ID ABCG2_HUMAN Reviewed; 655 AA. AC Q9UNQ0; A0A1W3; A8K1T5; O95374; Q4W5I3; Q53ZQ1; Q569L4; Q5YLG4; Q86V64; AC Q8IX16; Q96LD6; Q96TA8; Q9BY73; Q9NUS0; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 3. DT 27-MAR-2024, entry version 221. DE RecName: Full=Broad substrate specificity ATP-binding cassette transporter ABCG2 {ECO:0000305}; DE EC=7.6.2.2 {ECO:0000269|PubMed:11306452, ECO:0000269|PubMed:31254042}; DE AltName: Full=ATP-binding cassette sub-family G member 2; DE AltName: Full=Breast cancer resistance protein; DE AltName: Full=CDw338; DE AltName: Full=Mitoxantrone resistance-associated protein; DE AltName: Full=Placenta-specific ATP-binding cassette transporter; DE AltName: Full=Urate exporter; DE AltName: CD_antigen=CD338; GN Name=ABCG2; Synonyms=ABCP, BCRP, BCRP1, MXR; 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), VARIANTS GLU-166 AND SER-208, AND RP TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=9850061; RA Allikmets R., Schriml L.M., Hutchinson A., Romano-Spica V., Dean M.; RT "A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome RT 4q22 that is involved in multidrug resistance."; RL Cancer Res. 58:5337-5339(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Mammary cancer; RX PubMed=9861027; DOI=10.1073/pnas.95.26.15665; RA Doyle L.A., Yang W., Abruzzo L.V., Krogmann T., Gao Y., Rishi A.K., RA Ross D.D.; RT "A multidrug resistance transporter from human MCF-7 breast cancer cells."; RL Proc. Natl. Acad. Sci. U.S.A. 95:15665-15670(1998). RN [3] RP ERRATUM OF PUBMED:9861027. RA Doyle L.A., Yang W., Abruzzo L.V., Krogmann T., Gao Y., Rishi A.K., RA Ross D.D.; RL Proc. Natl. Acad. Sci. U.S.A. 96:2569-2569(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Kage K., Tsukahara S., Sugiyama T., Asada S., Ishikawa E., Tsuruo T., RA Sugimoto Y.; RT "Breast cancer resistance protein constitutes a 140-kDa complex as a RT homodimer."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=11306452; RA Komatani H., Kotani H., Hara Y., Nakagawa R., Matsumoto M., Arakawa H., RA Nishimura S.; RT "Identification of breast cancer resistant protein/mitoxantrone RT resistance/placenta-specific, ATP-binding cassette transporter as a RT transporter of NB-506 and J-107088, topoisomerase I inhibitors with an RT indolocarbazole structure."; RL Cancer Res. 61:2827-2832(2001). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11533706; DOI=10.1038/nm0901-1028; RA Zhou S., Schuetz J.D., Bunting K.D., Colapietro A.M., Sampath J., RA Morris J.J., Lagutina I., Grosveld G.C., Osawa M., Nakauchi H., RA Sorrentino B.P.; RT "The ABC transporter Bcrp1/ABCG2 is expressed in a wide variety of stem RT cells and is a molecular determinant of the side-population phenotype."; RL Nat. Med. 7:1028-1034(2001). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, RP TISSUE SPECIFICITY, AND VARIANTS GLU-166 AND SER-208. RC TISSUE=Brain endothelium; RX PubMed=12958161; DOI=10.1096/fj.02-1131fje; RA Zhang W., Mojsilovic-Petrovic J., Andrade M.F., Zhang H., Ball M., RA Stanimirovic D.B.; RT "The expression and functional characterization of ABCG2 in brain RT endothelial cells and vessels."; RL FASEB J. 17:2085-2087(2003). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-141. RA Yoshikawa M., Yabuuchi H., Ikegami Y., Ishikawa T.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-316. RA Sudarikov A., Makarik T., Andreeff M.; RT "Cell line K562 resistant to Hoechst 33342."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hippocampus, and Placenta; 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 [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-12; LYS-141; HIS-296 RP AND THR-528. RG SeattleSNPs variation discovery resource; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [12] 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 [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP LYS-141. RC TISSUE=Pancreas, and PNS; 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 [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 294-655 (ISOFORM 1). RX PubMed=9892175; RA Miyake K., Mickley L., Litman T., Zhan Z., Robey R.W., Cristensen B., RA Brangi M., Greenberger L., Dean M., Fojo T., Bates S.E.; RT "Molecular cloning of cDNAs which are highly overexpressed in mitoxantrone- RT resistant cells: demonstration of homology to ABC transport genes."; RL Cancer Res. 59:8-13(1999). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=12477054; RA Allen J.D., van Loevezijn A., Lakhai J.M., van der Valk M., RA van Tellingen O., Reid G., Schellens J.H., Koomen G.J., Schinkel A.H.; RT "Potent and specific inhibition of the breast cancer resistance protein RT multidrug transporter in vitro and in mouse intestine by a novel analogue RT of fumitremorgin C."; RL Mol. Cancer Ther. 1:417-425(2002). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12682043; DOI=10.1074/jbc.m212399200; RA Suzuki M., Suzuki H., Sugimoto Y., Sugiyama Y.; RT "ABCG2 transports sulfated conjugates of steroids and xenobiotics."; RL J. Biol. Chem. 278:22644-22649(2003). RN [17] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=15001581; DOI=10.1074/jbc.m310785200; RA Xu J., Liu Y., Yang Y., Bates S., Zhang J.T.; RT "Characterization of oligomeric human half-ABC transporter ATP-binding RT cassette G2."; RL J. Biol. Chem. 279:19781-19789(2004). RN [18] RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-596, LACK OF GLYCOSYLATION AT RP ASN-418 AND ASN-557, AND MUTAGENESIS OF ASN-418; ASN-557 AND ASN-596. RX PubMed=15807535; DOI=10.1021/bi0479858; RA Diop N.K., Hrycyna C.A.; RT "N-linked glycosylation of the human ABC transporter ABCG2 on asparagine RT 596 is not essential for expression, transport activity, or trafficking to RT the plasma membrane."; RL Biochemistry 44:5420-5429(2005). RN [19] RP FUNCTION, AND MUTAGENESIS OF ARG-482. RX PubMed=15670731; DOI=10.1016/j.bbamem.2004.11.005; RA Oezvegy-Laczka C., Koebloes G., Sarkadi B., Varadi A.; RT "Single amino acid (482) variants of the ABCG2 multidrug transporter: major RT differences in transport capacity and substrate recognition."; RL Biochim. Biophys. Acta 1668:53-63(2005). RN [20] RP MUTAGENESIS OF LYS-86, SUBCELLULAR LOCATION, AND HOMODIMERIZATION. RX PubMed=15769853; DOI=10.1242/jcs.01729; RA Henriksen U., Gether U., Litman T.; RT "Effect of Walker A mutation (K86M) on oligomerization and surface RT targeting of the multidrug resistance transporter ABCG2."; RL J. Cell Sci. 118:1417-1426(2005). RN [21] RP SUBUNIT, AND DISULFIDE BONDS. RX PubMed=17686774; DOI=10.1074/jbc.c700133200; RA Wakabayashi K., Nakagawa H., Tamura A., Koshiba S., Hoshijima K., RA Komada M., Ishikawa T.; RT "Intramolecular disulfide bond is a critical check point determining RT degradative fates of ATP-binding cassette (ABC) transporter ABCG2 RT protein."; RL J. Biol. Chem. 282:27841-27846(2007). RN [22] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, PHOSPHORYLATION AT THR-362, AND RP MUTAGENESIS OF THR-362. RX PubMed=18056989; DOI=10.1074/jbc.m707773200; RA Xie Y., Xu K., Linn D.E., Yang X., Guo Z., Shimelis H., Nakanishi T., RA Ross D.D., Chen H., Fazli L., Gleave M.E., Qiu Y.; RT "The 44-kDa Pim-1 kinase phosphorylates BCRP/ABCG2 and thereby promotes its RT multimerization and drug-resistant activity in human prostate cancer RT cells."; RL J. Biol. Chem. 283:3349-3356(2008). RN [23] RP POLYMORPHISM, AND INVOLVEMENT IN UAQTL1 AND GOUT. RX PubMed=18834626; DOI=10.1016/s0140-6736(08)61343-4; RA Dehghan A., Kottgen A., Yang Q., Hwang S.J., Kao W.L., Rivadeneira F., RA Boerwinkle E., Levy D., Hofman A., Astor B.C., Benjamin E.J., RA van Duijn C.M., Witteman J.C., Coresh J., Fox C.S.; RT "Association of three genetic loci with uric acid concentration and risk of RT gout: a genome-wide association study."; RL Lancet 