VAR_017530"
VARIANT 1172
/note="E -> D (associated with premature coronary heart
disease; dbSNP:rs33918808)"
/evidence="ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:11257261, ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15520867"
/id="VAR_012629"
VARIANT 1181
/note="S -> F (associated with reduced plasma HDL
cholesterol; dbSNP:rs76881554)"
/evidence="ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15297675"
/id="VAR_017016"
VARIANT 1216
/note="G -> V (in dbSNP:rs562403512)"
/evidence="ECO:0000269|PubMed:15520867"
/id="VAR_062494"
VARIANT 1289
/note="D -> N (in HDLD1; dbSNP:rs137854500)"
/evidence="ECO:0000269|PubMed:10706591,
ECO:0000269|PubMed:11476965"
/id="VAR_009152"
VARIANT 1341
/note="R -> T (associated with reduced plasma HDL
cholesterol; dbSNP:rs147743782)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062495"
VARIANT 1376
/note="S -> G (in dbSNP:rs145689805)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062496"
VARIANT 1379
/note="L -> F (in HDLD1; the mutant protein is retained in
the endoplasmic reticulum while the wild-type protein is
located at the plasma membrane)"
/evidence="ECO:0000269|PubMed:15158913"
/id="VAR_062497"
VARIANT 1407
/note="A -> T (in a colorectal cancer sample; somatic
mutation; dbSNP:rs189206655)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_035726"
VARIANT 1477
/note="C -> R (in HDLD1; loss of interaction with APOE;
unable to generate APOE-containing high density
lipoproteins; moderately decreased protein abundance;
moderately decreased ATPase activity; moderately decreased
phospholipid translocase activity; dbSNP:rs137854494)"
/evidence="ECO:0000269|PubMed:10431236,
ECO:0000269|PubMed:11086027, ECO:0000269|PubMed:14754908,
ECO:0000269|PubMed:24097981"
/id="VAR_009153"
VARIANT 1506
/note="S -> L (in HDLD1; dbSNP:rs137854497)"
/evidence="ECO:0000269|PubMed:11476961"
/id="VAR_012630"
VARIANT 1517
/note="I -> R (in HDLD1)"
/id="VAR_009154"
VARIANT 1555
/note="I -> T (in dbSNP:rs1997618)"
/evidence="ECO:0000269|PubMed:10092505,
ECO:0000269|PubMed:10431238"
/id="VAR_012638"
VARIANT 1587
/note="K -> R (associated with HDL cholesterol;
dbSNP:rs2230808)"
/evidence="ECO:0000269|PubMed:10092505,
ECO:0000269|PubMed:10431238, ECO:0000269|PubMed:10884428,
ECO:0000269|PubMed:10938021, ECO:0000269|PubMed:11238261,
ECO:0000269|PubMed:11352567, ECO:0000269|PubMed:12966036,
ECO:0000269|PubMed:15520867, ECO:0000269|Ref.2"
/id="VAR_012631"
VARIANT 1611
/note="N -> D (probable disease-associated mutation;
associated with atherosclerosis; deficient cellular
cholesterol efflux)"
/evidence="ECO:0000269|PubMed:11785958"
/id="VAR_012632"
VARIANT 1615
/note="R -> Q (associated with reduced plasma HDL
cholesterol; dbSNP:rs1251839800)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062498"
VARIANT 1648
/note="L -> P (in dbSNP:rs1883024)"
/evidence="ECO:0000269|PubMed:10092505,
ECO:0000269|PubMed:10431238"
/id="VAR_012639"
VARIANT 1670
/note="A -> T (associated with reduced plasma HDL
cholesterol; dbSNP:rs1203589782)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062499"
VARIANT 1680
/note="R -> Q (associated with increased plasma HDL
