ID ABCG1_HUMAN Reviewed; 678 AA. AC P45844; Q86SU8; Q96L76; Q9BXK6; Q9BXK7; Q9BXK8; Q9BXK9; Q9BXL0; AC Q9BXL1; Q9BXL2; Q9BXL3; Q9BXL4; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 3. DT 11-NOV-2015, entry version 165. DE RecName: Full=ATP-binding cassette sub-family G member 1; DE AltName: Full=ATP-binding cassette transporter 8; DE AltName: Full=White protein homolog; GN Name=ABCG1; Synonyms=ABC8, WHT1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-678 (ISOFORMS 1 AND 4). RC TISSUE=Retina; RX PubMed=8659545; RA Chen H.M., Rossier C., Lalioti M.D., Lynn A., Chakravarti A., RA Perrin G., Antonarakis S.E.; RT "Cloning of the cDNA for a human homologue of the Drosophila white RT gene and mapping to chromosome 21q22.3."; RL Am. J. Hum. Genet. 59:66-75(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=10950923; DOI=10.1006/geno.2000.6253; RA Berry A., Scott H.S., Kudoh J., Talior I., Korostishevsky M., RA Wattenhofer M., Guipponi M., Barras C., Rossier C., Shibuya K., RA Wang J., Kawasaki K., Asakawa S., Minoshima S., Shimizu N., RA Antonarakis S.E., Bonne-Tamir B.; RT "Refined localization of autosomal recessive nonsyndromic deafness RT DFNB10 locus using 34 novel microsatellite markers, genomic structure, RT and exclusion of six known genes in the region."; RL Genomics 68:22-29(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND REPRESSION BY RP ZNF202. RX PubMed=11279031; DOI=10.1074/jbc.M100218200; RA Porsch-Oezcueruemez M., Langmann T., Heimerl S., Borsukova H., RA Kaminski W.E., Drobnik W., Honer C., Schumacher C., Schmitz G.; RT "The zinc finger protein 202 (ZNF202) is a transcriptional repressor RT of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene RT expression and a modulator of cellular lipid efflux."; RL J. Biol. Chem. 276:12427-12433(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND RP 7). RX PubMed=11162488; DOI=10.1006/bbrc.2000.4089; RA Lorkowski S., Rust S., Engel T., Jung E., Tegelkamp K., Galinski E.A., RA Assmann G., Cullen P.; RT "Genomic sequence and structure of the human ABCG1 (ABC8) gene."; RL Biochem. Biophys. Res. Commun. 280:121-131(2001). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND VARIANT LEU-668. RX PubMed=11500512; DOI=10.1074/jbc.M105863200; RA Kennedy M.A., Venkateswaran A., Tarr P.T., Xenarios I., Kudoh J., RA Shimizu N., Edwards P.A.; RT "Characterization of the human ABCG1 gene: liver X receptor activates RT an internal promoter that produces a novel transcript encoding an RT alternative form of the protein."; RL J. Biol. Chem. 276:39438-39447(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1). RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-678. RC TISSUE=Fetal brain; RX PubMed=9034316; DOI=10.1016/S0378-1119(96)00633-6; RA Croop J.M., Tiller G.E., Fletcher J.A., Lux M.L., Raab E., RA Goldenson D., Son D., Arciniegas S., Wu R.; RT "Isolation and characterization of a mammalian homolog of the RT Drosophila white gene."; RL Gene 185:77-85(1997). RN [9] RP INDUCTION, AND PROBABLE FUNCTION. RX PubMed=10799558; DOI=10.1074/jbc.275.19.14700; RA Venkateswaran A., Repa J.J., Lobaccaro J.