372:1953-1961(2008). RN [24] RP POLYMORPHISM, INVOLVEMENT IN UAQTL1, ASSOCIATION OF VARIANT LYS-141 WITH RP GOUT, CHARACTERIZATION OF VARIANT LYS-141, FUNCTION, CATALYTIC ACTIVITY, RP AND SUBCELLULAR LOCATION. RX PubMed=19506252; DOI=10.1073/pnas.0901249106; RA Woodward O.M., Kottgen A., Coresh J., Boerwinkle E., Guggino W.B., RA Kottgen M.; RT "Identification of a urate transporter, ABCG2, with a common functional RT polymorphism causing gout."; RL Proc. Natl. Acad. Sci. U.S.A. 106:10338-10342(2009). RN [25] RP FUNCTION, CATALYTIC ACTIVITY, POLYMORPHISM, INVOLVEMENT IN UAQTL1, AND RP ASSOCIATION OF VARIANT LYS-141 WITH GOUT. RX PubMed=20368174; DOI=10.1126/scitranslmed.3000237; RA Matsuo H., Takada T., Ichida K., Nakamura T., Nakayama A., Ikebuchi Y., RA Ito K., Kusanagi Y., Chiba T., Tadokoro S., Takada Y., Oikawa Y., Inoue H., RA Suzuki K., Okada R., Nishiyama J., Domoto H., Watanabe S., Fujita M., RA Morimoto Y., Naito M., Nishio K., Hishida A., Wakai K., Asai Y., Niwa K., RA Kamakura K., Nonoyama S., Sakurai Y., Hosoya T., Kanai Y., Suzuki H., RA Hamajima N., Shinomiya N.; RT "Common defects of ABCG2, a high-capacity urate exporter, cause gout: a RT function-based genetic analysis in a Japanese population."; RL Sci. Transl. Med. 1:5RA11-5RA11(2009). RN [26] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20110355; DOI=10.1074/jbc.m109.064162; RA Takabe K., Kim R.H., Allegood J.C., Mitra P., Ramachandran S., RA Nagahashi M., Harikumar K.B., Hait N.C., Milstien S., Spiegel S.; RT "Estradiol induces export of sphingosine 1-phosphate from breast cancer RT cells via ABCC1 and ABCG2."; RL J. Biol. Chem. 285:10477-10486(2010). RN [27] RP CAUTION. RX PubMed=20332504; DOI=10.1074/jbc.m109.090506; RA Brechbuhl H.M., Gould N., Kachadourian R., Riekhof W.R., Voelker D.R., RA Day B.J.; RT "Glutathione transport is a unique function of the ATP-binding cassette RT protein ABCG2."; RL J. Biol. Chem. 285:16582-16587(2010). RN [28] RP FUNCTION, DOMAIN, AND MUTAGENESIS OF HIS-583; CYS-603 AND TYR-605. RX PubMed=20705604; DOI=10.1074/jbc.m110.139170; RA Desuzinges-Mandon E., Arnaud O., Martinez L., Huche F., Di Pietro A., RA Falson P.; RT "ABCG2 transports and transfers heme to albumin through its large RT extracellular loop."; RL J. Biol. Chem. 285:33123-33133(2010). RN [29] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=22132962; DOI=10.1080/15257770.2011.633953; RA Nakayama A., Matsuo H., Takada T., Ichida K., Nakamura T., Ikebuchi Y., RA Ito K., Hosoya T., Kanai Y., Suzuki H., Shinomiya N.; RT "ABCG2 is a high-capacity urate transporter and its genetic impairment RT increases serum uric acid levels in humans."; RL Nucleosides Nucleotides Nucleic Acids 30:1091-1097(2011). RN [30] RP POLYMORPHISM, INVOLVEMENT IN JR, AND VARIANT MET-12. RX PubMed=22246507; DOI=10.1038/ng.1075; RA Zelinski T., Coghlan G., Liu X.Q., Reid M.E.; RT "ABCG2 null alleles define the Jr(a-) blood group phenotype."; RL Nat. Genet. 44:131-132(2012). RN [31] RP POLYMORPHISM, AND INVOLVEMENT IN JR. RX PubMed=22246505; DOI=10.1038/ng.1070; RA Saison C., Helias V., Ballif B.A., Peyrard T., Puy H., Miyazaki T., RA Perrot S., Vayssier-Taussat M., Waldner M., Le Pennec P.Y., Cartron J.P., RA Arnaud L.; RT "Null alleles of ABCG2 encoding the breast cancer resistance protein define RT the new blood group system Junior."; RL Nat. Genet. 44:174-177(2012). RN [32] RP FUNCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION. RX PubMed=23189181; DOI=10.1371/journal.pone.0050082; RA Kobuchi H., Moriya K., Ogino T., Fujita H., Inoue K., Shuin T., Yasuda T., RA Utsumi K., Utsumi T.; RT "Mitochondrial localization of ABC transporter ABCG2 and its function in 5- RT aminolevulinic acid-mediated protoporphyrin IX accumulation."; RL PLoS ONE 7:E50082-E50082(2012). RN [33] RP CAUTION. RX PubMed=24312054; DOI=10.3389/fphar.2013.00138; RA Gauthier C., Ozvegy-Laczka C., Szakacs G., Sarkadi B., Di Pietro A.; RT "ABCG2 is not able to catalyze glutathione efflux and does not contribute RT to GSH-dependent collateral sensitivity."; RL Front. Pharmacol. 4:138-138(2013). RN [34] RP SUBCELLULAR LOCATION. RX PubMed=28623970; DOI=10.1016/j.placenta.2017.04.006; RA Szilagyi J.T., Vetrano A.M., Laskin J.D., Aleksunes L.M.; RT "Localization of the placental BCRP/ABCG2 transporter to lipid rafts: Role RT for cholesterol in mediating efflux activity."; RL Placenta 55:29-36(2017). RN [35] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, CHARACTERIZATION OF RP VARIANT LYS-141; TRP-147; MET-153; LYS-360 DEL; CYS-373; MET-434 AND RP PRO-476, AND MUTAGENESIS OF MET-71; LYS-86 AND ARG-383. RX PubMed=31254042; DOI=10.1007/s00018-019-03186-2; RA Zambo B., Mozner O., Bartos Z., Toeroek G., Varady G., Telbisz A., RA Homolya L., Orban T.I., Sarkadi B.; RT "Cellular expression and function of naturally occurring variants of the RT human ABCG2 multidrug transporter."; RL Cell. Mol. Life Sci. 77:365-378(2020). RN [36] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=36749388; DOI=10.1007/s00424-023-02792-1; RA Toyoda Y., Miyata H., Uchida N., Morimoto K., Shigesawa R., Kassai H., RA Nakao K., Tomioka N.H., Matsuo H., Ichida K., Hosoyamada M., Aiba A., RA Suzuki H., Takada T.; RT "Vitamin C transporter SVCT1 serves a physiological role as a urate RT importer: functional analyses and in vivo investigations."; RL Pflugers Arch. 475:489-504(2023). RN [37] RP STRUCTURE BY ELECTRON MICROSCOPY (3.78 ANGSTROMS) OF 2-655, FUNCTION, RP CATALYTIC ACTIVITY, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-596, AND RP MUTAGENESIS OF GLU-211. RX PubMed=28554189; DOI=10.1038/nature22345; RA Taylor N.M.I., Manolaridis I., Jackson S.M., Kowal J., Stahlberg H., RA Locher K.P.; RT "Structure of the human multidrug transporter ABCG2."; RL Nature 546:504-509(2017). RN [38] RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) IN COMPLEX WITH RP INHIBITORS. RX PubMed=29610494; DOI=10.1038/s41594-018-0049-1; RA Jackson S.M., Manolaridis I., Kowal J., Zechner M., Taylor N.M.I., RA Bause M., Bauer S., Bartholomaeus R., Bernhardt G., Koenig B., RA Buschauer A., Stahlberg H., Altmann K.H., Locher K.P.; RT "Structural basis of small-molecule inhibition of human multidrug RT transporter ABCG2."; RL Nat. Struct. Mol. Biol. 25:333-340(2018). RN [39] RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS) OF MUTANT GLN-211 IN RP COMPLEX WITH ATP, MUTAGENESIS OF GLU-211; THR-435; ASN-436; PHE-439; RP VAL-546; MET-549; LEU-554 AND LEU-555, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30405239; DOI=10.1038/s41586-018-0680-3; RA Manolaridis I., Jackson S.M., Taylor N.M.I., Kowal J., Stahlberg H., RA Locher K.P.; RT "Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and RT substrate-bound states."; RL Nature 563:426-430(2018). RN [40] RP VARIANTS MET-12 AND LYS-141. RX PubMed=12111378; DOI=10.1007/s100380200041; RA Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K., RA Harigae S., Osawa S., Nakamura Y.; RT "Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes RT encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8, RT ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and ABCG8."; RL J. Hum. Genet. 47:285-310(2002). RN [41] RP VARIANTS LEU-431 AND LEU-489. RX PubMed=15618737; DOI=10.2133/dmpk.18.212; RA Itoda M., Saito Y., Shirao K., Minami H., Ohtsu A., Yoshida T., Saijo N., RA Suzuki H., Sugiyama Y., Ozawa S., Sawada J.; RT "Eight novel single nucleotide polymorphisms in ABCG2/BCRP in Japanese RT cancer patients administered irinotacan."; RL Drug Metab. Pharmacokinet. 