ABCG1_MOUSE
ID ABCG1_MOUSE Reviewed; 666 AA.
AC Q64343;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=ATP-binding cassette sub-family G member 1 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:P45844};
DE AltName: Full=ATP-binding cassette transporter 8;
DE AltName: Full=White protein homolog;
GN Name=Abcg1 {ECO:0000312|MGI:MGI:107704}; Synonyms=Abc8, Wht1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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., Goldenson D.,
RA Son D., Arciniegas S., Wu R.;
RT "Isolation and characterization of a mammalian homolog of the Drosophila
RT white gene.";
RL Gene 185:77-85(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J;
RX PubMed=8703120; DOI=10.1007/s003359900203;
RA Savary S., Denizot F., Luciani M.-F., Mattei M.-G., Chimini G.;
RT "Molecular cloning of a mammalian ABC transporter homologous to Drosophila
RT white gene.";
RL Mamm. Genome 7:673-676(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [4]
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-loaded
RT macrophages. A transcriptional role for specific oxysterols.";
RL J. Biol. Chem. 275:14700-14707(2000).
RN [5]
RP FUNCTION.
RX PubMed=14668945; DOI=10.1358/dnp.2003.16.8.829346;
RA Ito T.;
RT "Physiological function of ABCG1.";
RL Drug News Perspect. 16:490-492(2003).
RN [6]
RP DOWN-REGULATION BY ENDOTOXIN.
RX PubMed=12777468; DOI=10.1194/jlr.m300100-jlr200;
RA Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C., Feingold K.R.;
RT "Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and
RT ABCG1 in J774 murine macrophages: differential role of LXR.";
RL J. Lipid Res. 44:1728-1736(2003).
RN [7]
RP PALMITOYLATION.
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 transporter G1:
RT Effect on protein trafficking and function.";
RL Biochim. Biophys. Acta 1831:1067-1078(2013).
CC -!- FUNCTION: Catalyzes the efflux of phospholipids such as sphingomyelin,
CC cholesterol and its oxygenated derivatives like 7beta-
CC hydroxycholesterol and this transport is coupled to hydrolysis of ATP
CC (PubMed:14668945). The lipid efflux is ALB-dependent. Is an active
CC component of the macrophage lipid export complex. Could also be
CC involved in intracellular lipid transport processes. The role in
CC cellular lipid homeostasis may not be limited to macrophages. Prevents
CC cell death by transporting cytotoxic 7beta-hydroxycholesterol (By
CC similarity). {ECO:0000250|UniProtKB:P45844,
CC ECO:0000269|PubMed:14668945}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7beta-hydroxycholesterol(in) + ATP + H2O = 7beta-
CC hydroxycholesterol(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:39795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:42989, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P45844};
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:0000250|UniProtKB:P45844};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-(acyl)-sphingosylphosphocholine(in) + ATP + H2O = ADP +
CC an N-(acyl)-sphingosylphosphocholine(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:46468, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64583,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P45844};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP +
CC H(+) + phosphate; Xref=Rhea:RHEA:38903, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P45844};
CC -!- ACTIVITY REGULATION: The cholesterol efflux is enhanced by APOA1.
CC {ECO:0000250|UniProtKB:P45844}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homooligomer. May form
CC heterodimers with several heterologous partners of the ABCG subfamily.
CC Forms heterodimers with ABCG4. Interacts with CAV1; this interaction
CC regulates ABCG1-mediated cholesterol efflux.
CC {ECO:0000250|UniProtKB:P45844}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P45844}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P45844}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:P45844}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P45844}. Cell membrane
CC {ECO:0000250|UniProtKB:P45844}. Note=Predominantly localized in the
CC intracellular compartments mainly associated with the endoplasmic
CC reticulum (ER) and Golgi membranes. {ECO:0000250|UniProtKB:P45844}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in brain, thymus, lung, adrenals,
CC spleen and placenta. Little or no expression in liver, kidney, heart,
CC muscle or testes.
CC -!- INDUCTION: Strongly induced in macrophage cell line RAW 264.7 during
CC cholesterol influx. Induction is mediated by the liver X
CC receptor/retinoid X receptor (LXR/RXR) pathway. Down-regulated by
CC endotoxins or cytokines (TNF and IL1) in J-774 macrophages.
CC {ECO:0000269|PubMed:10799558}.
CC -!- PTM: Palmitoylation at Cys-315 seems important for trafficking from the
CC endoplasmic reticulum. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; U34920; AAB47738.1; -; mRNA.
DR EMBL; Z48745; CAA88636.1; -; mRNA.
DR EMBL; AF323659; AAK27442.1; -; mRNA.
DR CCDS; CCDS28602.1; -.
DR RefSeq; NP_033723.1; NM_009593.2.
DR AlphaFoldDB; Q64343; -.
DR SMR; Q64343; -.
DR CORUM; Q64343; -.
DR STRING; 10090.ENSMUSP00000024829; -.
