ABCA8_HUMAN
ID ABCA8_HUMAN Reviewed; 1621 AA.
AC O94911; A1L3U3; C9JQE6; Q86WW0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 4.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=ABC-type organic anion transporter ABCA8;
DE EC=7.6.2.- {ECO:0000269|PubMed:12379217};
DE AltName: Full=ATP-binding cassette sub-family A member 8 {ECO:0000305};
GN Name=ABCA8 {ECO:0000312|HGNC:HGNC:38};
GN Synonyms=KIAA0822 {ECO:0000303|PubMed:10048485};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Kikuno R., Nagase T., Ishikawa K.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP VAL-416.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION (ISOFORM 1), TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES
RP (ISOFORM 1), ACTIVITY REGULATION (ISOFORM 1), AND CATALYTIC ACTIVITY
RP (ISOFORM 1).
RX PubMed=12379217; DOI=10.1016/s0006-291x(02)02389-6;
RA Tsuruoka S., Ishibashi K., Yamamoto H., Wakaumi M., Suzuki M.,
RA Schwartz G.J., Imai M., Fujimura A.;
RT "Functional analysis of ABCA8, a new drug transporter.";
RL Biochem. Biophys. Res. Commun. 298:41-45(2002).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP TISSUE SPECIFICITY, FUNCTION (ISOFORM 1), AND CATALYTIC ACTIVITY.
RX PubMed=23560799; DOI=10.1042/bj20121764;
RA Kim W.S., Hsiao J.H., Bhatia S., Glaros E.N., Don A.S., Tsuruoka S.,
RA Shannon Weickert C., Halliday G.M.;
RT "ABCA8 stimulates sphingomyelin production in oligodendrocytes.";
RL Biochem. J. 452:401-410(2013).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, FUNCTION (ISOFORM 3), CATALYTIC ACTIVITY (ISOFORM 3), AND
RP ACTIVITY REGULATION (ISOFORM 3).
RX PubMed=29300488; DOI=10.1021/acs.molpharmaceut.7b00679;
RA Sasaki K., Tachikawa M., Uchida Y., Hirano S., Kadowaki F., Watanabe M.,
RA Ohtsuki S., Terasaki T.;
RT "ATP-Binding Cassette Transporter A Subfamily 8 Is a Sinusoidal Efflux
RT Transporter for Cholesterol and Taurocholate in Mouse and Human Liver.";
RL Mol. Pharm. 15:343-355(2018).
RN [10]
RP VARIANT SER-331.
RX PubMed=12111378; DOI=10.1007/s100380200041;
RA Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K.,
RA Harigae S., Osawa S., Nakamura Y.;
RT "Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes
RT encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8,
RT ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and ABCG8.";
RL J. Hum. Genet. 47:285-310(2002).
RN [11]
RP VARIANTS ARG-649 AND 781-THR--PRO-1621 DEL, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, FUNCTION (ISOFORM 3), CHARACTERIZATION OF VARIANTS ARG-649 AND
RP 781-THR--PRO-1621 DEL, AND INTERACTION WITH ABCA1 (ISOFORM 3).
RX PubMed=28882873; DOI=10.1161/atvbaha.117.309574;
RA Trigueros-Motos L., van Capelleveen J.C., Torta F., Castano D., Zhang L.H.,
RA Chai E.C., Kang M., Dimova L.G., Schimmel A.W.M., Tietjen I., Radomski C.,
RA Tan L.J., Thiam C.H., Narayanaswamy P., Wu D.H., Dorninger F., Yakala G.K.,
RA Barhdadi A., Angeli V., Dube M.P., Berger J., Dallinga-Thie G.M.,
RA Tietge U.J.F., Wenk M.R., Hayden M.R., Hovingh G.K., Singaraja R.R.;
RT "ABCA8 Regulates Cholesterol Efflux and High-Density Lipoprotein
RT Cholesterol Levels.";
RL Arterioscler. Thromb. Vasc. Biol. 37:2147-2155(2017).
CC -!- FUNCTION: [Isoform 1]: Catalyzes ATP-dependent import of organic anions
CC such as taurocholate and estrone sulfate (PubMed:12379217). In vitro,
CC also imports ochratoxin A (PubMed:12379217). Also mediates cholesterol
CC efflux independent of apolipoprotein, and plays a role in sphingomyelin
CC production in oligodendrocytes (PubMed:23560799).
CC {ECO:0000269|PubMed:12379217, ECO:0000269|PubMed:23560799}.
