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   24-JAN-2024, entry version 179.
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 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   GlyCosmos; O94911; 16 sites, No reported glycans.
DR   GlyGen; O94911; 16 sites.
DR   iPTMnet; O94911; -.
DR   PhosphoSitePlus; O94911; -.
DR   SwissPalm; O94911; -.
DR   BioMuta; ABCA8; -.
DR   jPOST; O94911; -.
DR   MassIVE; O94911; -.
DR   PaxDb; 9606-ENSP00000467271; -.
DR   PeptideAtlas; O94911; -.
DR   ProteomicsDB; 11233; -.
DR   ProteomicsDB; 50546; -. [O94911-1]
DR   ProteomicsDB; 50547; -. [O94911-2]
DR   Antibodypedia; 31802; 155 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   AGR; HGNC:38; -.
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; GVCYHMP; -.
DR   OrthoDB; 6951at2759; -.
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 1162 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 192 other cell types or tissues.
DR   ExpressionAtlas; O94911; baseline and differential.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd03263; ABC_subfamily_A; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR026082; ABCA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR19229:SF148; ABC-TYPE ORGANIC ANION TRANSPORTER ABCA8; 1.
DR   PANTHER; PTHR19229; ATP-BINDING CASSETTE TRANSPORTER SUBFAMILY A ABCA; 1.
DR   Pfam; PF12698; ABC2_membrane_3; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   Genevisible; O94911; HS.
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
//