ABCG5_HUMAN
ID ABCG5_HUMAN Reviewed; 651 AA.
AC Q9H222; Q2T9G2; Q96QZ2; Q96QZ3;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=ATP-binding cassette sub-family G member 5 {ECO:0000305};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:Q99PE8};
DE AltName: Full=Sterolin-1 {ECO:0000303|PubMed:11452359};
GN Name=ABCG5 {ECO:0000312|HGNC:HGNC:13886};
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), VARIANT GLU-604, FUNCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11099417; DOI=10.1126/science.290.5497.1771;
RA Berge K.E., Tian H., Graf G.A., Yu L., Grishin N.V., Schultz J.,
RA Kwiterovich P., Shan B., Barnes R., Hobbs H.H.;
RT "Accumulation of dietary cholesterol in sitosterolemia caused by mutations
RT in adjacent ABC transporters.";
RL Science 290:1771-1775(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS STSL2 HIS-389; HIS-419 AND
RP PRO-419, VARIANT GLU-604, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11138003; DOI=10.1038/83799;
RA Lee M.-H., Lu K., Hazard S., Yu H., Shulenin S., Hidaka H., Kojima H.,
RA Allikmets R., Sakuma N., Pegoraro R., Srivastava A.K., Salen G., Dean M.,
RA Patel S.B.;
RT "Identification of a gene, ABCG5, important in the regulation of dietary
RT cholesterol absorption.";
RL Nat. Genet. 27:79-83(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-88 (ISOFORM 1), VARIANTS STSL2 GLN-146;
RP HIS-389; PRO-419; HIS-419 AND SER-550, AND VARIANT GLU-604.
RX PubMed=11452359; DOI=10.1086/321294;
RA Lu K., Lee M.-H., Hazard S., Brooks-Wilson A., Hidaka H., Kojima H.,
RA Ose L., Stalenhoef A.F.H., Mietinnen T., Bjorkhem I., Bruckert E.,
RA Pandya A., Brewer H.B. Jr., Salen G., Dean M., Srivastava A.K., Patel S.B.;
RT "Two genes that map to the STSL locus cause sitosterolemia: genomic
RT structure and spectrum of mutations involving sterolin-1 and sterolin-2,
RT encoded by ABCG5 and ABCG8, respectively.";
RL Am. J. Hum. Genet. 69:278-290(2001).
RN [7]
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=14504269; DOI=10.1074/jbc.m310223200;
RA Graf G.A., Yu L., Li W.P., Gerard R., Tuma P.L., Cohen J.C., Hobbs H.H.;
RT "ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and
RT biliary cholesterol excretion.";
RL J. Biol. Chem. 278:48275-48282(2003).
RN [9]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=16893193; DOI=10.1021/bi0608055;
RA Wang Z., Stalcup L.D., Harvey B.J., Weber J., Chloupkova M., Dumont M.E.,
RA Dean M., Urbatsch I.L.;
RT "Purification and ATP hydrolysis of the putative cholesterol transporters
RT ABCG5 and ABCG8.";
RL Biochemistry 45:9929-9939(2006).
RN [10]
RP FUNCTION, SUBUNIT, GLYCOSYLATION, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP 92-LYS-THR-93.
RX PubMed=20210363; DOI=10.1021/bi902064g;
RA Johnson B.J., Lee J.Y., Pickert A., Urbatsch I.L.;
RT "Bile acids stimulate ATP hydrolysis in the purified cholesterol
RT transporter ABCG5/G8.";
RL Biochemistry 49:3403-3411(2010).
RN [11] {ECO:0007744|PDB:5DO7}
RP X-RAY CRYSTALLOGRAPHY (3.93 ANGSTROMS) IN COMPLEX WITH ABCG8, FUNCTION,
RP ACTIVITY REGULATION, MUTAGENESIS OF TYR-432 AND ALA-540, SUBUNIT, AND
RP TOPOLOGY.
RX PubMed=27144356; DOI=10.1038/nature17666;
RA Lee J.Y., Kinch L.N., Borek D.M., Wang J., Wang J., Urbatsch I.L.,
RA Xie X.S., Grishin N.V., Cohen J.C., Otwinowski Z., Hobbs H.H.,
RA Rosenbaum D.M.;
RT "Crystal structure of the human sterol transporter ABCG5/ABCG8.";
RL Nature 533:561-564(2016).
