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ATP-binding cassette sub-family G member 1 (ATP-binding cassette transporter 8) (White protein homolog)

 ABCG1_MOUSE             Reviewed;         666 AA.
Q64343;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=ATP-binding cassette sub-family G member 1;
AltName: Full=ATP-binding cassette transporter 8;
AltName: Full=White protein homolog;
Name=Abcg1; Synonyms=Abc8, Wht1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9034316; DOI=10.1016/S0378-1119(96)00633-6;
Croop J.M., Tiller G.E., Fletcher J.A., Lux M.L., Raab E.,
Goldenson D., Son D., Arciniegas S., Wu R.;
"Isolation and characterization of a mammalian homolog of the
Drosophila white gene.";
Gene 185:77-85(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=DBA/2J;
PubMed=8703120; DOI=10.1007/s003359900203;
Savary S., Denizot F., Luciani M.-F., Mattei M.-G., Chimini G.;
"Molecular cloning of a mammalian ABC transporter homologous to
Drosophila white gene.";
Mamm. Genome 7:673-676(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11162488; DOI=10.1006/bbrc.2000.4089;
Lorkowski S., Rust S., Engel T., Jung E., Tegelkamp K., Galinski E.A.,
Assmann G., Cullen P.;
"Genomic sequence and structure of the human ABCG1 (ABC8) gene.";
Biochem. Biophys. Res. Commun. 280:121-131(2001).
[4]
INDUCTION, AND PROBABLE FUNCTION.
PubMed=10799558; DOI=10.1074/jbc.275.19.14700;
Venkateswaran A., Repa J.J., Lobaccaro J.-M.A., Bronson A.,
Mangelsdorf D.J., Edwards P.A.;
"Human white/murine ABC8 mRNA levels are highly induced in lipid-
loaded macrophages. A transcriptional role for specific oxysterols.";
J. Biol. Chem. 275:14700-14707(2000).
[5]
REVIEW.
PubMed=11590207;
Schmitz G., Langmann T., Heimerl S.;
"Role of ABCG1 and other ABCG family members in lipid metabolism.";
J. Lipid Res. 42:1513-1520(2001).
[6]
FUNCTION.
PubMed=14668945;
Ito T.;
"Physiological function of ABCG1.";
Drug News Perspect. 16:490-492(2003).
[7]
DOWN-REGULATION BY ENDOTOXIN.
PubMed=12777468; DOI=10.1194/jlr.M300100-JLR200;
Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C.,
Feingold K.R.;
"Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and
ABCG1 in J774 murine macrophages: differential role of LXR.";
J. Lipid Res. 44:1728-1736(2003).
[8]
PALMITOYLATION.
PubMed=23388354; DOI=10.1016/j.bbalip.2013.01.019;
Gu H.M., Li G., Gao X., Berthiaume L.G., Zhang D.W.;
"Characterization of palmitoylation of ATP binding cassette
transporter G1: Effect on protein trafficking and function.";
Biochim. Biophys. Acta 1831:1067-1078(2013).
-!- FUNCTION: Transporter involved in macrophage lipid homeostasis. Is
an active component of the macrophage lipid export complex. Could
also be involved in intracellular lipid transport processes. The
role in cellular lipid homeostasis may not be limited to
macrophages. {ECO:0000269|PubMed:14668945}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed mainly in brain, thymus, lung,
adrenals, spleen and placenta. Little or no expression in liver,
kidney, heart, muscle or testes.
-!- INDUCTION: Strongly induced in macrophage cell line RAW 264.7
during cholesterol influx. Induction is mediated by the liver X
receptor/retinoid X receptor (LXR/RXR) pathway. Down-regulated by
endotoxins or cytokines (TNF and IL1) in J-774 macrophages.
{ECO:0000269|PubMed:10799558}.
-!- PTM: Palmitoylation at Cys-315 seems important for trafficking
from the endoplasmic reticulum. {ECO:0000250}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG
family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U34920; AAB47738.1; -; mRNA.
EMBL; Z48745; CAA88636.1; -; mRNA.
EMBL; AF323659; AAK27442.1; -; mRNA.
CCDS; CCDS28602.1; -.
RefSeq; NP_033723.1; NM_009593.2.
UniGene; Mm.15691; -.
UniGene; Mm.470747; -.
ProteinModelPortal; Q64343; -.
SMR; Q64343; -.
CORUM; Q64343; -.
STRING; 10090.ENSMUSP00000024829; -.
iPTMnet; Q64343; -.