CC -!- FUNCTION: [Isoform 3]: Catalyzes ATP-dependent efflux of cholesterol
CC and taurocholate (PubMed:29300488). Interaction with ABCA1 potentiates
CC cholesterol efflux to lipid-free APOA1, which regulates high-density
CC lipoprotein cholesterol levels (PubMed:28882873).
CC {ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488}.
CC -!- CATALYTIC ACTIVITY: [Isoform 3]:
CC Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate +
CC taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:29300488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC Evidence={ECO:0000305|PubMed:29300488};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:23560799, ECO:0000269|PubMed:28882873,
CC ECO:0000269|PubMed:29300488};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000269|PubMed:28882873, ECO:0000269|PubMed:29300488};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=ATP + estrone 3-sulfate(out) + H2O = ADP + estrone 3-
CC sulfate(in) + H(+) + phosphate; Xref=Rhea:RHEA:65956,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60050, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:12379217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65957;
CC Evidence={ECO:0000305|PubMed:12379217};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=ATP + H2O + leukotriene C4(out) = ADP + H(+) + leukotriene
CC C4(in) + phosphate; Xref=Rhea:RHEA:65960, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:12379217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65961;
CC Evidence={ECO:0000305|PubMed:12379217};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=ATP + H2O + taurocholate(out) = ADP + H(+) + phosphate +
CC taurocholate(in); Xref=Rhea:RHEA:65964, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:12379217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65965;
CC Evidence={ECO:0000305|PubMed:12379217};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ATP + H2O =
CC 17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:65968, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82961, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:12379217};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65969;
CC Evidence={ECO:0000305|PubMed:12379217};
CC -!- ACTIVITY REGULATION: [Isoform 1]: Dofequidar (MS-209) and ochratoxin A
CC inhibited the 17beta-estradiol 17-O-(beta-D-glucuronate) influx.
CC {ECO:0000269|PubMed:12379217}.
CC -!- ACTIVITY REGULATION: [Isoform 3]: Cholesterol efflux is increased by
CC extracellularly applied taurocholate. {ECO:0000269|PubMed:29300488}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Isoform 1]:
CC Kinetic parameters:
CC KM=30.4 uM for estradiol-beta-glucuronide
CC {ECO:0000269|PubMed:12379217};
CC KM=0.1 uM for LTC4 {ECO:0000269|PubMed:12379217};
CC KM=10.3 uM for taurochlorate {ECO:0000269|PubMed:12379217};
CC KM=5.0 uM for PAH {ECO:0000269|PubMed:12379217};
CC KM=0.5 uM for estrone sulfate {ECO:0000269|PubMed:12379217};
CC KM=0.4 uM for ochratoxin A {ECO:0000269|PubMed:12379217};
CC -!- SUBUNIT: [Isoform 3]: Interacts with ABCA1; this interaction
CC potentiates cholesterol efflux. {ECO:0000269|PubMed:28882873}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28882873,
CC ECO:0000269|PubMed:29300488}; Multi-pass membrane protein
CC {ECO:0000305}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q8K440}. Note=Predominantly expressed on the
CC sinusoidal plasma membrane. {ECO:0000250|UniProtKB:Q8K440}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=O94911-3; Sequence=Displayed;
CC Name=1;
CC IsoId=O94911-1; Sequence=VSP_060912;
CC Name=2;
CC IsoId=O94911-2; Sequence=VSP_060911;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in heart,
CC skeletal muscle and liver (PubMed:12379217, PubMed:28882873,
CC PubMed:29300488). Highly expressed in the superior frontal white matter
CC and inferior temporal white matter (PubMed:12379217).
CC {ECO:0000269|PubMed:12379217, ECO:0000269|PubMed:28882873,
CC ECO:0000269|PubMed:29300488}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74845.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; AB020629; BAA74845.2; ALT_INIT; mRNA.
DR EMBL; AC005922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC024003; AAH24003.1; -; mRNA.
DR EMBL; BC047765; AAH47765.1; -; mRNA.
DR EMBL; BC094689; AAH94689.1; -; mRNA.
DR EMBL; BC130280; AAI30281.1; -; mRNA.
DR CCDS; CCDS11680.1; -. [O94911-1]
DR CCDS; CCDS74139.1; -. [O94911-3]
DR RefSeq; NP_001275914.1; NM_001288985.1. [O94911-3]
DR RefSeq; NP_001275915.1; NM_001288986.1.
DR RefSeq; NP_009099.1; NM_007168.3. [O94911-1]
DR RefSeq; XP_005256995.1; XM_005256938.2.