RN [12]
RP VARIANT STSL2 LYS-437, AND VARIANTS VAL-523; TYR-600; GLU-604 AND VAL-622.
RX PubMed=11668628; DOI=10.1002/humu.1206;
RA Hubacek J.A., Berge K.E., Cohen J.C., Hobbs H.H.;
RT "Mutations in ATP-cassette binding proteins G5 (ABCG5) and G8 (ABCG8)
RT causing sitosterolemia.";
RL Hum. Mutat. 18:359-360(2001).
RN [13]
RP CHARACTERIZATION OF VARIANTS STSL2 GLN-146; HIS-389; PRO-419; HIS-419 AND
RP LYS-437, AND FUNCTION.
RX PubMed=15054092; DOI=10.1074/jbc.m402634200;
RA Graf G.A., Cohen J.C., Hobbs H.H.;
RT "Missense mutations in ABCG5 and ABCG8 disrupt heterodimerization and
RT trafficking.";
RL J. Biol. Chem. 279:24881-24888(2004).
CC -!- FUNCTION: ABCG5 and ABCG8 form an obligate heterodimer that mediates
CC Mg(2+)- and ATP-dependent sterol transport across the cell membrane
CC (PubMed:27144356). Plays an essential role in the selective transport
CC of dietary plant sterols and cholesterol in and out of the enterocytes
CC and in the selective sterol excretion by the liver into bile
CC (PubMed:11099417, PubMed:11138003, PubMed:27144356, PubMed:15054092).
CC Required for normal sterol homeostasis (PubMed:11099417,
CC PubMed:11138003, PubMed:15054092). The heterodimer with ABCG8 has
CC ATPase activity (PubMed:16893193, PubMed:20210363, PubMed:27144356).
CC {ECO:0000269|PubMed:11138003, ECO:0000269|PubMed:15054092,
CC ECO:0000269|PubMed:16893193, ECO:0000269|PubMed:20210363,
CC ECO:0000269|PubMed:27144356, ECO:0000303|PubMed:11590207,
CC ECO:0000305|PubMed:11099417}.
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:Q99PE8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + sitosterol(in) = ADP + H(+) + phosphate +
CC sitosterol(out); Xref=Rhea:RHEA:39103, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27693, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39104;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q99PE8};
CC -!- ACTIVITY REGULATION: The ATPase activity of the heterodimer is
CC stimulated by cholate. Taurocholate, glycocholate,
CC taurochenodeoxycholate, glycochenodeoxycholate and taurodeoxycholate
CC also stimulate ATPase activity, but to a lower degree.
CC Glycodeoxycholate has no significant effect on ATPase activity. ATPase
CC activity is inhibited by vanadate and by berillium fluoride.
CC {ECO:0000269|PubMed:20210363, ECO:0000269|PubMed:27144356}.
CC -!- SUBUNIT: Heterodimer with ABCG8. {ECO:0000269|PubMed:16893193,
CC ECO:0000269|PubMed:20210363, ECO:0000269|PubMed:27144356}.
CC -!- INTERACTION:
CC Q9H222; Q9H221: ABCG8; NbExp=2; IntAct=EBI-1761423, EBI-3908684;
CC Q9H222; P16333: NCK1; NbExp=2; IntAct=EBI-1761423, EBI-389883;
CC Q9H222-1; Q9H221-1: ABCG8; NbExp=5; IntAct=EBI-16205983, EBI-16205990;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16893193,
CC ECO:0000305|PubMed:27144356}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27144356}. Apical cell membrane
CC {ECO:0000269|PubMed:14504269}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27144356}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H222-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H222-2; Sequence=VSP_055770;
CC -!- TISSUE SPECIFICITY: Strongly expressed in the liver, lower levels in
CC the small intestine and colon. {ECO:0000269|PubMed:11099417,
CC ECO:0000269|PubMed:11138003}.
CC -!- DOMAIN: The Walker motif (consensus sequence G-X-X-G-X-G-K-[ST]-T) is
CC expected to bind ATP. Within this motif, the conserved Lys is essential
CC for transport activity mediated by the heterodimer with ABCG8.
CC {ECO:0000250|UniProtKB:Q99PE8}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16893193,
CC ECO:0000269|PubMed:20210363}.