18:212-217(2003). RN [42] RP VARIANTS MET-12; LYS-141; LEU-206 AND TYR-590. RX PubMed=12544509; DOI=10.1097/00008571-200301000-00004; RA Zamber C.P., Lamba J.K., Yasuda K., Farnum J., Thummel K., Schuetz J.D., RA Schuetz E.G.; RT "Natural allelic variants of breast cancer resistance protein (BCRP) and RT their relationship to BCRP expression in human intestine."; RL Pharmacogenetics 13:19-28(2003). RN [43] RP CHARACTERIZATION OF VARIANTS MET-12; LYS-141 AND ASN-620. RX PubMed=15838659; DOI=10.1007/s00280-004-0931-x; RA Morisaki K., Robey R.W., Oezvegy-Laczka C., Honjo Y., Polgar O., RA Steadman K., Sarkadi B., Bates S.E.; RT "Single nucleotide polymorphisms modify the transporter activity of RT ABCG2."; RL Cancer Chemother. Pharmacol. 56:161-172(2005). RN [44] RP VARIANTS MET-12; LEU-13; LYS-141; GLN-160; ARG-354; LEU-431; ASN-441 AND RP LEU-489. RX PubMed=16702730; DOI=10.2133/dmpk.21.109; RA Maekawa K., Itoda M., Sai K., Saito Y., Kaniwa N., Shirao K., Hamaguchi T., RA Kunitoh H., Yamamoto N., Tamura T., Minami H., Kubota K., Ohtsu A., RA Yoshida T., Saijo N., Kamatani N., Ozawa S., Sawada J.; RT "Genetic variation and haplotype structure of the ABC transporter gene RT ABCG2 in a Japanese population."; RL Drug Metab. Pharmacokinet. 21:109-121(2006). RN [45] RP VARIANTS TRP-147; MET-153; LYS-360 DEL; CYS-373; ALA-421; MET-434; PRO-476; RP ARG-572 AND ASN-620, CHARACTERIZATION OF VARIANTS LYS-141; TRP-147; RP MET-153; LYS-360 DEL; CYS-373; ALA-421; MET-434; PRO-476; ARG-572 AND RP ASN-620, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=31003562; DOI=10.3390/cells8040363; RA Toyoda Y., Mancikova A., Krylov V., Morimoto K., Pavelcova K., Bohata J., RA Pavelka K., Pavlikova M., Suzuki H., Matsuo H., Takada T., Stiburkova B.; RT "Functional Characterization of Clinically-Relevant Rare Variants in ABCG2 RT Identified in a Gout and Hyperuricemia Cohort."; RL Cells 8:0-0(2019). CC -!- FUNCTION: Broad substrate specificity ATP-dependent transporter of the CC ATP-binding cassette (ABC) family that actively extrudes a wide variety CC of physiological compounds, dietary toxins and xenobiotics from cells CC (PubMed:11306452, PubMed:12958161, PubMed:19506252, PubMed:20705604, CC PubMed:28554189, PubMed:30405239, PubMed:31003562). Involved in CC porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) CC from both mitochondria to cytosol and cytosol to extracellular space, CC it also functions in the cellular export of heme (PubMed:20705604, CC PubMed:23189181). Also mediates the efflux of sphingosine-1-P from CC cells (PubMed:20110355). Acts as a urate exporter functioning in both CC renal and extrarenal urate excretion (PubMed:19506252, PubMed:20368174, CC PubMed:22132962, PubMed:31003562, PubMed:36749388). In kidney, it also CC functions as a physiological exporter of the uremic toxin indoxyl CC sulfate (By similarity). Also involved in the excretion of steroids CC like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, CC and other sulfate conjugates (PubMed:12682043, PubMed:28554189, CC PubMed:30405239). Mediates the secretion of the riboflavin and biotin CC vitamins into milk (By similarity). Extrudes pheophorbide a, a CC phototoxic porphyrin catabolite of chlorophyll, reducing its CC bioavailability (By similarity). Plays an important role in the CC exclusion of xenobiotics from the brain (Probable). It confers to cells CC a resistance to multiple drugs and other xenobiotics including CC mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, CC and the anthracyclines daunorubicin and doxorubicin, through the CC control of their efflux (PubMed:11306452, PubMed:12477054, CC PubMed:15670731, PubMed:18056989, PubMed:31254042). In placenta, it CC limits the penetration of drugs from the maternal plasma into the fetus CC (By similarity). May play a role in early stem cell self-renewal by CC blocking differentiation (By similarity). CC {ECO:0000250|UniProtKB:Q7TMS5, ECO:0000269|PubMed:11306452, CC ECO:0000269|PubMed:12477054, ECO:0000269|PubMed:12682043, CC ECO:0000269|PubMed:12958161, ECO:0000269|PubMed:15670731, CC ECO:0000269|PubMed:18056989, ECO:0000269|PubMed:19506252, CC ECO:0000269|PubMed:20110355, ECO:0000269|PubMed:20368174, CC ECO:0000269|PubMed:20705604, ECO:0000269|PubMed:22132962, CC ECO:0000269|PubMed:23189181, ECO:0000269|PubMed:28554189, CC ECO:0000269|PubMed:30405239, ECO:0000269|PubMed:31003562, CC ECO:0000269|PubMed:31254042, ECO:0000305|PubMed:12958161}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + CC xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:11306452, CC ECO:0000269|PubMed:12477054, ECO:0000269|PubMed:12958161, CC ECO:0000269|PubMed:31254042}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out); CC Xref=Rhea:RHEA:16461, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17775, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:36749388, CC ECO:0000305|PubMed:19506252, ECO:0000305|PubMed:20368174, CC ECO:0000305|PubMed:22132962, ECO:0000305|PubMed:31003562}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462; CC Evidence={ECO:0000269|PubMed:22132962}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + indoxyl sulfate(in) = ADP + H(+) + indoxyl CC sulfate(out) + phosphate; Xref=Rhea:RHEA:61332, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:144643, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q7TMS5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61333; CC Evidence={ECO:0000250|UniProtKB:Q7TMS5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) + CC phosphate + sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38951, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60119, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:20110355}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952; CC Evidence={ECO:0000269|PubMed:20110355}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + estrone 3-sulfate(in) + H2O = ADP + estrone 3- CC sulfate(out) + H(+) + phosphate; Xref=Rhea:RHEA:61348, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60050, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:12682043, ECO:0000269|PubMed:28554189, CC ECO:0000269|PubMed:30405239}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61349; CC Evidence={ECO:0000269|PubMed:12682043}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP + CC dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate; CC Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12682043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365; CC Evidence={ECO:0000269|PubMed:12682043}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-methylumbelliferone sulfate(in) + ATP + H2O = 4- CC methylumbelliferone sulfate(out) + ADP + H(+) + phosphate; CC Xref=Rhea:RHEA:61368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144581, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12682043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61369; CC Evidence={ECO:0000269|PubMed:12682043}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3- CC benzothiazol-6-yl beta-D-glucuronate(in) + ATP + H2O = 5,7-dimethyl- CC 2-methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl beta-D- CC glucuronate(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:61384, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:144584, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:12682043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61385; CC Evidence={ECO:0000269|PubMed:12682043}; CC -!- CATALYTIC ACTIVITY: CC Reaction=4-methylumbelliferone beta-D-glucuronate(in) + ATP + H2O = 4- CC methylumbelliferone beta-D-glucuronate(out) + ADP + H(+) + phosphate; CC Xref=Rhea:RHEA:61372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:144582, CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:12682043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61373; CC Evidence={ECO:0000269|PubMed:12682043}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)-1,3- CC benzothiazol-6-yl sulfate(in) + ATP + H2O = 5,7-dimethyl-2- CC methylamino-4-(3-pyridylmethyl)-1,3-benzothiazol-6-yl sulfate(out) + CC ADP + H(+) + phosphate; Xref=Rhea:RHEA:61376, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:144583, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:12682043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61377; CC Evidence={ECO:0000269|PubMed:12682043}; CC -!