ABCG4_HUMAN
ID ABCG4_HUMAN Reviewed; 646 AA.
AC Q9H172; A8K1B5; Q8WWH0; Q8WWH1; Q8WWH2;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=ATP-binding cassette sub-family G member 4;
DE EC=7.6.2.- {ECO:0000269|PubMed:15240127, ECO:0000269|PubMed:33141061};
GN Name=ABCG4 {ECO:0000312|HGNC:HGNC:13884}; Synonyms=WHITE2;
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] (ISOFORM 1), AND MISCELLANEOUS.
RX PubMed=11606068; DOI=10.1006/bbrc.2001.5756;
RA Engel T., Lorkowski S., Lueken A., Rust S., Schlueter B., Berger G.,
RA Cullen P., Assmann G.;
RT "The human ABCG4 gene is regulated by oxysterols and retinoids in monocyte-
RT derived macrophages.";
RL Biochem. Biophys. Res. Commun. 288:483-488(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-118 (ISOFORMS 2; 3 AND 4), ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=11856881; DOI=10.1159/000048816;
RA Annilo T., Tammur J., Hutchinson A., Rzhetsky A., Dean M., Allikmets R.;
RT "Human and mouse orthologs of a new ATP-binding cassette gene, ABCG4.";
RL Cytogenet. Cell Genet. 94:196-201(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-646 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Spinal ganglion;
RX PubMed=12183068; DOI=10.1016/s0167-4889(02)00269-0;
RA Oldfield S., Lowry C., Ruddick J., Lightman S.;
RT "ABCG4: a novel human white family ABC-transporter expressed in the brain
RT and eye.";
RL Biochim. Biophys. Acta 1591:175-179(2002).
RN [7]
RP SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-108.
RX PubMed=15240127; DOI=10.1016/j.bbrc.2004.06.037;
RA Cserepes J., Szentpetery Z., Seres L., Ozvegy-Laczka C., Langmann T.,
RA Schmitz G., Glavinas H., Klein I., Homolya L., Varadi A., Sarkadi B.,
RA Elkind N.B.;
RT "Functional expression and characterization of the human ABCG1 and ABCG4
RT proteins: indications for heterodimerization.";
RL Biochem. Biophys. Res. Commun. 320:860-867(2004).
RN [8]
RP SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-108, FUNCTION, AND
RP INTERACTION WITH ABCG1.
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).
RN [9]
RP INDUCTION, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=33141061; DOI=10.1016/j.bbagen.2020.129769;
RA Yang A., Alrosan A.Z., Sharpe L.J., Brown A.J., Callaghan R.,
RA Gelissen I.C.;
RT "Regulation of ABCG4 transporter expression by sterols and LXR ligands.";
RL Biochim. Biophys. Acta 1865:129769-129769(2021).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that may be involved in the cellular efflux of sterols, in
CC particular cholesterol and desmosterol (a cholesterol precursor), to
CC high-density lipoprotein (HDL) (PubMed:15240127, PubMed:33141061). May
CC play an important role in the removal of amyloid-beta peptides from
CC brain, in a process that can be antagonized by desmosterol. However it
CC is unclear whether ABCG4 can directly transport amyloid-beta peptides
CC or whether peptide export may be facilitated due to changes in the
CC membrane lipid environment (By similarity). Induces apoptosis in
CC various cells (PubMed:27228027). {ECO:0000250|UniProtKB:Q91WA9,
CC ECO:0000269|PubMed:15240127, ECO:0000269|PubMed:27228027,
CC ECO:0000269|PubMed:33141061}.
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:33141061};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000305|PubMed:33141061};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + desmosterol(in) + H2O = ADP + desmosterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:67932, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17737, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q91WA9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67933;
CC Evidence={ECO:0000250|UniProtKB:Q91WA9};
CC -!- SUBUNIT: Half-transporter that forms a functional transporter via
CC homo- or heterodimerization. Homodimer (PubMed:27228027). Heterodimers
CC with ABCG1 (Probable) (PubMed:27228027). {ECO:0000269|PubMed:27228027,
CC ECO:0000305|PubMed:15240127}.