CC -!- DISEASE: Sitosterolemia 2 (STSL2) [MIM:618666]: A form of
CC sitosterolemia, an autosomal recessive metabolic disorder characterized
CC by unregulated intestinal absorption of cholesterol, phytosterols and
CC shellfish sterols, and decreased biliary excretion of dietary sterols
CC into bile. Patients have hypercholesterolemia, very high levels of
CC plant sterols in the plasma, and frequently develop tendon and tuberous
CC xanthomas, accelerated atherosclerosis and premature coronary artery
CC disease. {ECO:0000269|PubMed:11138003, ECO:0000269|PubMed:11452359,
CC ECO:0000269|PubMed:11668628, ECO:0000269|PubMed:15054092}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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; AF320293; AAG40003.1; -; mRNA.
DR EMBL; AF312715; AAG53099.1; -; mRNA.
DR EMBL; AC011242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAX00286.1; -; Genomic_DNA.
DR EMBL; BC111541; AAI11542.1; -; mRNA.
DR EMBL; AF404106; AAK85387.1; -; Genomic_DNA.
DR EMBL; AF404107; AAK85388.1; -; Genomic_DNA.
DR CCDS; CCDS1814.1; -. [Q9H222-1]
DR RefSeq; NP_071881.1; NM_022436.2. [Q9H222-1]
DR PDB; 5DO7; X-ray; 3.93 A; A/C=1-651.
DR PDB; 7JR7; EM; 3.30 A; A=1-651.
DR PDB; 7R87; EM; 3.40 A; A=1-651.
DR PDB; 7R88; EM; 3.50 A; A=1-651.
DR PDB; 7R89; EM; 2.60 A; A=1-651.
DR PDB; 7R8A; EM; 2.90 A; A=1-651.
DR PDB; 7R8B; EM; 3.10 A; A=1-651.
DR PDBsum; 5DO7; -.
DR PDBsum; 7JR7; -.
DR PDBsum; 7R87; -.
DR PDBsum; 7R88; -.
DR PDBsum; 7R89; -.
DR PDBsum; 7R8A; -.
DR PDBsum; 7R8B; -.
DR AlphaFoldDB; Q9H222; -.
DR SMR; Q9H222; -.
DR BioGRID; 122124; 2.
DR CORUM; Q9H222; -.
DR DIP; DIP-42630N; -.
DR IntAct; Q9H222; 5.
DR MINT; Q9H222; -.
DR STRING; 9606.ENSP00000260645; -.
DR DrugBank; DB11635; Tocofersolan.
DR TCDB; 3.A.1.204.5; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q9H222; 2 sites.
DR iPTMnet; Q9H222; -.
DR PhosphoSitePlus; Q9H222; -.
DR BioMuta; ABCG5; -.
DR DMDM; 17432917; -.
DR MassIVE; Q9H222; -.
DR PaxDb; Q9H222; -.
DR PeptideAtlas; Q9H222; -.
DR PRIDE; Q9H222; -.
DR ProteomicsDB; 61443; -.
DR ProteomicsDB; 80475; -. [Q9H222-1]
DR Antibodypedia; 14899; 235 antibodies from 31 providers.
DR DNASU; 64240; -.
DR Ensembl; ENST00000405322.8; ENSP00000384513.2; ENSG00000138075.14. [Q9H222-1]
DR GeneID; 64240; -.
DR KEGG; hsa:64240; -.
DR MANE-Select; ENST00000405322.8; ENSP00000384513.2; NM_022436.3; NP_071881.1.
DR UCSC; uc002rtn.3; human. [Q9H222-1]
DR CTD; 64240; -.
DR DisGeNET; 64240; -.
DR GeneCards; ABCG5; -.
DR GeneReviews; ABCG5; -.
DR HGNC; HGNC:13886; ABCG5.
DR HPA; ENSG00000138075; Group enriched (intestine, liver).
DR MalaCards; ABCG5; -.
DR MIM; 605459; gene.
DR MIM; 618666; phenotype.
DR neXtProt; NX_Q9H222; -.
DR OpenTargets; ENSG00000138075; -.
DR Orphanet; 391665; Homozygous familial hypercholesterolemia.
DR Orphanet; 2882; Sitosterolemia.