- CATALYTIC ACTIVITY: CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O = CC 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) + CC phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:82961, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:12682043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; CC Evidence={ECO:0000269|PubMed:12682043}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + methotrexate(in) = ADP + H(+) + methotrexate(out) CC + phosphate; Xref=Rhea:RHEA:61356, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:50681, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:12682043}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61357; CC Evidence={ECO:0000269|PubMed:12682043}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + riboflavin(in) = ADP + H(+) + phosphate + CC riboflavin(out); Xref=Rhea:RHEA:61352, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57986, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q7TMS5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61353; CC Evidence={ECO:0000250|UniProtKB:Q7TMS5}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide CC a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58687, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:Q7TMS5}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361; CC Evidence={ECO:0000250|UniProtKB:Q7TMS5}; CC -!- ACTIVITY REGULATION: Specifically inhibited by the fungal toxin CC fumitremorgin C and Ko143. {ECO:0000269|PubMed:12477054}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=16.6 uM for estrone 3-sulfate {ECO:0000269|PubMed:12682043}; CC KM=1.23 mM for ATP {ECO:0000269|PubMed:12682043}; CC KM=12.9 uM for 4-methylumbelliferone sulfate CC {ECO:0000269|PubMed:12682043}; CC KM=26.9 uM for CC 6-hydroxy-5,7-dimethyl-2-methylamino-4-(3-pyridylmethyl)benzothiazole CC sulfate {ECO:0000269|PubMed:12682043}; CC KM=8.24 mM for urate {ECO:0000269|PubMed:22132962}; CC Vmax=2.34 nmol/min/mg enzyme for estrone 3-sulfate transport CC {ECO:0000269|PubMed:12682043}; CC Vmax=6.96 nmol/min/mg enzyme for urate transport CC {ECO:0000269|PubMed:22132962}; CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:15001581, PubMed:17686774, CC PubMed:18056989, PubMed:28554189). The minimal functional unit is a CC homodimer, but the major oligomeric form in plasma membrane is a CC homotetramer with possibility of higher order oligomerization up to CC homododecamers (PubMed:15001581). {ECO:0000269|PubMed:15001581, CC ECO:0000269|PubMed:17686774, ECO:0000269|PubMed:18056989, CC ECO:0000269|PubMed:28554189}. CC -!- INTERACTION: CC Q9UNQ0; Q9UNQ0: ABCG2; NbExp=5; IntAct=EBI-1569435, EBI-1569435; CC Q9UNQ0; P22413: ENPP1; NbExp=4; IntAct=EBI-1569435, EBI-3197846; CC Q9UNQ0; P11309-2: PIM1; NbExp=5; IntAct=EBI-1569435, EBI-1018633; CC Q9UNQ0; P0CG48: UBC; NbExp=2; IntAct=EBI-1569435, EBI-3390054; CC Q9UNQ0-1; Q9UNQ0-1: ABCG2; NbExp=3; IntAct=EBI-20717342, EBI-20717342; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15001581, CC ECO:0000269|PubMed:15769853, ECO:0000269|PubMed:15807535, CC ECO:0000269|PubMed:18056989, ECO:0000269|PubMed:31003562, CC ECO:0000269|PubMed:31254042}; Multi-pass membrane protein CC {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:19506252}; CC Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane CC {ECO:0000269|PubMed:23189181}; Multi-pass membrane protein CC {ECO:0000255}. Note=Enriched in membrane lipid rafts. CC {ECO:0000269|PubMed:28623970}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UNQ0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UNQ0-2; Sequence=VSP_014232, VSP_014233; CC -!- TISSUE SPECIFICITY: Highly expressed in placenta (PubMed:9850061). Low CC expression in small intestine, liver and colon (PubMed:9861027). CC Expressed in brain (at protein level) (PubMed:12958161). CC {ECO:0000269|PubMed:12958161, ECO:0000269|PubMed:9850061, CC ECO:0000269|PubMed:9861027}. CC -!- DOMAIN: The extracellular loop 3 (ECL3) is involved in binding CC porphyrins and transfer them to other carriers, probably albumin. CC {ECO:0000269|PubMed:20705604}. CC -!- PTM: N-glycosylated (PubMed:15807535, PubMed:23189181). Glycosylation- CC deficient ABCG2 is normally expressed and functional. CC {ECO:0000269|PubMed:15807535, ECO:0000269|PubMed:23189181}. CC -!- PTM: Phosphorylated. Phosphorylation at Thr-362 by PIM1 is induced by CC drugs like mitoxantrone and is associated with cells increased drug CC resistance. It regulates the localization to the plasma membrane, the CC homooligomerization and therefore, the activity of the transporter. CC {ECO:0000269|PubMed:18056989}. CC -!- POLYMORPHISM: Genetic variations in ABCG2 define the blood group Junior CC system (JR) [MIM:614490]. Individuals with Jr(a-) blood group lack the CC Jr(a) antigen on their red blood cells. These individuals may have CC anti-Jr(a) antibodies in their serum, which can cause transfusion CC reactions or hemolytic disease of the fetus or newborn. Although the CC clinical significance of the Jr(a-) blood group has been controversial, CC severe fatal hemolytic disease of the newborn has been reported. The CC Jr(a-) phenotype has a higher frequency in individuals of Asian CC descent, compared to those of European descent. The Jr(a-) phenotype is CC inherited as an autosomal recessive trait. CC {ECO:0000269|PubMed:22246505, ECO:0000269|PubMed:22246507}. CC -!- POLYMORPHISM: Genetic variations in ABCG2 influence the variance in CC serum uric acid concentrations and define the serum uric acid CC concentration quantitative trait locus 1 (UAQTL1) [MIM:138900]. Excess CC serum accumulation of uric acid can lead to the development of gout, a CC common disorder characterized by tissue deposition of monosodium urate CC crystals as a consequence of hyperuricemia (PubMed:18834626, CC PubMed:19506252, PubMed:20368174). {ECO:0000269|PubMed:18834626, CC ECO:0000269|PubMed:19506252, ECO:0000269|PubMed:20368174}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family. CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}. CC -!- CAUTION: Was originally proposed to function as a glutathione CC transporter (PubMed:20332504). However, some evidences suggest it is CC not the case (PubMed:24312054). {ECO:0000269|PubMed:20332504, CC ECO:0000269|PubMed:24312054}. CC -!- SEQUENCE CAUTION: CC Sequence=AF093771; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AF093772; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/abcg2/"; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The unwalkable disease CC - Issue 222 of February 2020; CC URL="https://web.expasy.org/spotlight/back_issues/222/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF103796; AAD09188.1; -; mRNA. DR EMBL; AF098951; AAC97367.1; -; mRNA. DR EMBL; AB056867; BAB39212.1; -; mRNA. DR EMBL; AB051855; BAB46933.1; -; mRNA. DR EMBL; AY017168; AAG52982.1; -; mRNA. DR EMBL; AY289766; AAP44087.1; -; mRNA. DR EMBL; AY288307; AAP31310.1; -; mRNA. DR EMBL; AF463519; AAO14617.1; -; mRNA. DR EMBL; AY333755; AAQ92941.1; -; mRNA. DR EMBL; AY333756; AAQ92942.1; -; mRNA. DR EMBL; AK002040; BAA92050.1; -; mRNA. DR EMBL; AK290000; BAF82689.1; -; mRNA. DR EMBL; DQ996467; ABI97388.1; -; Genomic_DNA. DR EMBL; AC084732; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC097484; AAY40902.1; -; Genomic_DNA. DR EMBL; BC021281; AAH21281.1; -; mRNA. DR EMBL; BC092408; AAH92408.1; -; mRNA. DR EMBL; AF093771; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF093772; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS3628.1; -. [Q9UNQ0-1] DR