cholesterol; dbSNP:rs150125857)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062500"
VARIANT 1680
/note="R -> W (in HDLD1; dbSNP:rs137854498)"
/evidence="ECO:0000269|PubMed:12111371"
/id="VAR_037970"
VARIANT 1704
/note="V -> D (in HDLD1; the mutant protein is retained in
the endoplasmic reticulum while the wild-type protein is
located at the plasma membrane)"
/evidence="ECO:0000269|PubMed:15158913"
/id="VAR_062501"
VARIANT 1731
/note="S -> C (in dbSNP:rs760507032)"
/evidence="ECO:0000269|PubMed:11238261"
/id="VAR_012633"
VARIANT 1800
/note="N -> H (in HDLD1; dbSNP:rs146292819)"
/evidence="ECO:0000269|PubMed:10706591,
ECO:0000269|PubMed:15019541, ECO:0000269|PubMed:15297675,
ECO:0000269|PubMed:15520867"
/id="VAR_009155"
VARIANT 1851
/note="R -> Q (in HDLD1; dbSNP:rs1055285452)"
/evidence="ECO:0000269|PubMed:14576201"
/id="VAR_062502"
VARIANT 1893..1894
/note="Missing (in HDLD2)"
/evidence="ECO:0000269|PubMed:10533863,
ECO:0000269|PubMed:11086027"
/id="VAR_012634"
VARIANT 1897
/note="R -> W (in HDLD2; uncertain pathological
significance; dbSNP:rs760768125)"
/evidence="ECO:0000269|PubMed:15722566"
/id="VAR_062503"
VARIANT 1901
/note="R -> S (in HDLD1)"
/evidence="ECO:0000269|PubMed:15019541"
/id="VAR_062504"
VARIANT 1925
/note="R -> Q (in Scott syndrome; shows impaired
trafficking of the mutant protein to the plasma membrane;
dbSNP:rs142688906)"
/evidence="ECO:0000269|PubMed:15790791"
/id="VAR_062505"
VARIANT 2009
/note="F -> S (in HDLD2; dbSNP:rs137854499)"
/evidence="ECO:0000269|PubMed:12009425"
/id="VAR_037971"
VARIANT 2081
/note="R -> W (in HDLD1; highly decreased protein
abundance; highly decreased ATPase activity; highly
decreased phospholipid translocase activity; loss protein
subcellular localization to the plasma membrane;
dbSNP:rs137854501)"
/evidence="ECO:0000269|PubMed:11476965,
ECO:0000269|PubMed:24097981"
/id="VAR_012635"
VARIANT 2109
/note="A -> T (in a colorectal cancer sample; somatic
mutation)"
/evidence="ECO:0000269|PubMed:16959974"
/id="VAR_035727"
VARIANT 2150
/note="P -> L (in HDLD2; moderately decreased protein
abundance; does not affect ATPase activity; moderately
decreased phospholipid translocase activity;
dbSNP:rs369098049)"
/evidence="ECO:0000269|PubMed:11086027,
ECO:0000269|PubMed:24097981"
/id="VAR_012636"
VARIANT 2163
/note="F -> S (could be associated with reduced plasma HDL
cholesterol)"
/evidence="ECO:0000269|PubMed:15262183"
/id="VAR_062506"
VARIANT 2168
/note="L -> P (in dbSNP:rs2853577)"
/evidence="ECO:0000269|PubMed:10092505,
ECO:0000269|PubMed:10431238, ECO:0000269|PubMed:11257260"
/id="VAR_012637"
VARIANT 2196
/note="Q -> H (in HDLD1; dbSNP:rs564764153)"
/evidence="ECO:0000269|PubMed:15019541"
/id="VAR_062507"
VARIANT 2243
/note="D -> E (in dbSNP:rs34879708)"
/evidence="ECO:0000269|PubMed:15297675"
/id="VAR_062508"
VARIANT 2244
/note="V -> I (could be associated with reduced plasma HDL
cholesterol; dbSNP:rs144588452)"
/evidence="ECO:0000269|PubMed:15262183"
/id="VAR_062509"
MUTAGEN 100
/note="S->C: Highly decreased protein abundance. Highly
decreased ATPase activity. Highly decreased phospholipid
translocase activity."