CC -!- INTERACTION:
CC Q9H172; P45844-4: ABCG1; NbExp=2; IntAct=EBI-8584118, EBI-8584087;
CC Q9H172; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-8584118, EBI-13345167;
CC Q9H172; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-8584118, EBI-742388;
CC Q9H172; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-8584118, EBI-744081;
CC Q9H172; O95807: TMEM50A; NbExp=3; IntAct=EBI-8584118, EBI-12903814;
CC Q9H172; O76024: WFS1; NbExp=3; IntAct=EBI-8584118, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27228027};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q91WA9}; Multi-pass membrane protein
CC {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q91WA9}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=B;
CC IsoId=Q9H172-1; Sequence=Displayed;
CC Name=2; Synonyms=T3, T4;
CC IsoId=Q9H172-2; Sequence=VSP_054267;
CC Name=3; Synonyms=M, T1;
CC IsoId=Q9H172-3; Sequence=VSP_054268;
CC Name=4; Synonyms=T2;
CC IsoId=Q9H172-4; Sequence=VSP_054266;
CC -!- TISSUE SPECIFICITY: Expressed specifically in the brain and the eye.
CC {ECO:0000269|PubMed:11856881, ECO:0000269|PubMed:12183068}.
CC -!- INDUCTION: Protein expression is stabilized by cellular cholesterol
CC status and cholesterol synthesis intermediates desmosterol, lathosterol
CC and lanosterol. {ECO:0000269|PubMed:33141061}.
CC -!- MISCELLANEOUS: Whether ABCG4 is an LXR target gene, is still under
CC debate. Studies performed in monocytes, and in one astrocyte cell line
CC indicated that ABCG4 expression could be up-regulated by oxysterols and
CC other LXR ligands (PubMed:11606068, PubMed:33141061). However,
CC subsequent observations in a number of different cell types (primary
CC mouse cells, oligodendrocytes and neuron-like cell lines) have not
CC confirmed this observation (By similarity) (PubMed:33141061).
CC {ECO:0000250|UniProtKB:Q91WA9, ECO:0000269|PubMed:11606068,
CC ECO:0000269|PubMed:33141061}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {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; AJ308237; CAC87131.1; -; mRNA.
DR EMBL; AK289830; BAF82519.1; -; mRNA.
DR EMBL; AK290035; BAF82724.1; -; mRNA.
DR EMBL; CH471065; EAW67464.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW67465.1; -; Genomic_DNA.
DR EMBL; CH471065; EAW67466.1; -; Genomic_DNA.
DR EMBL; BC041091; AAH41091.1; -; mRNA.
DR EMBL; AY055472; AAL16400.1; -; Genomic_DNA.
DR EMBL; AY055472; AAL16401.1; -; Genomic_DNA.
DR EMBL; AY055472; AAL16402.1; -; Genomic_DNA.
DR EMBL; AJ300465; CAC17140.1; -; mRNA.
DR CCDS; CCDS8415.1; -. [Q9H172-1]
DR PIR; JC7777; JC7777.
DR RefSeq; NP_001135977.1; NM_001142505.1. [Q9H172-1]
DR RefSeq; NP_001335120.1; NM_001348191.1. [Q9H172-1]
DR RefSeq; NP_001335121.1; NM_001348192.1. [Q9H172-2]
DR RefSeq; NP_071452.2; NM_022169.4. [Q9H172-1]
DR RefSeq; XP_011541254.1; XM_011542952.2. [Q9H172-3]
DR AlphaFoldDB; Q9H172; -.
DR SMR; Q9H172; -.
DR BioGRID; 122083; 7.
DR IntAct; Q9H172; 7.
DR MINT; Q9H172; -.
DR STRING; 9606.ENSP00000481728; -.
DR TCDB; 3.A.1.204.20; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q9H172; 1 site.
DR iPTMnet; Q9H172; -.
DR PhosphoSitePlus; Q9H172; -.
DR BioMuta; ABCG4; -.
DR DMDM; 17432915; -.
DR MassIVE; Q9H172; -.
DR PaxDb; Q9H172; -.
DR PeptideAtlas; Q9H172; -.
DR PRIDE; Q9H172; -.
DR ProteomicsDB; 80375; -. [Q9H172-1]
DR Antibodypedia; 32624; 202 antibodies from 31 providers.
DR DNASU; 64137; -.
DR Ensembl; ENST00000615496.4; ENSP00000479253.1; ENSG00000172350.10. [Q9H172-1]
DR Ensembl; ENST00000619701.5; ENSP00000481728.1; ENSG00000172350.10. [Q9H172-1]
DR Ensembl; ENST00000622721.1; ENSP00000484289.1; ENSG00000172350.10. [Q9H172-1]
DR GeneID; 64137; -.
DR KEGG; hsa:64137; -.
DR MANE-Select; ENST00000619701.5; ENSP00000481728.1; NM_022169.5; NP_071452.2.
DR UCSC; uc031yhk.2; human. [Q9H172-1]
DR CTD; 64137; -.
DR DisGeNET; 64137; -.