CCDS; CCDS58910.1; -. [Q9UNQ0-2] DR RefSeq; NP_001244315.1; NM_001257386.1. [Q9UNQ0-2] DR RefSeq; NP_004818.2; NM_004827.2. [Q9UNQ0-1] DR RefSeq; XP_005263412.1; XM_005263355.3. DR RefSeq; XP_011530722.1; XM_011532420.2. [Q9UNQ0-1] DR PDB; 5NJ3; EM; 3.78 A; A/B=2-655. DR PDB; 5NJG; EM; 3.78 A; A/B=2-655. DR PDB; 6ETI; EM; 3.10 A; A/B=1-655. DR PDB; 6FEQ; EM; 3.60 A; A/B=1-655. DR PDB; 6FFC; EM; 3.56 A; A/B=2-655. DR PDB; 6HBU; EM; 3.09 A; A/B=1-655. DR PDB; 6HCO; EM; 3.58 A; A/B=2-655. DR PDB; 6HIJ; EM; 3.56 A; A/B=1-655. DR PDB; 6HZM; EM; 3.09 A; A/B=1-655. DR PDB; 6VXF; EM; 3.50 A; A/B=1-655. DR PDB; 6VXH; EM; 4.00 A; A/B=1-655. DR PDB; 6VXI; EM; 3.70 A; A/B=1-655. DR PDB; 6VXJ; EM; 4.10 A; A/B=1-655. DR PDB; 7NEQ; EM; 3.12 A; A/B=1-655. DR PDB; 7NEZ; EM; 3.39 A; A/B=1-655. DR PDB; 7NFD; EM; 3.51 A; A/B=1-655. DR PDB; 7OJ8; EM; 3.40 A; A/B=2-655. DR PDB; 7OJH; EM; 3.10 A; A/B=2-655. DR PDB; 7OJI; EM; 3.40 A; A/B=2-655. DR PDB; 8BHT; EM; 3.10 A; A/B=2-655. DR PDB; 8BI0; EM; 3.20 A; A/B=2-655. DR PDB; 8P7W; EM; 3.04 A; A/B=1-655. DR PDB; 8P8A; EM; 3.20 A; A/B=1-655. DR PDB; 8P8J; EM; 3.49 A; A/B=1-655. DR PDB; 8U2C; EM; 2.50 A; A/B=1-655. DR PDBsum; 5NJ3; -. DR PDBsum; 5NJG; -. DR PDBsum; 6ETI; -. DR PDBsum; 6FEQ; -. DR PDBsum; 6FFC; -. DR PDBsum; 6HBU; -. DR PDBsum; 6HCO; -. DR PDBsum; 6HIJ; -. DR PDBsum; 6HZM; -. DR PDBsum; 6VXF; -. DR PDBsum; 6VXH; -. DR PDBsum; 6VXI; -. DR PDBsum; 6VXJ; -. DR PDBsum; 7NEQ; -. DR PDBsum; 7NEZ; -. DR PDBsum; 7NFD; -. DR PDBsum; 7OJ8; -. DR PDBsum; 7OJH; -. DR PDBsum; 7OJI; -. DR PDBsum; 8BHT; -. DR PDBsum; 8BI0; -. DR PDBsum; 8P7W; -. DR PDBsum; 8P8A; -. DR PDBsum; 8P8J; -. DR PDBsum; 8U2C; -. DR AlphaFoldDB; Q9UNQ0; -. DR EMDB; EMD-0190; -. DR EMDB; EMD-0196; -. DR EMDB; EMD-12290; -. DR EMDB; EMD-12295; -. DR EMDB; EMD-12300; -. DR EMDB; EMD-12939; -. DR EMDB; EMD-12951; -. DR EMDB; EMD-12952; -. DR EMDB; EMD-17537; -. DR EMDB; EMD-17543; -. DR EMDB; EMD-17547; -. DR EMDB; EMD-21436; -. DR EMDB; EMD-21437; -. DR EMDB; EMD-21438; -. DR EMDB; EMD-21439; -. DR EMDB; EMD-21440; -. DR EMDB; EMD-21441; -. DR EMDB; EMD-2715; -. DR EMDB; EMD-3654; -. DR EMDB; EMD-3953; -. DR EMDB; EMD-41845; -. DR EMDB; EMD-4246; -. DR EMDB; EMD-4256; -. DR SMR; Q9UNQ0; -. DR BioGRID; 114821; 60. DR DIP; DIP-29162N; -. DR IntAct; Q9UNQ0; 21. DR MINT; Q9UNQ0; -. DR STRING; 9606.ENSP00000498246; -. DR BindingDB; Q9UNQ0; -. DR ChEMBL; CHEMBL5393; -. DR DrugBank; DB12001; Abemaciclib. DR DrugBank; DB08916; Afatinib. DR DrugBank; DB11363; Alectinib. DR DrugBank; DB00437; Allopurinol. DR DrugBank; DB12015; Alpelisib. DR DrugBank; DB03496; Alvocidib. DR DrugBank; DB06288; Amisulpride. DR DrugBank; DB11901; Apalutamide. DR DrugBank; DB06605; Apixaban. DR DrugBank; DB09274; Artesunate. DR DrugBank; DB12597; Asciminib. DR DrugBank; DB16098; Atogepant. DR DrugBank; DB06237; Avanafil. DR DrugBank; DB15233; Avapritinib. DR DrugBank; DB11995; Avatrombopag. DR DrugBank; DB16407; Azvudine. DR DrugBank; DB13997; Baloxavir marboxil. DR DrugBank; DB11817; Baricitinib. DR DrugBank; DB00394; Beclomethasone dipropionate. DR DrugBank; DB16703; Belumosudil. DR DrugBank; DB15982; Berotralstat. DR DrugBank; DB04851; Biricodar. DR DrugBank; DB12267; Brigatinib. DR DrugBank; DB12151; Brincidofovir. DR DrugBank; DB00921; Buprenorphine. DR DrugBank; DB06772; Cabazitaxel. DR DrugBank; DB11751; Cabotegravir. DR DrugBank; DB00201; Caffeine. DR DrugBank; DB04690; Camptothecin. DR DrugBank; DB08907; Canagliflozin. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB14737; Cannabinol. DR DrugBank; DB11791; Capmatinib. DR DrugBank; DB00958; Carboplatin. DR DrugBank; DB00482; Celecoxib. DR DrugBank; DB00439; Cerivastatin. DR DrugBank; DB04540; Cholesterol. DR DrugBank; DB00515; Cisplatin. DR DrugBank; DB00242; Cladribine. DR DrugBank; DB00631; Clofarabine. DR DrugBank; DB00845; Clofazimine. DR DrugBank; DB09065; Cobicistat. DR DrugBank; DB05239; Cobimetinib. DR DrugBank; DB00286; Conjugated estrogens. DR DrugBank; DB12483; Copanlisib. DR DrugBank; DB00091; Cyclosporine. DR DrugBank; DB08912; Dabrafenib. DR DrugBank; DB09102; Daclatasvir. DR DrugBank; DB11963; Dacomitinib. DR DrugBank; DB00970; Dactinomycin. DR DrugBank; DB02115; Daidzin. DR DrugBank; DB12941; Darolutamide. DR DrugBank; DB09183; Dasabuvir. DR DrugBank; DB01254; Dasatinib. DR DrugBank; DB00694; Daunorubicin. DR DrugBank; DB11943; Delafloxacin. DR DrugBank; DB16650; Deucravacitinib. DR DrugBank; DB01234; Dexamethasone. DR DrugBank; DB14649; Dexamethasone acetate. DR DrugBank; DB00255; Diethylstilbestrol. DR DrugBank; DB01248; Docetaxel. DR DrugBank; DB08930; Dolutegravir. DR DrugBank; DB00843; Donepezil. DR DrugBank; DB05928; Dovitinib. DR DrugBank; DB00997; Doxorubicin. DR DrugBank; DB00470; Dronabinol. DR DrugBank; DB11952; Duvelisib. DR DrugBank; DB04881; Elacridar. DR DrugBank; DB06210; Eltrombopag. DR DrugBank; DB09038; Empagliflozin. DR DrugBank; DB13874; Enasidenib. DR DrugBank; DB00530; Erlotinib. DR DrugBank; DB11827; Ertugliflozin. DR DrugBank; DB00783; Estradiol. DR DrugBank; DB13952; Estradiol acetate. DR DrugBank; DB13953; Estradiol benzoate. DR DrugBank; DB13954; Estradiol cypionate. DR DrugBank; DB13955; Estradiol dienanthate. DR DrugBank; DB13956; Estradiol valerate. DR DrugBank; DB00655; Estrone. DR DrugBank; DB00773; Etoposide. DR DrugBank; DB00973; Ezetimibe. DR DrugBank; DB04854; Febuxostat. DR DrugBank; DB12500; Fedratinib. DR DrugBank; DB09279; Fimasartan. DR DrugBank; DB00544; Fluorouracil. DR DrugBank; DB00158; Folic acid. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB11796; Fostemsavir. DR DrugBank; DB02703; Fusidic acid. DR DrugBank; DB15149; Futibatinib. DR DrugBank; DB00317; Gefitinib. DR DrugBank; DB01645; Genistein. DR DrugBank; DB12141; Gilteritinib. DR DrugBank; DB11978; Glasdegib. DR DrugBank; DB13879; Glecaprevir. DR DrugBank; DB01016; Glyburide. DR DrugBank; DB01094; Hesperetin. DR DrugBank; DB14538; Hydrocortisone aceponate. DR DrugBank; DB14539; Hydrocortisone acetate. DR DrugBank; DB14540; Hydrocortisone butyrate. DR DrugBank; DB14541; Hydrocortisone cypionate. DR DrugBank; DB14542; Hydrocortisone phosphate. DR DrugBank; DB14543; Hydrocortisone probutate. DR DrugBank; DB14544; Hydrocortisone valerate. DR DrugBank; DB09054; Idelalisib. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB11886; Infigratinib. DR DrugBank; DB00762; Irinotecan. DR DrugBank; DB11633; Isavuconazole. DR DrugBank; DB11757; Istradefylline. DR DrugBank; DB00602; Ivermectin. DR DrugBank; DB00709; Lamivudine. DR DrugBank; DB00448; Lansoprazole. DR DrugBank; DB14723; Larotrectinib. DR DrugBank; DB11732; Lasmiditan. DR DrugBank; DB09027; Ledipasvir. DR DrugBank; DB01097; Leflunomide. DR DrugBank; DB09078; Lenvatinib. DR DrugBank; DB12070; Letermovir. DR DrugBank; DB17083; Linzagolix. DR DrugBank; DB06448; Lonafarnib. DR DrugBank; DB13125; Lusutrombopag. DR DrugBank; DB06234; Maribavir. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB00563; Methotrexate. DR DrugBank; DB01204; Mitoxantrone. DR DrugBank; DB16390; Mobocertinib. DR DrugBank; DB00688; Mycophenolate mofetil. DR DrugBank; DB14011; Nabiximols. DR DrugBank; DB03467; Naringenin. DR DrugBank; DB00220; Nelfinavir. DR DrugBank; DB11820; Nifurtimox. DR DrugBank; DB04868; Nilotinib. DR DrugBank; DB09079; Nintedanib. DR DrugBank; DB11793; Niraparib. DR DrugBank; DB00698; Nitrofurantoin. DR DrugBank; DB01051; Novobiocin. DR DrugBank; DB09074; Olaparib. DR DrugBank; DB16267; Olutasidenib. DR DrugBank; DB09296; Ombitasvir. DR DrugBank; DB00338; Omeprazole. DR DrugBank; DB11632; Opicapone. DR DrugBank; DB09330; Osimertinib. DR DrugBank; DB13055; Oteseconazole. DR DrugBank; DB00526; Oxaliplatin. DR DrugBank; DB12612; Ozanimod. DR DrugBank; DB11697; Pacritinib. DR DrugBank; DB09073; Palbociclib. DR DrugBank; DB00213; Pantoprazole. DR DrugBank; DB09297; Paritaprevir. DR DrugBank; DB06589; Pazopanib. DR DrugBank; DB00642; Pemetrexed. DR DrugBank; DB15102; Pemigatinib. DR DrugBank; DB13878; Pibrentasvir. DR DrugBank; DB08860; Pitavastatin. DR DrugBank; DB08901; Ponatinib. DR DrugBank; DB06813; Pralatrexate. DR DrugBank; DB15822; Pralsetinib. