ABCG1_HUMAN
ID ABCG1_HUMAN Reviewed; 678 AA.
AC P45844; Q86SU8; Q96L76; Q9BXK6; Q9BXK7; Q9BXK8; Q9BXK9; Q9BXL0; Q9BXL1;
AC Q9BXL2; Q9BXL3; Q9BXL4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=ATP-binding cassette sub-family G member 1 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000269|PubMed:16702602};
DE AltName: Full=ATP-binding cassette transporter 8;
DE AltName: Full=White protein homolog;
GN Name=ABCG1 {ECO:0000312|HGNC:HGNC:73}; Synonyms=ABC8, WHT1;
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 [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., Perrin G.,
RA Antonarakis S.E.;
RT "Cloning of the cDNA for a human homologue of the Drosophila white gene and
RT 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., Wang J.,
RA Kawasaki K., Asakawa S., Minoshima S., Shimizu N., Antonarakis S.E.,
RA Bonne-Tamir B.;
RT "Refined localization of autosomal recessive nonsyndromic deafness DFNB10
RT locus using 34 novel microsatellite markers, genomic structure, and
RT 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 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 of ATP
RT binding cassette transporter A1 (ABCA1) and ABCG1 gene expression and a
RT 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 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 an
RT internal promoter that produces a novel transcript encoding an alternative
RT 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., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., 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 project:
RT 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., 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 [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-loaded
RT 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., Porsch-Oezcueruemez M.,
RA Liebisch G., Kapinsky M., Diederich W., Drobnik W., Dean M., Allikmets R.,
RA 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 ABCG1 via
RT 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) in
RT Tangier disease.";
RL Biochem. Biophys. Res. Commun. 283:821-830(2001).
RN [14]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, SUBUNIT, MUTAGENESIS
RP OF LYS-124, AND ACTIVITY REGULATION.
RX PubMed=16702602; DOI=10.1194/jlr.m500546-jlr200;
RA Kobayashi A., Takanezawa Y., Hirata T., Shimizu Y., Misasa K., Kioka N.,
RA Arai H., Ueda K., Matsuo M.;
RT "Efflux of sphingomyelin, cholesterol, and phosphatidylcholine by ABCG1.";
RL J. Lipid Res. 47:1791-1802(2006).
RN [15]
RP CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF LYS-124, AND INDUCTION.
RX PubMed=17408620; DOI=10.1016/j.febslet.2007.03.038;
RA Engel T., Kannenberg F., Fobker M., Nofer J.R., Bode G., Lueken A.,
RA Assmann G., Seedorf U.;
RT "Expression of ATP binding cassette-transporter ABCG1 prevents cell death
RT by transporting cytotoxic 7beta-hydroxycholesterol.";
RL FEBS Lett. 581:1673-1680(2007).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=22042635; DOI=10.1074/mcp.m111.013458;
RA Uhlen M., Oksvold P., Algenas C., Hamsten C., Fagerberg L., Klevebring D.,
RA Lundberg E., Odeberg J., Ponten F., Kondo T., Sivertsson A.;
RT "Antibody-based protein profiling of the human chromosome 21.";
RL Mol. Cell. Proteomics 11:M111.013458-M111.013458(2012).
RN [17]
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 transporter G1:
RT Effect on protein trafficking and function.";
RL Biochim. Biophys. Acta 1831:1067-1078(2013).
RN [18]
RP CATALYTIC ACTIVITY, INTERACTION WITH CAV1, FUNCTION, MUTAGENESIS OF
RP TYR-491; TYR-493; TYR-498 AND TYR-499, AND SUBCELLULAR LOCATION.
RX PubMed=24576892; DOI=10.1016/j.bbalip.2014.02.002;
RA Gu H.M., Wang F.Q., Zhang D.W.;
RT "Caveolin-1 interacts with ATP binding cassette transporter G1 (ABCG1) and
RT regulates ABCG1-mediated cholesterol efflux.";
RL Biochim. Biophys. Acta 1841:847-858(2014).
RN [19]
RP SUBUNIT, INTERACTION WITH ABCG4, AND MUTAGENESIS OF LYS-124.
RX PubMed=27228027; DOI=10.1371/journal.pone.0156516;
RA Hegyi Z., Homolya L.;
RT "Functional Cooperativity between ABCG4 and ABCG1 Isoforms.";
RL PLoS ONE 11:e0156516-e0156516(2016).
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:17408620, PubMed:24576892). The lipid efflux is ALB-dependent
CC (PubMed:16702602). Is an active component of the macrophage lipid
CC export complex. Could also be involved in intracellular lipid transport
CC processes. The role in cellular lipid homeostasis may not be limited to
CC macrophages. Prevents cell death by transporting cytotoxic 7beta-
CC hydroxycholesterol (PubMed:17408620). {ECO:0000269|PubMed:16702602,
CC ECO:0000269|PubMed:17408620, ECO:0000269|PubMed:24576892}.