DR GeneCards; ABCG4; -.
DR HGNC; HGNC:13884; ABCG4.
DR HPA; ENSG00000172350; Tissue enriched (retina).
DR MIM; 607784; gene.
DR neXtProt; NX_Q9H172; -.
DR OpenTargets; ENSG00000172350; -.
DR PharmGKB; PA24410; -.
DR VEuPathDB; HostDB:ENSG00000172350; -.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000157853; -.
DR HOGENOM; CLU_000604_57_6_1; -.
DR InParanoid; Q9H172; -.
DR OMA; VTDVDHI; -.
DR OrthoDB; 324553at2759; -.
DR PhylomeDB; Q9H172; -.
DR TreeFam; TF105210; -.
DR PathwayCommons; Q9H172; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR SignaLink; Q9H172; -.
DR BioGRID-ORCS; 64137; 9 hits in 1070 CRISPR screens.
DR GeneWiki; ABCG4; -.
DR GenomeRNAi; 64137; -.
DR Pharos; Q9H172; Tbio.
DR PRO; PR:Q9H172; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H172; protein.
DR Bgee; ENSG00000172350; Expressed in right hemisphere of cerebellum and 138 other tissues.
DR ExpressionAtlas; Q9H172; baseline and differential.
DR Genevisible; Q9H172; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0034041; F:ABC-type sterol transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0071403; P:cellular response to high density lipoprotein particle stimulus; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:Ensembl.
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; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
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 PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasmic vesicle;
KW Endosome; Glycoprotein; Lipid transport; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..646
FT /note="ATP-binding cassette sub-family G member 4"
FT /id="PRO_0000093392"
FT TOPO_DOM 1..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..503
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..532
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 554..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 618..638
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 61..301
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 386..641
FT /note="ABC transmembrane type-2"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11856881"
FT /id="VSP_054266"
FT VAR_SEQ 1..79
FT /note="MAEKALEAVGCGLGPGAVAMAVTLEDGAEPPVLTTHLKKVENHITEAQRFSH
FT LPKRSAVDIEFVELSYSVREGPCWRKR -> MRDLELREVKQLARGHTA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:11856881"
FT /id="VSP_054267"
FT VAR_SEQ 1..79
FT /note="MAEKALEAVGCGLGPGAVAMAVTLEDGAEPPVLTTHLKKVENHITEAQRFSH
FT LPKRSAVDIEFVELSYSVREGPCWRKR -> MCGFSHAFQKRIVAS (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:11856881"
FT /id="VSP_054268"
FT VARIANT 352
FT /note="P -> L (in dbSNP:rs35060365)"
FT /id="VAR_048141"
FT MUTAGEN 108
FT /note="K->M: Abrogates ATPase activity. Induces a dominant-
FT negative effect on ABCG1 ATP-activity. Does not affect
FT subcellular localization."
FT /evidence="ECO:0000269|PubMed:15240127,
FT ECO:0000269|PubMed:27228027"
SQ SEQUENCE 646 AA; 71896 MW; 9CCEC6E150772611 CRC64;
MAEKALEAVG CGLGPGAVAM AVTLEDGAEP PVLTTHLKKV ENHITEAQRF SHLPKRSAVD
IEFVELSYSV REGPCWRKRG YKTLLKCLSG KFCRRELIGI MGPSGAGKST FMNILAGYRE
SGMKGQILVN GRPRELRTFR KMSCYIMQDD MLLPHLTVLE AMMVSANLKL SEKQEVKKEL
VTEILTALGL MSCSHTRTAL LSGGQRKRLA IALELVNNPP VMFFDEPTSG LDSASCFQVV
SLMKSLAQGG RTIICTIHQP SAKLFEMFDK LYILSQGQCI FKGVVTNLIP YLKGLGLHCP
TYHNPADFII EVASGEYGDL NPMLFRAVQN GLCAMAEKKS SPEKNEVPAP CPPCPPEVDP
IESHTFATST LTQFCILFKR TFLSILRDTV LTHLRFMSHV VIGVLIGLLY LHIGDDASKV
FNNTGCLFFS MLFLMFAALM PTVLTFPLEM AVFMREHLNY WYSLKAYYLA KTMADVPFQV
VCPVVYCSIV YWMTGQPAET SRFLLFSALA TATALVAQSL GLLIGAASNS LQVATFVGPV
TAIPVLLFSG FFVSFKTIPT YLQWSSYLSY VRYGFEGVIL TIYGMERGDL TCLEERCPFR
EPQSILRALD VEDAKLYMDF LVLGIFFLAL RLLAYLVLRY RVKSER