/evidence="ECO:0000269|PubMed:24097981"
MUTAGEN 593
/note="F->L: Moderately decreased protein abundance. Highly
decreased ATPase activity. Highly decreased phospholipid
translocase activity."
/evidence="ECO:0000269|PubMed:24097981"
MUTAGEN 939
/note="K->M: Inhibits ATPase activity; when associated with
M-1952. Decreases translocase activity; when associated
with M-1952. Does not affect protein subcellular
localization in plasma membrane and endosome; when
associated with M-1952."
/evidence="ECO:0000269|PubMed:24097981"
MUTAGEN 1512
/note="T->M: Moderately decreased protein abundance. Does
not affect ATPase activity. Moderately decreased
phospholipid translocase activity."
/evidence="ECO:0000269|PubMed:24097981"
MUTAGEN 1952
/note="K->M: Inhibits ATPase activity; when associated with
M-939. Decreases translocase activity; when associated with
M-939. Does not affect protein subcellular localization in
plasma membrane and endosome; when associated with M-939."
/evidence="ECO:0000269|PubMed:24097981"
CONFLICT 793
/note="Y -> C (in Ref. 3; AAK43526)"
/evidence="ECO:0000305"
CONFLICT 831
/note="D -> N (in Ref. 3; AAK43526)"
/evidence="ECO:0000305"
CONFLICT 1005
/note="E -> K (in Ref. 3; AAK43526)"
/evidence="ECO:0000305"
CONFLICT 1745..1746
/note="Missing (in Ref. 7; AAD49852)"
/evidence="ECO:0000305"
SEQUENCE 2261 AA; 254302 MW; 21A2CF8F3F518D6D CRC64;
MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA
MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVARLFSDAR RLLLYSQKDT
SMKDMRKVLR TLQQIKKSSS NLKLQDFLVD NETFSGFLYH NLSLPKSTVD KMLRADVILH
KVFLQGYQLH LTSLCNGSKS EEMIQLGDQE VSELCGLPRE KLAAAERVLR SNMDILKPIL
RTLNSTSPFP SKELAEATKT LLHSLGTLAQ ELFSMRSWSD MRQEVMFLTN VNSSSSSTQI
YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNGTE EDAETFYDNS TTPYCNDLMK
NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS
PKIWTFMENS QEMDLVRMLL DSRDNDHFWE QQLDGLDWTA QDIVAFLAKH PEDVQSSNGS
VYTWREAFNE TNQAIRTISR FMECVNLNKL EPIATEVWLI NKSMELLDER KFWAGIVFTG
ITPGSIELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
EQAIIRVLTG TEKKTGVYMQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKGIV
YEKEARLKET MRIMGLDNSI LWFSWFISSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV
FLSVFAVVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFTLKIFAS
LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTSVSMMLF DTFLYGVMTW
YIEAVFPGQY GIPRPWYFPC TKSYWFGEES DEKSHPGSNQ KRISEICMEE EPTHLKLGVS
IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL
GKDIRSEMST IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG
LPSSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ
GRTIILSTHH MDEADVLGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS
SCRNSSSTVS YLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE
TSDGTLPARR NRRAFGDKQS CLRPFTEDDA ADPNDSDIDP ESRETDLLSG MDGKGSYQVK
GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ
PWMYNEQYTF VSNDAPEDTG TLELLNALTK DPGFGTRCME GNPIPDTPCQ AGEEEWTTAP
VPQTIMDLFQ NGNWTMQNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QNTADILQDL
TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NTQALPPSQE VNDAIKQMKK
HLKLAKDSSA DRFLNSLGRF MTGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK
GENPSHYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER
VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL
LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTDNKLNNIN
DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG
VVFFLITVLI QYRFFIRPRP VNAKLSPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI
YRRKRKPAVD RICVGIPPGE CFGLLGVNGA GKSSTFKMLT GDTTVTRGDA FLNKNSILSN
IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK
YAGNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSV VKEGRSVVLT
SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQDFFG
LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF
AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V


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