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:0000269|PubMed:17408620};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39796;
CC Evidence={ECO:0000269|PubMed:17408620};
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:16702602, ECO:0000269|PubMed:24576892};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000269|PubMed:17408620};
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:0000269|PubMed:16702602};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46469;
CC Evidence={ECO:0000269|PubMed:16702602};
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:0000269|PubMed:16702602};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38904;
CC Evidence={ECO:0000269|PubMed:16702602};
CC -!- ACTIVITY REGULATION: The cholesterol efflux is enhanced by APOA1.
CC {ECO:0000269|PubMed:16702602}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:16702602). Homooligomer
CC (PubMed:16702602). May form heterodimers with several heterologous
CC partners of the ABCG subfamily. Forms heterodimers with ABCG4
CC (PubMed:27228027). Interacts with CAV1; this interaction regulates
CC ABCG1-mediated cholesterol efflux (PubMed:24576892).
CC {ECO:0000269|PubMed:16702602, ECO:0000269|PubMed:24576892,
CC ECO:0000269|PubMed:27228027}.
CC -!- INTERACTION:
CC P45844-4; Q9H172: ABCG4; NbExp=2; IntAct=EBI-8584087, EBI-8584118;
CC P45844-4; Q13520: AQP6; NbExp=3; IntAct=EBI-8584087, EBI-13059134;
CC P45844-6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25873349, EBI-21591415;
CC P45844-6; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-25873349, EBI-5280197;
CC P45844-6; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-25873349, EBI-2623095;
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}. Cell membrane
CC {ECO:0000269|PubMed:16702602, ECO:0000269|PubMed:24576892}.
CC Note=Predominantly localized in the intracellular compartments mainly
CC associated with the endoplasmic 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 with
CC 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 ECO:0000269|PubMed:16702602, ECO:0000269|PubMed:17408620}.
CC -!- PTM: Palmitoylation at Cys-315 seems important for trafficking from the
CC endoplasmic reticulum. {ECO:0000269|PubMed:23388354}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC51098.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK28841.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA95530.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB13728.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA62631.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC00730.1; Type=Erroneous initiation; Note=Truncated 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; 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 PDB; 7OZ1; EM; 4.00 A; A/B=1-678.
DR PDB; 7R8C; EM; 3.70 A; A/B=1-678.
DR PDB; 7R8D; EM; 3.20 A; A/B=1-678.
DR PDB; 7R8E; EM; 3.68 A; A/B=1-678.
DR PDBsum; 7OZ1; -.
DR PDBsum; 7R8C; -.
DR PDBsum; 7R8D; -.
DR PDBsum; 7R8E; -.
DR AlphaFoldDB; P45844; -.
DR SMR; P45844; -.
DR BioGRID; 114980; 67.
DR IntAct; P45844; 9.
DR MINT; P45844; -.
DR STRING; 9606.ENSP00000354995; -.
DR DrugBank; DB00171; ATP.
DR DrugBank; DB00163; Vitamin E.
DR SwissLipids; SLP:000000420; -.
DR TCDB; 3.A.1.204.12; the atp-binding cassette (abc) superfamily.
DR GlyGen; P45844; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P45844; -.
DR PhosphoSitePlus; P45844; -.
DR SwissPalm; P45844; -.
DR BioMuta; ABCG1; -.
DR DMDM; 17433715; -.
DR EPD; P45844; -.
DR jPOST; P45844; -.
DR MassIVE; P45844; -.
DR MaxQB; P45844; -.
DR PaxDb; P45844; -.
DR PeptideAtlas; P45844; -.
DR PRIDE; P45844; -.
DR ProteomicsDB; 55678; -. [P45844-1]
DR ProteomicsDB; 55679; -. [P45844-2]
DR ProteomicsDB; 55680; -. [P45844-3]
DR ProteomicsDB; 55681; -. [P45844-4]
DR ProteomicsDB; 55682; -. [P45844-5]
DR ProteomicsDB; 55683; -. [P45844-6]
DR ProteomicsDB; 55684; -. [P45844-7]
DR ProteomicsDB; 55685; -. [P45844-8]
DR TopDownProteomics; P45844-8; -. [P45844-8]
DR Antibodypedia; 23734; 410 antibodies from 35 providers.
DR DNASU; 9619; -.
DR Ensembl; ENST00000343687.7; ENSP00000339744.3; ENSG00000160179.19. [P45844-2]
DR Ensembl; ENST00000347800.6; ENSP00000291524.4; ENSG00000160179.19. [P45844-5]
DR Ensembl; ENST00000361802.6; ENSP00000354995.2; ENSG00000160179.19. [P45844-1]
DR Ensembl; ENST00000398449.8; ENSP00000381467.3; ENSG00000160179.19. [P45844-4]
DR Ensembl; ENST00000398457.6; ENSP00000381475.2; ENSG00000160179.19. [P45844-3]
DR GeneID; 9619; -.