DR PharmGKB; PA24411; -.
DR VEuPathDB; HostDB:ENSG00000138075; -.
DR eggNOG; KOG0061; Eukaryota.
DR GeneTree; ENSGT00940000157985; -.
DR HOGENOM; CLU_000604_57_9_1; -.
DR InParanoid; Q9H222; -.
DR OMA; RVRPWWD; -.
DR OrthoDB; 1022017at2759; -.
DR PhylomeDB; Q9H222; -.
DR TreeFam; TF105212; -.
DR PathwayCommons; Q9H222; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-HSA-5679090; Defective ABCG8 causes GBD4 and sitosterolemia.
DR Reactome; R-HSA-5679096; Defective ABCG5 causes sitosterolemia.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; Q9H222; -.
DR SIGNOR; Q9H222; -.
DR BioGRID-ORCS; 64240; 7 hits in 1060 CRISPR screens.
DR ChiTaRS; ABCG5; human.
DR GeneWiki; ABCG5; -.
DR GenomeRNAi; 64240; -.
DR Pharos; Q9H222; Tbio.
DR PRO; PR:Q9H222; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9H222; protein.
DR Bgee; ENSG00000138075; Expressed in jejunal mucosa and 43 other tissues.
DR Genevisible; Q9H222; HS.
DR GO; GO:0016324; C:apical plasma membrane; IMP:BHF-UCL.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0120020; F:cholesterol transfer activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR GO; GO:0038183; P:bile acid signaling pathway; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IMP:UniProtKB.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:UniProtKB.
DR GO; GO:0030299; P:intestinal cholesterol absorption; IC:BHF-UCL.
DR GO; GO:0045796; P:negative regulation of intestinal cholesterol absorption; IMP:BHF-UCL.
DR GO; GO:0010949; P:negative regulation of intestinal phytosterol absorption; IMP:BHF-UCL.
DR GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0015918; P:sterol transport; ISS:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
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; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Disease variant; Glycoprotein; Lipid transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..651
FT /note="ATP-binding cassette sub-family G member 5"
FT /id="PRO_0000093393"
FT TOPO_DOM 1..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TRANSMEM 384..404
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TOPO_DOM 405..421
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TRANSMEM 422..442
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TOPO_DOM 443..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TRANSMEM 468..489
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TOPO_DOM 490..500
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TRANSMEM 501..521
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TOPO_DOM 522..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TRANSMEM 529..549
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TOPO_DOM 550..623
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TRANSMEM 624..644
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:27144356"
FT TOPO_DOM 645..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27144356"
FT DOMAIN 52..293
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 388..645
FT /note="ABC transmembrane type-2"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..395
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055770"
FT VARIANT 50
FT /note="R -> C (in dbSNP:rs6756629)"
FT /id="VAR_048142"
FT VARIANT 146
FT /note="E -> Q (in STSL2; decreased maturation of glycan
FT chains; dbSNP:rs758551848)"
FT /evidence="ECO:0000269|PubMed:11452359,
FT ECO:0000269|PubMed:15054092"
FT /id="VAR_012244"
FT VARIANT 389
FT /note="R -> H (in STSL2; loss of normal maturation of
FT glycan chains; dbSNP:rs119480069)"
FT /evidence="ECO:0000269|PubMed:11138003,
FT ECO:0000269|PubMed:11452359, ECO:0000269|PubMed:15054092"
FT /id="VAR_012245"
FT VARIANT 419
FT /note="R -> H (in STSL2; loss of normal maturation of
FT glycan chains; dbSNP:rs119479067)"
FT /evidence="ECO:0000269|PubMed:11138003,
FT ECO:0000269|PubMed:11452359, ECO:0000269|PubMed:15054092"
FT /id="VAR_012246"
FT VARIANT 419
FT /note="R -> P (in STSL2; strongly decreased maturation of
FT glycan chains; dbSNP:rs119479067)"