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB00175; Pravastatin. DR DrugBank; DB00457; Prazosin. DR DrugBank; DB00396; Progesterone. DR DrugBank; DB04216; Quercetin. DR DrugBank; DB01129; Rabeprazole. DR DrugBank; DB00481; Raloxifene. DR DrugBank; DB08896; Regorafenib. DR DrugBank; DB11853; Relugolix. DR DrugBank; DB11855; Revefenacin. DR DrugBank; DB08864; Rilpivirine. DR DrugBank; DB00740; Riluzole. DR DrugBank; DB12457; Rimegepant. DR DrugBank; DB08931; Riociguat. DR DrugBank; DB14840; Ripretinib. DR DrugBank; DB15305; Risdiplam. DR DrugBank; DB00503; Ritonavir. DR DrugBank; DB06228; Rivaroxaban. DR DrugBank; DB09291; Rolapitant. DR DrugBank; DB01098; Rosuvastatin. DR DrugBank; DB04847; Roxadustat. DR DrugBank; DB12332; Rucaparib. DR DrugBank; DB06654; Safinamide. DR DrugBank; DB01232; Saquinavir. DR DrugBank; DB15685; Selpercatinib. DR DrugBank; DB11689; Selumetinib. DR DrugBank; DB06290; Simeprevir. DR DrugBank; DB08934; Sofosbuvir. DR DrugBank; DB00398; Sorafenib. DR DrugBank; DB12713; Sotagliflozin. DR DrugBank; DB15569; Sotorasib. DR DrugBank; DB09118; Stiripentol. DR DrugBank; DB00795; Sulfasalazine. DR DrugBank; DB00391; Sulpiride. DR DrugBank; DB00669; Sumatriptan. DR DrugBank; DB01268; Sunitinib. DR DrugBank; DB11644; Tafamidis. DR DrugBank; DB11760; Talazoparib. DR DrugBank; DB00675; Tamoxifen. DR DrugBank; DB04348; Taurocholic acid. DR DrugBank; DB12887; Tazemetostat. DR DrugBank; DB12020; Tecovirimat. DR DrugBank; DB01079; Tegaserod. DR DrugBank; DB00966; Telmisartan. DR DrugBank; DB12095; Telotristat ethyl. DR DrugBank; DB00853; Temozolomide. DR DrugBank; DB00444; Teniposide. DR DrugBank; DB09299; Tenofovir alafenamide. DR DrugBank; DB15133; Tepotinib. DR DrugBank; DB08880; Teriflunomide. DR DrugBank; DB00624; Testosterone. DR DrugBank; DB13943; Testosterone cypionate. DR DrugBank; DB13944; Testosterone enanthate. DR DrugBank; DB13946; Testosterone undecanoate. DR DrugBank; DB11712; Tezacaftor. DR DrugBank; DB11800; Tivozanib. DR DrugBank; DB01685; Topiroxostat. DR DrugBank; DB01030; Topotecan. DR DrugBank; DB14962; Trastuzumab deruxtecan. DR DrugBank; DB15442; Trilaciclib. DR DrugBank; DB11652; Tucatinib. DR DrugBank; DB15328; Ubrogepant. DR DrugBank; DB15091; Upadacitinib. DR DrugBank; DB05294; Vandetanib. DR DrugBank; DB11613; Velpatasvir. DR DrugBank; DB08881; Vemurafenib. DR DrugBank; DB11581; Venetoclax. DR DrugBank; DB00285; Venlafaxine. DR DrugBank; DB15456; Vericiguat. DR DrugBank; DB00541; Vincristine. DR DrugBank; DB08828; Vismodegib. DR DrugBank; DB12026; Voxilaprevir. DR DrugBank; DB00549; Zafirlukast. DR DrugBank; DB00495; Zidovudine. DR DrugCentral; Q9UNQ0; -. DR GuidetoPHARMACOLOGY; 792; -. DR TCDB; 3.A.1.204.2; the atp-binding cassette (abc) superfamily. DR GlyCosmos; Q9UNQ0; 1 site, No reported glycans. DR GlyGen; Q9UNQ0; 1 site. DR iPTMnet; Q9UNQ0; -. DR PhosphoSitePlus; Q9UNQ0; -. DR SwissPalm; Q9UNQ0; -. DR BioMuta; ABCG2; -. DR DMDM; 67462103; -. DR EPD; Q9UNQ0; -. DR jPOST; Q9UNQ0; -. DR MassIVE; Q9UNQ0; -. DR MaxQB; Q9UNQ0; -. DR PaxDb; 9606-ENSP00000237612; -. DR PeptideAtlas; Q9UNQ0; -. DR ProteomicsDB; 85323; -. [Q9UNQ0-1] DR ProteomicsDB; 85324; -. [Q9UNQ0-2] DR ABCD; Q9UNQ0; 1 sequenced antibody. DR Antibodypedia; 14577; 453 antibodies from 45 providers. DR DNASU; 9429; -. DR Ensembl; ENST00000237612.8; ENSP00000237612.3; ENSG00000118777.12. [Q9UNQ0-1] DR Ensembl; ENST00000515655.5; ENSP00000426917.1; ENSG00000118777.12. [Q9UNQ0-2] DR Ensembl; ENST00000650821.1; ENSP00000498246.1; ENSG00000118777.12. [Q9UNQ0-1] DR GeneID; 9429; -. DR KEGG; hsa:9429; -. DR MANE-Select; ENST00000237612.8; ENSP00000237612.3; NM_004827.3; NP_004818.2. DR UCSC; uc003hrg.4; human. [Q9UNQ0-1] DR AGR; HGNC:74; -. DR CTD; 9429; -. DR DisGeNET; 9429; -. DR GeneCards; ABCG2; -. DR HGNC; HGNC:74; ABCG2. DR HPA; ENSG00000118777; Tissue enhanced (intestine). DR MalaCards; ABCG2; -. DR MIM; 138900; phenotype. DR MIM; 603756; gene. DR MIM; 614490; phenotype. DR neXtProt; NX_Q9UNQ0; -. DR OpenTargets; ENSG00000118777; -. DR PharmGKB; PA390; -. DR VEuPathDB; HostDB:ENSG00000118777; -. DR eggNOG; KOG0061; Eukaryota. DR GeneTree; ENSGT00940000162658; -. DR HOGENOM; CLU_000604_57_8_1; -. DR InParanoid; Q9UNQ0; -. DR OMA; FWYYTFY; -. DR OrthoDB; 936137at2759; -. DR PhylomeDB; Q9UNQ0; -. DR TreeFam; TF105211; -. DR BRENDA; 7.6.2.2; 2681. DR BRENDA; 7.6.2.3; 2681. DR PathwayCommons; Q9UNQ0; -. DR Reactome; R-HSA-189451; Heme biosynthesis. DR Reactome; R-HSA-189483; Heme degradation. DR Reactome; R-HSA-2161517; Abacavir transmembrane transport. DR Reactome; R-HSA-917937; Iron uptake and transport. DR Reactome; R-HSA-9753281; Paracetamol ADME. DR Reactome; R-HSA-9793528; Ciprofloxacin ADME. DR Reactome; R-HSA-9818032; NFE2L2 regulating MDR associated enzymes. DR SABIO-RK; Q9UNQ0; -. DR SignaLink; Q9UNQ0; -. DR SIGNOR; Q9UNQ0; -. DR BioGRID-ORCS; 9429; 12 hits in 1152 CRISPR screens. DR ChiTaRS; ABCG2; human. DR GeneWiki; ABCG2; -. DR GenomeRNAi; 9429; -. DR Pharos; Q9UNQ0; Tchem. DR PRO; PR:Q9UNQ0; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q9UNQ0; Protein. DR Bgee; ENSG00000118777; Expressed in jejunal mucosa and 162 other cell types or tissues. DR ExpressionAtlas; Q9UNQ0; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB. DR GO; GO:0098591; C:external side of apical plasma membrane; ISS:ARUK-UCL. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0015225; F:biotin transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISS:ARUK-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015143; F:urate transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISS:ARUK-UCL. DR GO; GO:0015878; P:biotin transport; ISS:UniProtKB. DR GO; GO:1990748; P:cellular detoxification; IDA:GO_Central. DR GO; GO:0140115; P:export across plasma membrane; ISS:ARUK-UCL. DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW. DR GO; GO:0015711; P:organic anion transport; ISS:ARUK-UCL. DR GO; GO:0097744; P:renal urate salt excretion; IMP:UniProtKB. DR GO; GO:0032218; P:riboflavin transport; IDA:UniProtKB. DR GO; GO:0070633; P:transepithelial transport; IDA:ARUK-UCL. DR GO; GO:0055085; P:transmembrane transport; IMP:UniProtKB. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0046415; P:urate metabolic process; IMP:UniProtKB. DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; IDA:ARUK-UCL. 