DR iPTMnet; Q64343; -.
DR PhosphoSitePlus; Q64343; -.
DR SwissPalm; Q64343; -.
DR MaxQB; Q64343; -.
DR PaxDb; Q64343; -.
DR PRIDE; Q64343; -.
DR ProteomicsDB; 285818; -.
DR Antibodypedia; 23734; 410 antibodies from 35 providers.
DR DNASU; 11307; -.
DR Ensembl; ENSMUST00000024829; ENSMUSP00000024829; ENSMUSG00000024030.
DR GeneID; 11307; -.
DR KEGG; mmu:11307; -.
DR UCSC; uc008buj.2; mouse.
DR CTD; 9619; -.
DR MGI; MGI:107704; Abcg1.
DR VEuPathDB; HostDB:ENSMUSG00000024030; -.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000160131; -.
DR HOGENOM; CLU_000604_57_6_1; -.
DR InParanoid; Q64343; -.
DR OMA; IRIAMYM; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q64343; -.
DR TreeFam; TF105210; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-MMU-8964058; HDL remodeling.
DR BioGRID-ORCS; 11307; 2 hits in 79 CRISPR screens.
DR ChiTaRS; Abcg1; mouse.
DR PRO; PR:Q64343; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q64343; protein.
DR Bgee; ENSMUSG00000024030; Expressed in peripheral lymph node and 245 other tissues.
DR ExpressionAtlas; Q64343; baseline and differential.
DR Genevisible; Q64343; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:BHF-UCL.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:BHF-UCL.
DR GO; GO:0034041; F:ABC-type sterol transporter activity; ISO:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:MGI.
DR GO; GO:0140328; F:floppase activity; ISO:MGI.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; ISO:MGI.
DR GO; GO:0071403; P:cellular response to high density lipoprotein particle stimulus; IDA:BHF-UCL.
DR GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
DR GO; GO:0030301; P:cholesterol transport; IDA:MGI.
DR GO; GO:0034436; P:glycoprotein transport; ISO:MGI.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR GO; GO:0032367; P:intracellular cholesterol transport; ISO:MGI.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR GO; GO:0010888; P:negative regulation of lipid storage; IMP:BHF-UCL.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
DR GO; GO:0033700; P:phospholipid efflux; ISO:MGI.
DR GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:BHF-UCL.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:1904411; P:positive regulation of secretory granule organization; ISO:MGI.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:BHF-UCL.
DR GO; GO:0033993; P:response to lipid; ISO:MGI.
DR GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR020064; ABCG1.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005284; Pigment_permease/Abcg.
DR PANTHER; PTHR48041:SF90; PTHR48041:SF90; 1.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 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 ATP-binding; Cell membrane; Endoplasmic reticulum; Golgi apparatus;
KW Lipid transport; Lipoprotein; Membrane; Nucleotide-binding; Palmitate;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..666
FT /note="ATP-binding cassette sub-family G member 1"
FT /id="PRO_0000093385"
FT TOPO_DOM 1..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 556..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..637
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 638..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 77..317
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 403..661
FT /note="ABC transmembrane type-2"
FT BINDING 118..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT LIPID 30
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 154
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 315
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 394
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 666 AA; 74033 MW; EDDC6AFBD43950B6 CRC64;
MACLMAAFSV GTAMNASSYS AAMTEPKSVC VSVDEVVSSN VDEVETDLLN GHLKKVDNNF
TEAQRFSSLP RRAAVNIEFK DLSYSVPEGP WWKKKGYKTL LKGISGKFNS GELVAIMGPS
GAGKSTLMNI LAGYRETGMK GAVLINGMPR DLRCFRKVSC YIMQDDMLLP HLTVQEAMMV
SAHLKLQEKD EGRREMVKEI LTALGLLPCA NTRTGSLSGG QRKRLAIALE LVNNPPVMFF
DEPTSGLDSA SCFQVVSLMK GLAQGGRSIV CTIHQPSAKL FELFDQLYVL SQGQCVYRGK
VSNLVPYLRD LGLNCPTYHN PADFVMEVAS GEYGDQNSRL VRAVREGMCD ADYKRDLGGD
TDVNPFLWHR PAEEDSASME GCHSFSASCL TQFCILFKRT FLSIMRDSVL THLRITSHIG
IGLLIGLLYL GIGNEAKKVL SNSGFLFFSM LFLMFAALMP TVLTFPLEMS VFLREHLNYW
YSLKAYYLAK TMADVPFQIM FPVAYCSIVY WMTSQPSDAV RFVLFAALGT MTSLVAQSLG
LLIGAASTSL QVATFVGPVT AIPVLLFSGF FVSFDTIPAY LQWMSYISYV RYGFEGVILS
IYGLDREDLH CDIAETCHFQ KSEAILRELD VENAKLYLDF IVLGIFFISL RLIAYFVLRY
KIRAER