-M.A., Bronson A., RA Mangelsdorf D.J., Edwards P.A.; RT "Human white/murine ABC8 mRNA levels are highly induced in lipid- RT loaded macrophages. A transcriptional role for specific oxysterols."; RL J. Biol. Chem. 275:14700-14707(2000). RN [10] RP INDUCTION, AND PROBABLE FUNCTION. RX PubMed=10639163; DOI=10.1073/pnas.97.2.817; RA Klucken J., Buechler C., Orso E., Kaminski W.E., RA Porsch-Oezcueruemez M., Liebisch G., Kapinsky M., Diederich W., RA Drobnik W., Dean M., Allikmets R., Schmitz G.; RT "ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a RT regulator of macrophage cholesterol and phospholipid transport."; RL Proc. Natl. Acad. Sci. U.S.A. 97:817-822(2000). RN [11] RP INDUCTION. RX PubMed=12032171; RA Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.; RT "Bacterial lipopolysaccharide induces expression of ABCA1 but not RT ABCG1 via an LXR-independent pathway."; RL J. Lipid Res. 43:952-959(2002). RN [12] RP REVIEW. RX PubMed=11590207; RA Schmitz G., Langmann T., Heimerl S.; RT "Role of ABCG1 and other ABCG family members in lipid metabolism."; RL J. Lipid Res. 42:1513-1520(2001). RN [13] RP TISSUE SPECIFICITY. RX PubMed=11350058; DOI=10.1006/bbrc.2001.4863; RA Lorkowski S., Kratz M., Wenner C., Schmidt R., Weitkamp B., Fobker M., RA Reinhardt J., Rauterberg J., Galinski E.A., Cullen P.; RT "Expression of the ATP-binding cassette transporter gene ABCG1 (ABC8) RT in Tangier disease."; RL Biochem. Biophys. Res. Commun. 283:821-830(2001). RN [14] RP SUBCELLULAR LOCATION, AND MISCELLANEOUS. RX PubMed=22042635; DOI=10.1074/mcp.M111.013458; RA Uhlen M., Oksvold P., Algenas C., Hamsten C., Fagerberg L., RA Klevebring D., Lundberg E., Odeberg J., Ponten F., Kondo T., RA Sivertsson A.; RT "Antibody-based protein profiling of the human chromosome 21."; RL Mol. Cell. Proteomics 11:0-0(2012). RN [15] RP PALMITOYLATION AT CYS-30; CYS-154; CYS-315; CYS-394 AND CYS-406, AND RP MUTAGENESIS OF CYS-30; CYS-154; CYS-315; CYS-394 AND CYS-406. RX PubMed=23388354; DOI=10.1016/j.bbalip.2013.01.019; RA Gu H.M., Li G., Gao X., Berthiaume L.G., Zhang D.W.; RT "Characterization of palmitoylation of ATP binding cassette RT transporter G1: Effect on protein trafficking and function."; RL Biochim. Biophys. Acta 1831:1067-1078(2013). CC -!- FUNCTION: Transporter involved in macrophage lipid homeostasis. Is CC an active component of the macrophage lipid export complex. Could CC also be involved in intracellular lipid transport processes. The CC role in cellular lipid homeostasis may not be limited to CC macrophages. CC -!- SUBUNIT: May form heterodimers with several heterologous partners CC of the ABCG subfamily. CC -!- INTERACTION: CC Q9H172:ABCG4; NbExp=2; IntAct=EBI-8584087, EBI-8584118; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:22042635}; Multi-pass membrane protein CC {ECO:0000269|PubMed:22042635}. Golgi apparatus membrane CC {ECO:0000269|PubMed:22042635}; Multi-pass membrane protein CC {ECO:0000269|PubMed:22042635}. Note=Predominantly localized in the CC intracellular compartments mainly associated with the endoplasmic CC reticulum (ER) and Golgi membranes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=P45844-1; Sequence=Displayed; CC Name=2; Synonyms=J; CC IsoId=P45844-2; Sequence=VSP_000047, VSP_000051; CC Name=3; Synonyms=ABDE; CC IsoId=P45844-3; Sequence=VSP_000048, VSP_000051; CC Name=4; Synonyms=G; CC IsoId=P45844-4; Sequence=VSP_000051; CC Name=5; Synonyms=F; CC IsoId=P45844-5; Sequence=VSP_000049, VSP_000051; CC Name=6; Synonyms=HI; CC IsoId=P45844-6; Sequence=VSP_000046, VSP_000051; CC Name=7; Synonyms=C; CC IsoId=P45844-7; Sequence=VSP_000050, VSP_000051; CC Name=8; CC IsoId=P45844-8; Sequence=VSP_010718; CC -!