DR KEGG; hsa:9619; -.
DR MANE-Select; ENST00000398449.8; ENSP00000381467.3; NM_016818.3; NP_058198.2. [P45844-4]
DR UCSC; uc002zan.3; human. [P45844-1]
DR CTD; 9619; -.
DR DisGeNET; 9619; -.
DR GeneCards; ABCG1; -.
DR HGNC; HGNC:73; ABCG1.
DR HPA; ENSG00000160179; Low tissue specificity.
DR MIM; 603076; gene.
DR neXtProt; NX_P45844; -.
DR OpenTargets; ENSG00000160179; -.
DR PharmGKB; PA24408; -.
DR VEuPathDB; HostDB:ENSG00000160179; -.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000160131; -.
DR HOGENOM; CLU_000604_57_6_1; -.
DR InParanoid; P45844; -.
DR OMA; IRIAMYM; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; P45844; -.
DR TreeFam; TF105210; -.
DR PathwayCommons; P45844; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-HSA-8964058; HDL remodeling.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; P45844; -.
DR SIGNOR; P45844; -.
DR BioGRID-ORCS; 9619; 108 hits in 1078 CRISPR screens.
DR ChiTaRS; ABCG1; human.
DR GeneWiki; ABCG1; -.
DR GenomeRNAi; 9619; -.
DR Pharos; P45844; Tbio.
DR PRO; PR:P45844; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P45844; protein.
DR Bgee; ENSG00000160179; Expressed in right adrenal gland and 190 other tissues.
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; HDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:BHF-UCL.
DR GO; GO:0034041; F:ABC-type sterol transporter activity; IDA: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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015485; F:cholesterol binding; IC:BHF-UCL.
DR GO; GO:0120020; F:cholesterol transfer activity; IDA:BHF-UCL.
DR GO; GO:0140328; F:floppase activity; IDA:ARUK-UCL.
DR GO; GO:0090554; F:phosphatidylcholine floppase activity; IDA:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IC:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0071403; P:cellular response to high density lipoprotein particle stimulus; IEA:Ensembl.
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: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: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:1902004; P:positive regulation of amyloid-beta formation; IDA:ARUK-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:0050714; P:positive regulation of protein secretion; IDA:ARUK-UCL.
DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISS:BHF-UCL.
DR GO; GO:0033993; P:response to lipid; IDA:BHF-UCL.
DR GO; GO:0010033; P:response to organic substance; IEP:UniProtKB.
DR GO; GO:0043691; P:reverse cholesterol transport; ISS: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 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Endoplasmic reticulum; Golgi apparatus; Lipid transport; Lipoprotein;
KW Membrane; Nucleotide-binding; Palmitate; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..678
FT /note="ATP-binding cassette sub-family G member 1"
FT /id="PRO_0000093384"
FT TOPO_DOM 1..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..456
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..533
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..555
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..669
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..678
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 77..317
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 415..673
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:0000269|PubMed:23388354"
FT LIPID 154
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23388354"
FT LIPID 315
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23388354"
FT LIPID 394
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23388354"
FT LIPID 406
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23388354"
FT VAR_SEQ 1..95
FT /note="MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNMEATETDLLNGH
FT LKKVDNNLTEAQRFSSLPRRAAVNIEFRDLSYSVPEGPWWRKK -> MVRRGWSVCTAI
FT LLARLWCLVPTHTFLSEYPEAAEYPHPGWVYWLQMAVAPGHLRAWVMRNNVTTNIPSAF
FT SGTLTHEEKAVLTVFTGTATAVHVQVAALASAKLESSVFVTDCVSCKIENVCDSALQGK
FT RVPMSGLQGSSIVIMPPSNRPLASAASCTWSVQVQGGPHHLGVVAISGKVLSAAHGAGR
FT AYGWGFPGDPMEE (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:11500512"
FT /id="VSP_010718"
FT VAR_SEQ 1..22
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11162488"
FT /id="VSP_000050"
FT VAR_SEQ 1..14
FT /note="MACLMAAFSVGTAM -> MRISLPRAPERDGGVSASSLLDTVT (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11162488"
FT /id="VSP_000047"
FT VAR_SEQ 1..14
FT /note="MACLMAAFSVGTAM -> MLGTQGWTKQRKPCPQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11162488"
FT /id="VSP_000048"
FT VAR_SEQ 1..14
FT /note="MACLMAAFSVGTAM -> MIMRLPQPHGT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:11162488"
FT /id="VSP_000049"
FT VAR_SEQ 1..4
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:11162488"
FT /id="VSP_000046"
FT VAR_SEQ 375..386
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5, isoform 6 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:11162488,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8659545"
FT /id="VSP_000051"
FT VARIANT 668
FT /note="F -> L"
FT /evidence="ECO:0000269|PubMed:11500512"
FT /id="VAR_012279"
FT MUTAGEN 30
FT /note="C->A: No significant effect."