FT /evidence="ECO:0000269|PubMed:11138003,
FT ECO:0000269|PubMed:11452359, ECO:0000269|PubMed:15054092"
FT /id="VAR_012247"
FT VARIANT 437
FT /note="N -> K (in STSL2; loss of normal maturation of
FT glycan chains; dbSNP:rs575266356)"
FT /evidence="ECO:0000269|PubMed:11668628,
FT ECO:0000269|PubMed:15054092"
FT /id="VAR_020781"
FT VARIANT 517
FT /note="T -> S (in dbSNP:rs17031672)"
FT /id="VAR_033457"
FT VARIANT 523
FT /note="I -> V (in dbSNP:rs140899003)"
FT /evidence="ECO:0000269|PubMed:11668628"
FT /id="VAR_020782"
FT VARIANT 550
FT /note="R -> S (in STSL2)"
FT /evidence="ECO:0000269|PubMed:11452359"
FT /id="VAR_012248"
FT VARIANT 600
FT /note="C -> Y (in dbSNP:rs779109455)"
FT /evidence="ECO:0000269|PubMed:11668628"
FT /id="VAR_020783"
FT VARIANT 604
FT /note="Q -> E (in dbSNP:rs6720173)"
FT /evidence="ECO:0000269|PubMed:11099417,
FT ECO:0000269|PubMed:11138003, ECO:0000269|PubMed:11452359,
FT ECO:0000269|PubMed:11668628"
FT /id="VAR_012249"
FT VARIANT 622
FT /note="M -> V (in dbSNP:rs140374206)"
FT /evidence="ECO:0000269|PubMed:11668628"
FT /id="VAR_020784"
FT MUTAGEN 92..93
FT /note="KT->RA: Abolishes increase of the very low basal
FT ATPase activity by cholate."
FT /evidence="ECO:0000269|PubMed:20210363"
FT MUTAGEN 432
FT /note="Y->A: Strongly decreases cholesterol secretion into
FT bile."
FT /evidence="ECO:0000269|PubMed:27144356"
FT MUTAGEN 540
FT /note="A->F: Strongly decreases cholesterol secretion into
FT bile."
FT /evidence="ECO:0000269|PubMed:27144356"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:7R8B"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:7R89"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:7R8B"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7R8A"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 161..174
FT /evidence="ECO:0007829|PDB:7R89"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:7R89"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:7R89"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 225..240
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 244..248
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:7R89"
FT TURN 257..259
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 277..286
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 312..330
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:7R8B"
FT HELIX 364..380
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 383..404
FT /evidence="ECO:0007829|PDB:7R89"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 415..453
FT /evidence="ECO:0007829|PDB:7R89"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 460..490
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 496..523
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 527..544
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 546..550
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 557..563
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 567..579
FT /evidence="ECO:0007829|PDB:7R89"
FT STRAND 580..582
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 605..612
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:7R87"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:7R89"
FT HELIX 620..648
FT /evidence="ECO:0007829|PDB:7R89"
SQ SEQUENCE 651 AA; 72504 MW; 950BABFCBB6A1536 CRC64;
MGDLSSLTPG GSMGLQVNRG SQSSLEGAPA TAPEPHSLGI LHASYSVSHR VRPWWDITSC
RQQWTRQILK DVSLYVESGQ IMCILGSSGS GKTTLLDAMS GRLGRAGTFL GEVYVNGRAL
RREQFQDCFS YVLQSDTLLS SLTVRETLHY TALLAIRRGN PGSFQKKVEA VMAELSLSHV
ADRLIGNYSL GGISTGERRR VSIAAQLLQD PKVMLFDEPT TGLDCMTANQ IVVLLVELAR
RNRIVVLTIH QPRSELFQLF DKIAILSFGE LIFCGTPAEM LDFFNDCGYP CPEHSNPFDF
YMDLTSVDTQ SKEREIETSK RVQMIESAYK KSAICHKTLK NIERMKHLKT LPMVPFKTKD
SPGVFSKLGV LLRRVTRNLV RNKLAVITRL LQNLIMGLFL LFFVLRVRSN VLKGAIQDRV
GLLYQFVGAT PYTGMLNAVN LFPVLRAVSD QESQDGLYQK WQMMLAYALH VLPFSVVATM
IFSSVCYWTL GLHPEVARFG YFSAALLAPH LIGEFLTLVL LGIVQNPNIV NSVVALLSIA
GVLVGSGFLR NIQEMPIPFK IISYFTFQKY CSEILVVNEF YGLNFTCGSS NVSVTTNPMC
AFTQGIQFIE KTCPGATSRF TMNFLILYSF IPALVILGIV VFKIRDHLIS R