- TISSUE SPECIFICITY: Expressed in several tissues. Expressed in CC macrophages; expression is increased in macrophages from patients CC with Tangier disease. {ECO:0000269|PubMed:11350058}. CC -!- INDUCTION: Strongly induced in monocyte-derived macrophages during CC cholesterol influx. Conversely, mRNA and protein expression are CC suppressed by lipid efflux. Induction is mediated by the liver X CC receptor/retinoid X receptor (LXR/RXR) pathway. Not induced by CC bacterial lipopolysaccharides (LPS). Repressed by ZNF202. CC {ECO:0000269|PubMed:10639163, ECO:0000269|PubMed:10799558, CC ECO:0000269|PubMed:11279031, ECO:0000269|PubMed:12032171}. CC -!- PTM: Palmitoylation at Cys-315 seems important for trafficking CC from the endoplasmic reticulum. {ECO:0000269|PubMed:23388354}. CC -!- MISCELLANEOUS: A protein of the expected size has been detected by CC antibody binding and Western blot in at least one of the analyzed CC tissues or cells. {ECO:0000305|PubMed:22042635}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG CC family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-2 domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC51098.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAK28841.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAA95530.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=BAB13728.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=CAA62631.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=CAC00730.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P45844"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X91249; CAA62631.1; ALT_INIT; mRNA. DR EMBL; AB038161; BAB13728.2; ALT_INIT; Genomic_DNA. DR EMBL; AJ289137; CAC00730.1; ALT_INIT; Genomic_DNA. DR EMBL; AJ289138; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289139; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289140; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289141; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289142; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289143; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289144; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289145; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289146; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289147; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289148; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289149; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289150; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289151; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AF323658; AAK28836.1; -; Genomic_DNA. DR EMBL; AF323644; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323645; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323664; AAK28842.1; -; mRNA. DR EMBL; AF323658; AAK28833.1; -; Genomic_DNA. DR EMBL; AF323640; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323645; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323660; AAK28838.1; -; mRNA. DR EMBL; AF323663; AAK28841.1; ALT_INIT; mRNA. DR EMBL; AF323658; AAK28835.1; -; Genomic_DNA. DR