DR AlphaFoldDB; O94911; -.
DR SMR; O94911; -.
DR BioGRID; 115632; 7.
DR IntAct; O94911; 1.
DR STRING; 9606.ENSP00000467271; -.
DR TCDB; 3.A.1.211.6; the atp-binding cassette (abc) superfamily.
DR GlyGen; O94911; 16 sites.
DR iPTMnet; O94911; -.
DR PhosphoSitePlus; O94911; -.
DR BioMuta; ABCA8; -.
DR jPOST; O94911; -.
DR MassIVE; O94911; -.
DR PaxDb; O94911; -.
DR PeptideAtlas; O94911; -.
DR PRIDE; O94911; -.
DR ProteomicsDB; 11233; -.
DR ProteomicsDB; 50546; -. [O94911-1]
DR ProteomicsDB; 50547; -. [O94911-2]
DR Antibodypedia; 31802; 139 antibodies from 27 providers.
DR DNASU; 10351; -.
DR Ensembl; ENST00000269080.6; ENSP00000269080.1; ENSG00000141338.15. [O94911-1]
DR Ensembl; ENST00000586539.6; ENSP00000467271.1; ENSG00000141338.15. [O94911-3]
DR GeneID; 10351; -.
DR KEGG; hsa:10351; -.
DR MANE-Select; ENST00000586539.6; ENSP00000467271.1; NM_001288985.2; NP_001275914.1.
DR UCSC; uc002jhp.5; human. [O94911-3]
DR CTD; 10351; -.
DR DisGeNET; 10351; -.
DR GeneCards; ABCA8; -.
DR HGNC; HGNC:38; ABCA8.
DR HPA; ENSG00000141338; Low tissue specificity.
DR MIM; 612505; gene.
DR neXtProt; NX_O94911; -.
DR OpenTargets; ENSG00000141338; -.
DR PharmGKB; PA24383; -.
DR VEuPathDB; HostDB:ENSG00000141338; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000162012; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; O94911; -.
DR OMA; IMTTHFL; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; O94911; -.
DR TreeFam; TF105192; -.
DR PathwayCommons; O94911; -.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR SABIO-RK; O94911; -.
DR SignaLink; O94911; -.
DR BioGRID-ORCS; 10351; 13 hits in 1080 CRISPR screens.
DR ChiTaRS; ABCA8; human.
DR GeneWiki; ABCA8; -.
DR GenomeRNAi; 10351; -.
DR Pharos; O94911; Tbio.
DR PRO; PR:O94911; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O94911; protein.
DR Bgee; ENSG00000141338; Expressed in dorsal root ganglion and 190 other tissues.
DR ExpressionAtlas; O94911; baseline and differential.
DR Genevisible; O94911; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; IMP:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; IMP:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0010874; P:regulation of cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0006686; P:sphingomyelin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0042908; P:xenobiotic transport; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR030372; ABCA8.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR PANTHER; PTHR19229:SF148; PTHR19229:SF148; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein;
KW Lipid transport; Membrane; Nucleotide-binding; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1621
FT /note="ABC-type organic anion transporter ABCA8"
FT /id="PRO_0000250677"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 864..884
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1019..1039
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1136..1156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1161..1181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1197..1217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 480..715
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1285..1518
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 516..523
