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   27-MAR-2024, entry version 197.
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   BioGRID; 197904; 1.
DR   CORUM; Q64343; -.
DR   STRING; 10090.ENSMUSP00000024829; -.
DR   GlyGen; Q64343; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q64343; -.
DR   PhosphoSitePlus; Q64343; -.
DR   SwissPalm; Q64343; -.
DR   MaxQB; Q64343; -.
DR   PaxDb; 10090-ENSMUSP00000024829; -.
DR   ProteomicsDB; 285818; -.
DR   Antibodypedia; 23734; 491 antibodies from 35 providers.
DR   DNASU; 11307; -.
DR   Ensembl; ENSMUST00000024829.8; ENSMUSP00000024829.7; ENSMUSG00000024030.8.
DR   GeneID; 11307; -.
DR   KEGG; mmu:11307; -.
DR   UCSC; uc008buj.2; mouse.
DR   AGR; MGI:107704; -.
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; TILKCVN; -.
DR   OrthoDB; 1126902at2759; -.
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 84 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 247 other cell types or tissues.
DR   ExpressionAtlas; Q64343; baseline and differential.
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: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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   CDD; cd03213; ABCG_EPDR; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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; IPR043926; ABCG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005284; Pigment_permease/Abcg.
DR   NCBIfam; TIGR00955; 3a01204; 1.
DR   PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR   PANTHER; PTHR48041:SF90; ATP-BINDING CASSETTE SUB-FAMILY G MEMBER 1; 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; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   Genevisible; Q64343; MM.
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
//