EMBL; AF323642; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323645; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323662; AAK28840.1; -; mRNA. DR EMBL; AF323658; AAK28837.1; -; Genomic_DNA. DR EMBL; AF323643; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323645; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323658; AAK28834.1; -; Genomic_DNA. DR EMBL; AF323645; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323661; AAK28839.1; -; mRNA. DR EMBL; AY048757; AAL06598.1; -; mRNA. DR EMBL; AP001746; BAA95530.1; ALT_INIT; Genomic_DNA. DR EMBL; BC029158; AAH29158.2; -; mRNA. DR EMBL; U34919; AAC51098.1; ALT_INIT; mRNA. DR CCDS; CCDS13681.1; -. [P45844-5] DR CCDS; CCDS13682.1; -. [P45844-1] DR CCDS; CCDS13683.1; -. [P45844-2] DR CCDS; CCDS42937.1; -. [P45844-3] DR CCDS; CCDS42938.1; -. [P45844-4] DR RefSeq; NP_004906.3; NM_004915.3. [P45844-1] DR RefSeq; NP_058198.2; NM_016818.2. [P45844-4] DR RefSeq; NP_997057.1; NM_207174.1. [P45844-2] DR RefSeq; NP_997510.1; NM_207627.1. [P45844-3] DR RefSeq; NP_997511.1; NM_207628.1. [P45844-7] DR RefSeq; NP_997512.1; NM_207629.1. [P45844-5] DR UniGene; Hs.124649; -. DR UniGene; Hs.418279; -. DR ProteinModelPortal; P45844; -. DR SMR; P45844; 9-323. DR BioGrid; 114980; 1. DR IntAct; P45844; 2. DR STRING; 9606.ENSP00000354995; -. DR DrugBank; DB00171; Adenosine triphosphate. DR TCDB; 3.A.1.204.12; the atp-binding cassette (abc) superfamily. DR PhosphoSite; P45844; -. DR BioMuta; ABCG1; -. DR DMDM; 17433715; -. DR MaxQB; P45844; -. DR PaxDb; P45844; -. DR PRIDE; P45844; -. DR DNASU; 9619; -. DR Ensembl; ENST00000343687; ENSP00000339744; ENSG00000160179. [P45844-2] DR Ensembl; ENST00000347800; ENSP00000291524; ENSG00000160179. [P45844-5] DR Ensembl; ENST00000361802; ENSP00000354995; ENSG00000160179. [P45844-1] DR Ensembl; ENST00000398449; ENSP00000381467; ENSG00000160179. [P45844-4] DR Ensembl; ENST00000398457; ENSP00000381475; ENSG00000160179. [P45844-3] DR GeneID; 9619; -. DR KEGG; hsa:9619; -. DR UCSC; uc002zam.3; human. [P45844-7] DR UCSC; uc002zan.3; human. [P45844-3] DR UCSC; uc002zao.3; human. [P45844-5] DR UCSC; uc002zap.3; human. [P45844-4] DR UCSC; uc002zaq.3; human. [P45844-1] DR UCSC; uc002zar.3; human. [P45844-2] DR CTD; 9619; -. DR GeneCards; ABCG1; -. DR HGNC; HGNC:73; ABCG1. DR HPA; HPA031470; -. DR HPA; HPA031471; -. DR MIM; 603076; gene. DR neXtProt; NX_P45844; -. DR PharmGKB; PA24408; -. DR eggNOG; KOG0061; Eukaryota. DR eggNOG; COG1131; LUCA. DR GeneTree; ENSGT00740000114855; -. DR HOVERGEN; HBG103052; -. DR InParanoid; P45844; -. DR KO; K05679; -. DR OMA; ASMEGCH; -. DR OrthoDB; EOG7KWSGT; -. DR PhylomeDB; P45844; -. DR TreeFam; TF105210; -. DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis. DR Reactome; R-HSA-194223; HDL-mediated lipid transport. DR ChiTaRS; ABCG1; human. DR GeneWiki; ABCG1; -. DR GenomeRNAi; 9619; -. DR NextBio; 36087; -. DR PRO; PR:P45844; -. DR Proteomes; UP000005640; Chromosome 21. DR Bgee; P45844; -. DR ExpressionAtlas; P45844; baseline and differential. DR Genevisible; P45844; HS. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; ISS:BHF-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0055037; C:recycling endosome; ISS:BHF-UCL. DR GO; GO:0043531; F:ADP binding; IDA:BHF-UCL. DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL. DR GO; GO:0015485; F:cholesterol binding; IC:BHF-UCL. DR GO; GO:0017127; F:cholesterol transporter activity; IDA:BHF-UCL. DR GO; GO:0034437; F:glycoprotein transporter activity; IDA:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IC:BHF-UCL. DR GO; GO:0005548; F:phospholipid transporter activity; IDA:BHF-UCL. DR GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0034041; F:sterol-transporting ATPase activity; IDA:BHF-UCL. DR GO; GO:0019534; F:toxin transporter activity; IDA:BHF-UCL. DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IDA:BHF-UCL. DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL. DR GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL. DR GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL. DR GO; GO:0009720; P:detection of hormone stimulus; NAS:UniProtKB. DR GO; GO:0034436; P:glycoprotein transport; IDA:BHF-UCL. DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:BHF-UCL. DR GO; GO:0032367; P:intracellular cholesterol transport; IMP:BHF-UCL. DR GO; GO:0042157; P:lipoprotein metabolic process; TAS:Reactome. DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISS:BHF-UCL. DR GO; GO:0010887; P:negative regulation of cholesterol storage; TAS:BHF-UCL. DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; TAS:BHF-UCL. DR GO; GO:0033700; P:phospholipid efflux; IMP:BHF-UCL. DR GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL. DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISS:BHF-UCL. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl. DR GO; GO:0010872; P:regulation of cholesterol esterification; ISS:BHF-UCL. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:BHF-UCL. DR GO; GO:0055099; P:response to high density lipoprotein particle; IEA:Ensembl. DR GO; GO:0033993; P:response to lipid; IDA:BHF-UCL. DR GO; GO:0010033; P:response to organic substance; IDA:UniProtKB. DR GO; GO:0043691; P:reverse cholesterol transport; ISS:BHF-UCL. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:1901998; P:toxin transport; IDA:GOC. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013525; ABC_2_trans. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR020064; ABCG1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005284; Pigment_permease. DR PANTHER; PTHR19241:SF177; PTHR19241:SF177; 1. DR Pfam; PF01061; ABC2_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00955; 3a01204; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Complete proteome; KW Endoplasmic reticulum; Golgi apparatus; Lipid transport; Lipoprotein; KW Membrane; Nucleotide-binding; Palmitate; Polymorphism; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 678 ATP-binding cassette sub-family G member FT 1. FT /FTId=PRO_0000093384. FT TOPO_DOM 1 426 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 427 445 Helical. {ECO:0000255}. FT TOPO_DOM 446 456 Extracellular. {ECO:0000255}. FT TRANSMEM 457 477 Helical. {ECO:0000255}. FT TOPO_DOM 478 506 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 507 525 Helical. {ECO:0000255}. FT TOPO_DOM 526 533 Extracellular. {ECO:0000255}. FT TRANSMEM 534 555 Helical. {ECO:0000255}. FT TOPO_DOM 556 567 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 568 586 Helical. {ECO:0000255}. FT TOPO_DOM 587 649 Extracellular. {ECO:0000255}. FT TRANSMEM 650 669 Helical. {ECO:0000255}. FT TOPO_DOM 670 678 Cytoplasmic. {ECO:0000255}. FT DOMAIN 77 317 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 415 673 