PhosphoSitePlus; Q64343; -.
MaxQB; Q64343; -.
PaxDb; Q64343; -.
PRIDE; Q64343; -.
Ensembl; ENSMUST00000024829; ENSMUSP00000024829; ENSMUSG00000024030.
GeneID; 11307; -.
KEGG; mmu:11307; -.
UCSC; uc008buj.2; mouse.
CTD; 9619; -.
MGI; MGI:107704; Abcg1.
eggNOG; KOG0061; Eukaryota.
eggNOG; COG1131; LUCA.
GeneTree; ENSGT00740000114855; -.
HOGENOM; HOG000236364; -.
HOVERGEN; HBG103052; -.
InParanoid; Q64343; -.
KO; K05679; -.
OMA; VYVLVVY; -.
OrthoDB; EOG091G050S; -.
PhylomeDB; Q64343; -.
TreeFam; TF105210; -.
Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
Reactome; R-MMU-8964058; HDL remodeling.
PRO; PR:Q64343; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024030; -.
ExpressionAtlas; Q64343; baseline and differential.
Genevisible; Q64343; MM.
GO; GO:0005768; C:endosome; IDA:BHF-UCL.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0055037; C:recycling endosome; IDA:BHF-UCL.
GO; GO:0043531; F:ADP binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; ISO:MGI.
GO; GO:0017127; F:cholesterol transporter activity; ISO:MGI.
GO; GO:0034437; F:glycoprotein transporter activity; ISO:MGI.
GO; GO:0005548; F:phospholipid transporter activity; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0034041; F:sterol-transporting ATPase activity; ISO:MGI.
GO; GO:0019534; F:toxin transporter activity; ISO:MGI.
GO; GO:0042987; P:amyloid precursor protein catabolic process; ISO:MGI.
GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
GO; GO:0042632; P:cholesterol homeostasis; ISO:MGI.
GO; GO:0008203; P:cholesterol metabolic process; ISO:MGI.
GO; GO:0030301; P:cholesterol transport; IDA:MGI.
GO; GO:0034436; P:glycoprotein transport; ISO:MGI.
GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP:BHF-UCL.
GO; GO:0032367; P:intracellular cholesterol transport; ISO:MGI.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IMP:BHF-UCL.
GO; GO:0010888; P:negative regulation of lipid storage; IMP:BHF-UCL.
GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:0033700; P:phospholipid efflux; ISO:MGI.
GO; GO:0055091; P:phospholipid homeostasis; ISO:MGI.
GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IMP:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:BHF-UCL.
GO; GO:0010872; P:regulation of cholesterol esterification; IMP:BHF-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0055099; P:response to high density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0033993; P:response to lipid; ISO:MGI.
GO; GO:0010033; P:response to organic substance; ISO:MGI.
GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR020064; ABCG1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005284; Pigment_permease.
PANTHER; PTHR19241:SF177; PTHR19241:SF177; 1.
Pfam; PF01061; ABC2_membrane; 1.
Pfam; PF00005; ABC_tran; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00955; 3a01204; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Lipid transport; Lipoprotein;
Membrane; Nucleotide-binding; Palmitate; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 666 ATP-binding cassette sub-family G member
1.
/FTId=PRO_0000093385.
TOPO_DOM 1 414 Cytoplasmic. {ECO:0000255}.
TRANSMEM 415 433 Helical. {ECO:0000255}.
TOPO_DOM 434 444 Extracellular. {ECO:0000255}.
TRANSMEM 445 465 Helical. {ECO:0000255}.
TOPO_DOM 466 494 Cytoplasmic. {ECO:0000255}.
TRANSMEM 495 513 Helical. {ECO:0000255}.
TOPO_DOM 514 521 Extracellular. {ECO:0000255}.
TRANSMEM 522 543 Helical. {ECO:0000255}.
TOPO_DOM 544 555 Cytoplasmic. {ECO:0000255}.
TRANSMEM 556 574 Helical. {ECO:0000255}.
TOPO_DOM 575 637 Extracellular. {ECO:0000255}.
TRANSMEM 638 657 Helical. {ECO:0000255}.
TOPO_DOM 658 666 Cytoplasmic. {ECO:0000255}.
DOMAIN 77 317 ABC transporter. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 403 661 ABC transmembrane type-2.
NP_BIND 118 125 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
LIPID 30 30 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 154 154 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 315 315 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 394 394 S-palmitoyl cysteine. {ECO:0000250}.
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


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