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1323..1330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 797
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 919
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 967
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1435
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 267..1621
FT /note="Missing (in isoform 2)"
FT /id="VSP_060911"
FT VAR_SEQ 598..637
FT /note="Missing (in isoform 1)"
FT /id="VSP_060912"
FT VARIANT 256
FT /note="T -> A (in dbSNP:rs16973446)"
FT /id="VAR_027590"
FT VARIANT 331
FT /note="G -> S (in dbSNP:rs4147979)"
FT /evidence="ECO:0000269|PubMed:12111378"
FT /id="VAR_027591"
FT VARIANT 416
FT /note="A -> V (in dbSNP:rs35621847)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048130"
FT VARIANT 489
FT /note="Y -> F (in dbSNP:rs12150510)"
FT /id="VAR_027592"
FT VARIANT 649
FT /note="P -> R (affects localization at the plasma membrane;
FT loss of cholesterol efflux to APOA1; dbSNP:rs144777539)"
FT /evidence="ECO:0000269|PubMed:28882873"
FT /id="VAR_084139"
FT VARIANT 659
FT /note="L -> R (in dbSNP:rs35844316)"
FT /id="VAR_048131"
FT VARIANT 720
FT /note="C -> G (in dbSNP:rs16973424)"
FT /id="VAR_027593"
FT VARIANT 781..1621
FT /note="Missing (loss of expression; loss of cholesterol
FT efflux to APOA1)"
FT /evidence="ECO:0000269|PubMed:28882873"
FT /id="VAR_084140"
FT VARIANT 1470
FT /note="G -> S (in dbSNP:rs35403175)"
FT /id="VAR_048132"
SQ SEQUENCE 1621 AA; 183677 MW; C50C8E2624BA4734 CRC64;
MRKRKISVCQ QTWALLCKNF LKKWRMKRES LMEWLNSLLL LLCLYIYPHS HQVNDFSSLL
TMDLGRVDTF NESRFSVVYT PVTNTTQQIM NKVASTPFLA GKEVLGLPDE ESIKEFTANY
PEEIVRVTFT NTYSYHLKFL LGHGMPAKKE HKDHTAHCYE TNEDVYCEVS VFWKEGFVAL
QAAINAAIIE ITTNHSVMEE LMSVTGKNMK MHSFIGQSGV ITDLYLFSCI ISFSSFIYYA
SVNVTRERKR MKALMTMMGL RDSAFWLSWG LLYAGFIFIM ALFLALVIRS TQFIILSGFM
VVFSLFLLYG LSLVALAFLM SILVKKSFLT GLVVFLLTVF WGCLGFTSLY RHLPASLEWI
LSLLSPFAFM LGMAQLLHLD YDLNSNAFPH PSDGSNLIVA TNFMLAFDTC LYLALAIYFE
KILPNEYGHR RPPLFFLKSS FWSQTQKTDH VALEDEMDAD PSFHDSFEQA PPEFQGKEAI
RIRNVTKEYK GKPDKIEALK DLVFDIYEGQ ITAILGHSGA GKSTLLNILS GLSVPTKGSV
TIYNNKLSEM ADLENLSKLT GVCPQSNVQF DFLTVRENLR LFAKIKGILP QEVDKEIQRV
LLELEMKNIQ DVLAQNLSGG QKRKLTFGIA ILGDPQIFLL DEPTAGLDPF SRHQVWNLLK
ERKTDRVILF STQFMDEADI LADRKVFLSQ GKLKCAGSSL FLKKKWGIGY HLSLQLNEIC
VEENITSLVK QHIPDAKLSA KSEGKLIYTL PLERTNKFPE LYKDLDSYPD LGIENYGVSM
TTLNEVFLKL EGKSTINESD IAILGEVQAE KADDTERLVE MEQVLSSLNK MRKTIGGVAL
WRQQICAIAR VRLLKLKHER KALLALLLIL MAGFCPLLVE YTMVKIYQNS YTWELSPHLY
FLAPGQQPHD PLTQLLIINK TGASIDDFIQ SVEHQNIALE VDAFGTRNGT DDPSYNGAIT
VCCNEKNYSF SLACNAKRLN CFPVLMDIVS NGLLGMVKPS VHIRTERSTF LENGQDNPIG
FLAYIMFWLV LTSSCPPYIA MSSIDDYKNR ARSQLRISGL SPSAYWFGQA LVDVSLYFLV
FVFIYLMSYI SNFEDMLLTI IHIIQIPCAV GYSFSLIFMT YVISFIFRKG RKNSGIWSFC
FYVVTVFSVA GFAFSIFESD IPFIFTFLIP PATMIGCLFL SSHLLFSSLF SEERMDVQPF
LVFLIPFLHF IIFLFTLRCL EWKFGKKSMR KDPFFRISPR SSDVCQNPEE PEGEDEDVQM
ERVRTANALN STNFDEKPVI IASCLRKEYA GKRKGCFSKR KNKIATRNVS FCVRKGEVLG
LLGHNGAGKS TSIKVITGDT KPTAGQVLLK GSGGGDALEF LGYCPQENAL WPNLTVRQHL
EVYAAVKGLR KGDAEVAITR LVDALKLQDQ LKSPVKTLSE GIKRKLCFVL SILGNPSVVL
LDEPSTGMDP EGQQQMWQAI RATFRNTERG ALLTTHYMAE AEAVCDRVAI MVSGRLRCIG
SIQHLKSKFG KDYLLEMKVK NLAQVEPLHA EILRLFPQAA RQERYSSLMV YKLPVEDVQP
LAQAFFKLEK VKQSFDLEEY SLSQSTLEQV FLELSKEQEL GDFEEDFDPS VKWKLLPQEE
P