ABC transmembrane type-2. FT NP_BIND 118 125 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT LIPID 30 30 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:23388354}. FT LIPID 154 154 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:23388354}. FT LIPID 315 315 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:23388354}. FT LIPID 394 394 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:23388354}. FT LIPID 406 406 S-palmitoyl cysteine. FT {ECO:0000269|PubMed:23388354}. FT VAR_SEQ 1 95 MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNM FT EATETDLLNGHLKKVDNNLTEAQRFSSLPRRAAVNIEFRDL FT SYSVPEGPWWRKK -> MVRRGWSVCTAILLARLWCLVPTH FT TFLSEYPEAAEYPHPGWVYWLQMAVAPGHLRAWVMRNNVTT FT NIPSAFSGTLTHEEKAVLTVFTGTATAVHVQVAALASAKLE FT SSVFVTDCVSCKIENVCDSALQGKRVPMSGLQGSSIVIMPP FT SNRPLASAASCTWSVQVQGGPHHLGVVAISGKVLSAAHGAG FT RAYGWGFPGDPMEE (in isoform 8). FT {ECO:0000303|PubMed:11500512}. FT /FTId=VSP_010718. FT VAR_SEQ 1 22 Missing (in isoform 7). FT {ECO:0000303|PubMed:11162488}. FT /FTId=VSP_000050. FT VAR_SEQ 1 14 MACLMAAFSVGTAM -> MRISLPRAPERDGGVSASSLLDT FT VT (in isoform 2). FT {ECO:0000303|PubMed:11162488}. FT /FTId=VSP_000047. FT VAR_SEQ 1 14 MACLMAAFSVGTAM -> MLGTQGWTKQRKPCPQ (in FT isoform 3). FT {ECO:0000303|PubMed:11162488}. FT /FTId=VSP_000048. FT VAR_SEQ 1 14 MACLMAAFSVGTAM -> MIMRLPQPHGT (in isoform FT 5). {ECO:0000303|PubMed:11162488}. FT /FTId=VSP_000049. FT VAR_SEQ 1 4 Missing (in isoform 6). FT {ECO:0000303|PubMed:11162488}. FT /FTId=VSP_000046. FT VAR_SEQ 375 386 Missing (in isoform 2, isoform 3, isoform FT 4, isoform 5, isoform 6 and isoform 7). FT {ECO:0000303|PubMed:11162488, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8659545}. FT /FTId=VSP_000051. FT VARIANT 668 668 F -> L. {ECO:0000269|PubMed:11500512}. FT /FTId=VAR_012279. FT MUTAGEN 30 30 C->A: No significant effect. FT {ECO:0000269|PubMed:23388354}. FT MUTAGEN 154 154 C->A: No significant effect. FT {ECO:0000269|PubMed:23388354}. FT MUTAGEN 315 315 C->A,S: Significantly decreases ABCG1- FT mediated cholesterol efflux. FT {ECO:0000269|PubMed:23388354}. FT MUTAGEN 394 394 C->A: No significant effect. FT {ECO:0000269|PubMed:23388354}. FT MUTAGEN 406 406 C->A: No significant effect. FT {ECO:0000269|PubMed:23388354}. FT CONFLICT 38 38 S -> T (in Ref. 4; AAK28839/AAK28841). FT {ECO:0000305}. FT CONFLICT 448 448 A -> T (in Ref. 1; CAA62631, 4; AAK28838/ FT AAK28839/AAK28840/AAK28841/AAK28842 and FT 5; AAL06598). {ECO:0000305}. FT CONFLICT 533 533 R -> A (in Ref. 8; AAC51098). FT {ECO:0000305}. SQ SEQUENCE 678 AA; 75592 MW; B901CABDA6C19E09 CRC64; MACLMAAFSV GTAMNASSYS AEMTEPKSVC VSVDEVVSSN MEATETDLLN GHLKKVDNNL TEAQRFSSLP RRAAVNIEFR DLSYSVPEGP WWRKKGYKTL LKGISGKFNS GELVAIMGPS GAGKSTLMNI LAGYRETGMK GAVLINGLPR DLRCFRKVSC YIMQDDMLLP HLTVQEAMMV SAHLKLQEKD EGRREMVKEI LTALGLLSCA NTRTGSLSGG QRKRLAIALE LVNNPPVMFF DEPTSGLDSA SCFQVVSLMK GLAQGGRSII CTIHQPSAKL FELFDQLYVL SQGQCVYRGK VCNLVPYLRD LGLNCPTYHN PADFVMEVAS GEYGDQNSRL VRAVREGMCD SDHKRDLGGD AEVNPFLWHR PSEEVKQTKR LKGLRKDSSS MEGCHSFSAS CLTQFCILFK RTFLSIMRDS VLTHLRITSH IGIGLLIGLL YLGIGNEAKK VLSNSGFLFF SMLFLMFAAL MPTVLTFPLE MGVFLREHLN YWYSLKAYYL AKTMADVPFQ IMFPVAYCSI VYWMTSQPSD AVRFVLFAAL GTMTSLVAQS LGLLIGAAST SLQVATFVGP VTAIPVLLFS GFFVSFDTIP TYLQWMSYIS YVRYGFEGVI LSIYGLDRED LHCDIDETCH FQKSEAILRE LDVENAKLYL DFIVLGIFFI SLRLIAYFVL RYKIRAER //