FT /evidence="ECO:0000269|PubMed:23388354"
FT MUTAGEN 124
FT /note="K->M: Affects ATP binding. Does not affect efflux of
FT 7beta-hydroxycholesterol. Does not affect localization at
FT plasma membrane. Does not affect homodimerization.
FT Decreases cholesterol and phospholipids efflux. Does not
FT affect heretodimerization with ABCG4."
FT /evidence="ECO:0000269|PubMed:16702602,
FT ECO:0000269|PubMed:17408620, ECO:0000269|PubMed:27228027"
FT MUTAGEN 154
FT /note="C->A: No significant effect."
FT /evidence="ECO:0000269|PubMed:23388354"
FT MUTAGEN 315
FT /note="C->A,S: Significantly decreases ABCG1-mediated
FT cholesterol efflux."
FT /evidence="ECO:0000269|PubMed:23388354"
FT MUTAGEN 394
FT /note="C->A: No significant effect."
FT /evidence="ECO:0000269|PubMed:23388354"
FT MUTAGEN 406
FT /note="C->A: No significant effect."
FT /evidence="ECO:0000269|PubMed:23388354"
FT MUTAGEN 491
FT /note="Y->A: Significantly reduces interaction with CAV1;
FT when associated with A-493. Significantly reduces ABCG1-
FT mediated cholesterol efflux; when associated with A-493."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 493
FT /note="Y->A: Significantly reduces interaction with CAV1;
FT when associated with A-491. Significantly reduces ABCG1-
FT mediated cholesterol efflux; when associated with A-491."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 498
FT /note="Y->A: Significantly reduces interaction with CAV1;
FT when associated with A-499. Significantly reduces ABCG1-
FT mediated cholesterol efflux; when associated with A-499.
FT Affects subcellular location at plasma membrane; when
FT associated with A-499. Affects ABCG1 traffincking to the
FT plasma membrane; when associated with A-499."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 498
FT /note="Y->F: Does not affect ABCG1-mediated cholesterol
FT efflux; when associated with I-499."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 498
FT /note="Y->I: Dramatically reduces the ability of ABCG1 to
FT mediate cholesterol efflux; when associated with I-499."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 498
FT /note="Y->W: Does not affect ABCG1-mediated cholesterol
FT efflux; when associated with I-499."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 499
FT /note="Y->A: Significantly reduces interaction with CAV1;
FT when associated with A-498. Significantly reduces ABCG1-
FT mediated cholesterol efflux; when associated with A-498.
FT Affects subcellular location at plasma membrane; when
FT associated with A-498. Affects ABCG1 traffincking to the
FT plasma membrane; when associated with A-498."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 499
FT /note="Y->F: Does not affect ABCG1-mediated cholesterol
FT efflux; when associated with I-498."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 499
FT /note="Y->I: Dramatically reduces the ability of ABCG1 to
FT mediate cholesterol efflux; when associated with I-498."
FT /evidence="ECO:0000269|PubMed:24576892"
FT MUTAGEN 499
FT /note="Y->W: Does not affect ABCG1-mediated cholesterol
FT efflux; when associated with I-498."
FT /evidence="ECO:0000269|PubMed:24576892"
FT CONFLICT 38
FT /note="S -> T (in Ref. 4; AAK28839/AAK28841)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="A -> T (in Ref. 1; CAA62631, 4; AAK28838/AAK28839/
FT AAK28840/AAK28841/AAK28842 and 5; AAL06598)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="R -> A (in Ref. 8; AAC51098)"
FT /evidence="ECO:0000305"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:7R8D"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 249..264
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 304..309
FT /evidence="ECO:0007829|PDB:7R8D"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 321..329
FT /evidence="ECO:0007829|PDB:7R8D"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 401..416
FT /evidence="ECO:0007829|PDB:7R8D"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 425..440
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 451..489
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 495..521
FT /evidence="ECO:0007829|PDB:7R8D"
FT TURN 522..526
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 533..557
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 562..578
FT /evidence="ECO:0007829|PDB:7R8D"
FT STRAND 579..584
FT /evidence="ECO:0007829|PDB:7R8D"
FT TURN 586..588
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 591..598
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 601..613
FT /evidence="ECO:0007829|PDB:7R8D"
FT TURN 633..635
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 636..640
FT /evidence="ECO:0007829|PDB:7R8D"
FT HELIX 648..677
FT /evidence="ECO:0007829|PDB:7R8D"
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