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; IPR043926; ABCG_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1. DR PANTHER; PTHR48041:SF92; BROAD SUBSTRATE SPECIFICITY ATP-BINDING CASSETTE TRANSPORTER ABCG2; 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; PS50893; ABC_TRANSPORTER_2; 1. DR Genevisible; Q9UNQ0; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Disulfide bond; Glycoprotein; Lipid transport; Membrane; Mitochondrion; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..655 FT /note="Broad substrate specificity ATP-binding cassette FT transporter ABCG2" FT /id="PRO_0000093386" FT TOPO_DOM 1..395 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 396..416 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 417..428 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 429..449 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 450..477 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 478..498 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 499..506 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 507..527 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 528..535 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 536..556 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 557..630 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 631..651 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 652..655 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 37..286 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 389..651 FT /note="ABC transmembrane type-2" FT BINDING 80..87 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434, FT ECO:0000269|PubMed:30405239, ECO:0007744|PDB:6HBU, FT ECO:0007744|PDB:6HZM" FT BINDING 184..190 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:30405239, FT ECO:0007744|PDB:6HBU, ECO:0007744|PDB:6HZM" FT BINDING 211 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:30405239, FT ECO:0007744|PDB:6HBU, ECO:0007744|PDB:6HZM" FT BINDING 243 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:30405239, FT ECO:0007744|PDB:6HBU, ECO:0007744|PDB:6HZM" FT SITE 418 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:15807535" FT SITE 557 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:15807535" FT MOD_RES 362 FT /note="Phosphothreonine; by PIM1" FT /evidence="ECO:0000269|PubMed:18056989" FT CARBOHYD 596 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:15807535, FT ECO:0000269|PubMed:28554189, ECO:0007744|PDB:5NJ3, FT ECO:0007744|PDB:5NJG" FT DISULFID 592..608 FT /evidence="ECO:0000269|PubMed:17686774, FT ECO:0000269|PubMed:28554189, ECO:0007744|PDB:5NJ3, FT ECO:0007744|PDB:5NJG" FT DISULFID 603 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:17686774, FT ECO:0000269|PubMed:28554189, ECO:0007744|PDB:5NJ3, FT ECO:0007744|PDB:5NJG" FT VAR_SEQ 550..611 FT /note="IFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQNFCPGLNATGNN FT PCNYATCTGE -> VCWSISQPLHLGCHGFSTSAFHDMDLRLCSIMNFWDKTSAQDSMQ FT QETILVTMQHVLAKNIW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014232" FT VAR_SEQ 612..655 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014233" FT VARIANT 12 FT /note="V -> M (found in Jr(a-) blood group phenotype; FT dbSNP:rs2231137)" FT /evidence="ECO:0000269|PubMed:12111378, FT ECO:0000269|PubMed:12544509, ECO:0000269|PubMed:15838659, FT ECO:0000269|PubMed:16702730, ECO:0000269|PubMed:22246507, FT ECO:0000269|Ref.11" FT /id="VAR_020779" FT VARIANT 13 FT /note="S -> L (in dbSNP:rs1319203095)" FT /evidence="ECO:0000269|PubMed:16702730" FT /id="VAR_067363" FT VARIANT 141 FT /note="Q -> K (associated with high serum levels of uric FT acid and increased risk of gout; results in lower urate FT transport rates compared to wild-type; decreased protein FT abundance; dbSNP:rs2231142)" FT /evidence="ECO:0000269|PubMed:12111378, FT ECO:0000269|PubMed:12544509, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15838659, ECO:0000269|PubMed:16702730, FT ECO:0000269|PubMed:19506252, ECO:0000269|PubMed:31003562, FT ECO:0000269|PubMed:31254042, ECO:0000269|Ref.11, FT ECO:0000269|Ref.8" FT /id="VAR_020780" FT VARIANT 147 FT /note="R -> W (loss of protein expression; loss of FT localization to the plasma membrane; dbSNP:rs372192400)" FT /evidence="ECO:0000269|PubMed:31003562, FT ECO:0000269|PubMed:31254042" FT /id="VAR_082302" FT VARIANT 153 FT /note="T -> M (decreased protein abundance; no effect on FT localization to the plasma membrane; no effect on substrate FT transmembrane transport; decreased ATPase activity; no FT effect on ATPase-coupled transmembrane transporter FT activity; dbSNP:rs753759474)" FT /evidence="ECO:0000269|PubMed:31003562, FT ECO:0000269|PubMed:31254042" FT /id="VAR_082303" FT VARIANT 160 FT /note="R -> Q (in dbSNP:rs528655917)" FT /evidence="ECO:0000269|PubMed:16702730" FT /id="VAR_067364" FT VARIANT 166 FT /note="Q -> E (in dbSNP:rs1061017)" FT /evidence="ECO:0000269|PubMed:12958161, FT ECO:0000269|PubMed:9850061" FT /id="VAR_022704" FT VARIANT 206 FT /note="I -> L (in dbSNP:rs12721643)" FT /evidence="ECO:0000269|PubMed:12544509" FT /id="VAR_022705" FT VARIANT 208 FT /note="F -> S (in dbSNP:rs1061018)" FT /evidence="ECO:0000269|PubMed:12958161, FT ECO:0000269|PubMed:9850061" FT /id="VAR_022706" FT VARIANT 248 FT /note="S -> P (in dbSNP:rs3116448)" FT /id="VAR_022707" FT VARIANT 296 FT /note="D -> H (in dbSNP:rs41282401)" FT /evidence="ECO:0000269|Ref.11" FT /id="VAR_030357" FT VARIANT 316 FT /note="T -> P" FT /evidence="ECO:0000269|Ref.9" FT /id="VAR_022443" FT VARIANT 354 FT /note="G -> R (in dbSNP:rs138606116)" FT /evidence="ECO:0000269|PubMed:16702730" FT /id="VAR_067365" FT VARIANT 360 FT /note="Missing (no effect on protein abundance; no effect FT on localization to the plasma membrane; no effect on ATPase FT activity; no effect on substrate transmembrane transport)" FT /evidence="ECO:0000269|PubMed:31003562, FT ECO:0000269|PubMed:31254042" FT /id="VAR_082304" FT VARIANT 373 FT /note="F -> C (decreased protein abundance; decreased FT localization to the plasma membrane; no effect on FT ATPase-coupled transmembrane transporter activity; FT dbSNP:rs752626614)" FT /evidence="ECO:0000269|PubMed:31003562, FT ECO:0000269|PubMed:31254042" FT /id="VAR_082305" FT VARIANT 421 FT /note="T -> A (no effect on protein abundance; no effect on FT substrate transmembrane transport; dbSNP:rs199854112)" FT /evidence="ECO:0000269|PubMed:31003562" FT /id="VAR_082306" FT VARIANT 431 FT /note="F -> L" FT /evidence="ECO:0000269|PubMed:15618737, FT ECO:0000269|PubMed:16702730" FT /id="VAR_018349" FT VARIANT 434 FT /note="T -> M (no effect on protein abundance; no effect on FT localization to the plasma membrane; increased ATPase FT activity; decreased ATPase-coupled transmembrane FT transporter activity; dbSNP:rs769734146)" FT /evidence="ECO:0000269|PubMed:31003562, FT ECO:0000269|PubMed:31254042" FT /id="VAR_082307" FT VARIANT 441 FT /note="S -> N (in dbSNP:rs1354553769)" FT /evidence="ECO:0000269|PubMed:16702730" FT /id="VAR_067366" FT VARIANT 476 FT /note="S -> P (no effect on protein abundance; no effect on FT localization to the plasma membrane; no effect on ATPase FT activity; decreased ATPase-coupled transmembrane FT transporter activity; dbSNP:rs1274428653)" FT /evidence="ECO:0000269|PubMed:31003562, FT ECO:0000269|PubMed:31254042" FT /id="VAR_082308" FT VARIANT 489 FT /note="F -> L (in dbSNP:rs192169063)" FT /evidence="ECO:0000269|PubMed:15618737, FT ECO:0000269|PubMed:16702730" FT /id="VAR_018350" FT VARIANT 528 FT /note="A -> T (in dbSNP:rs45605536)" FT /evidence="ECO:0000269|Ref.11" FT /id="VAR_030358" FT VARIANT 571 FT /note="F -> I (in dbSNP:rs9282571)" FT /id="VAR_022708" FT VARIANT 572 FT /note="S -> R (decreased protein abundance; loss of FT localization to the plasma membrane; dbSNP:rs200894058)" FT /evidence="ECO:0000269|PubMed:31003562" FT /id="VAR_082309" FT VARIANT 590 FT /note="N -> Y (in dbSNP:rs34264773)" FT /evidence="ECO:0000269|PubMed:12544509" FT /id="VAR_035355" FT VARIANT 620 FT /note="D -> N (no effect on protein abundance; no effect on FT substrate transmembrane transport; dbSNP:rs34783571)" FT /evidence="ECO:0000269|PubMed:15838659, FT ECO:0000269|PubMed:31003562" FT /id="VAR_022709" FT MUTAGEN 71 FT /note="M->V: Decreased protein abundance. No effect on FT substrate transmembrane transport." FT /evidence="ECO:0000269|PubMed:31254042" FT MUTAGEN 86 FT /note="K->M: Decreased protein abundance. Decreased FT localization to the plasma membrane and retained FT intracellularly. Loss of ATPase-coupled transmembrane FT transporter activity." FT /evidence="ECO:0000269|PubMed:15769853, FT ECO:0000269|PubMed:31254042" FT MUTAGEN 211 FT /note="E->Q: Decreased estrone-3 sulfate ATPase-coupled FT transmembrane transporter activity. Decreased FT substrate-induced ATP hydrolysis. Decreased substrate FT transport." FT /evidence="ECO:0000269|PubMed:28554189, FT ECO:0000269|PubMed:30405239" FT MUTAGEN 362 FT /note="T->A: Loss of phosphorylation by PIM1. Decreased FT localization to the plasma membrane. Decreased FT homooligomerization. Loss of function in resistance to drug FT treatment." FT /evidence="ECO:0000269|PubMed:18056989" FT MUTAGEN 362 FT /note="T->D: Loss of phosphorylation by PIM1. Constitutive FT drug resistance independent of PIM1." FT /evidence="ECO:0000269|PubMed:18056989" FT MUTAGEN 383 FT /note="R->C: Loss of protein expression." FT /evidence="ECO:0000269|PubMed:31254042" FT MUTAGEN 418 FT /note="N->Q: No effect." FT /evidence="ECO:0000269|PubMed:15807535" FT MUTAGEN 435 FT /note="T->A: No effect on stability. Increased estrone-3 FT sulfate ATPase-coupled transmembrane transporter activity. FT Increased substrate-induced ATP hydrolysis. Increased FT substrate transport." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 435 FT /note="T->F: No effect on stability. Decreased estrone-3 FT sulfate ATPase-coupled transmembrane transporter activity. FT Decreased substrate-induced ATP hydrolysis. Decreased FT substrate transport." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 436 FT /note="N->A: No effect on stability. Decreased estrone-3 FT sulfate ATPase-coupled transmembrane transporter activity. FT Decreased substrate-induced ATP hydrolysis. Decreased FT substrate transport." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 439 FT /note="F->A: No effect on stability. Decreased estrone-3 FT sulfate ATPase-coupled transmembrane transporter activity. FT Decreased substrate-induced ATP hydrolysis. Decreased FT substrate transport." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 482 FT /note="R->D: Decreases ATPase activity." FT /evidence="ECO:0000269|PubMed:15670731" FT MUTAGEN 482 FT /note="R->G,N,S,T: Increases ATPase activity." FT /evidence="ECO:0000269|PubMed:15670731" FT MUTAGEN 482 FT /note="R->K,I,M,Y: No change in ATPase activity." FT /evidence="ECO:0000269|PubMed:15670731" FT MUTAGEN 482 FT /note="R->T,Y: Decreases transport activity." FT /evidence="ECO:0000269|PubMed:15670731" FT MUTAGEN 546 FT /note="V->A: No effect on stability. No effect on estrone-3 FT sulfate ATPase-coupled transmembrane transporter activity. FT No effect on substrate-induced ATP hydrolysis. No effect on FT substrate transport." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 546 FT /note="V->F: No effect on stability. Decreased estrone-3 FT sulfate ATPase-coupled transmembrane transporter activity. FT Increased basal and substrate-induced ATP hydrolysis. FT Decreased substrate transport." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 549 FT /note="M->A: No effect on stability. No effect on estrone-3 FT sulfate ATPase-coupled transmembrane transporter activity. FT No effect on substrate-induced ATP hydrolysis. No effect on FT substrate transport." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 554 FT /note="L->A: No effect on stability. Increased estrone-3 FT sulfate ATPase-coupled transmembrane transporter activity. FT Increased basal and substrate-induced ATP hydrolysis. FT Increased substrate transport." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 555 FT /note="L->A: Loss of protein expression." FT /evidence="ECO:0000269|PubMed:30405239" FT MUTAGEN 557 FT /note="N->Q: No effect." FT /evidence="ECO:0000269|PubMed:15807535" FT MUTAGEN 583 FT /note="H->A: Strongly reduced binding to hemin but not to FT PPIX." FT /evidence="ECO:0000269|PubMed:20705604" FT MUTAGEN 596 FT /note="N->Q: Loss of glycosylation." FT /evidence="ECO:0000269|PubMed:15807535" FT MUTAGEN 603 FT /note="C->A: Strongly reduced binding to hemin but not to FT PPIX." FT /evidence="ECO:0000269|PubMed:20705604" FT MUTAGEN 605 FT /note="Y->A: No effect on hemin binding." FT /evidence="ECO:0000269|PubMed:20705604" FT CONFLICT 24 FT /note="A -> V (in Ref. 1; AAD09188 and 7; AAP44087)" FT /evidence="ECO:0000305" FT CONFLICT 315..316 FT /note="Missing (in Ref. 10; BAA92050)" FT /evidence="ECO:0000305" FT CONFLICT 390 FT /note="G -> V (in Ref. 13; AAH92408)" FT /evidence="ECO:0000305" FT CONFLICT 482 FT /note="R -> G (in Ref. 14; AF093771/AF093772)" FT /evidence="ECO:0000305" FT CONFLICT 482 FT /note="R -> T (in Ref. 2; AAC97367)" FT /evidence="ECO:0000305" FT CONFLICT 484..485 FT /note="LP -> FT (in Ref. 14; AF093772)" FT /evidence="ECO:0000305" FT CONFLICT 501 FT /note="P -> A (in Ref. 6; AAG52982)" FT /evidence="ECO:0000305" FT STRAND 37..45 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 62..71 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 73..79 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 82..85 FT /evidence="ECO:0007829|PDB:7NEQ" FT HELIX 86..93 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 99..101 FT /evidence="ECO:0007829|PDB:6ETI" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 115..120 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 132..135 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 136..147 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 154..168 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 172..175 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 188..198 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 199..202 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 205..210 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:6HBU" FT HELIX 220..233 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 247..250 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 254..260 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 273..278 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 279..281 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:7NEQ" FT HELIX 290..299 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 303..307 FT /evidence="ECO:0007829|PDB:6HBU" FT HELIX 329..337 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 340..351 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 373..390 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 392..394 FT /evidence="ECO:0007829|PDB:6ETI" FT HELIX 395..412 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 413..415 FT /evidence="ECO:0007829|PDB:7OJH" FT STRAND 418..421 FT /evidence="ECO:0007829|PDB:6VXF" FT HELIX 422..439 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 440..446 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 452..461 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 466..475 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 476..478 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 479..493 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 494..497 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 503..527 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 528..530 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 537..550 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 552..556 FT /evidence="ECO:0007829|PDB:8P7W" FT TURN 558..560 FT /evidence="ECO:0007829|PDB:6HBU" FT TURN 563..565 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 566..571 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 573..585 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 586..588 FT /evidence="ECO:0007829|PDB:6HBU" FT TURN 597..599 FT /evidence="ECO:0007829|PDB:8P7W" FT STRAND 602..605 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 610..616 FT /evidence="ECO:0007829|PDB:8P7W" FT HELIX 624..649 FT /evidence="ECO:0007829|PDB:8P7W" SQ SEQUENCE 655 AA; 72314 MW; A8AF66B96034C5A8 CRC64; MSSSNVEVFI PVSQGNTNGF PATASNDLKA FTEGAVLSFH NICYRVKLKS GFLPCRKPVE KEILSNINGI MKPGLNAILG PTGGGKSSLL DVLAARKDPS GLSGDVLING APRPANFKCN SGYVVQDDVV MGTLTVRENL QFSAALRLAT TMTNHEKNER INRVIQELGL DKVADSKVGT QFIRGVSGGE RKRTSIGMEL ITDPSILFLD EPTTGLDSST ANAVLLLLKR MSKQGRTIIF SIHQPRYSIF KLFDSLTLLA SGRLMFHGPA QEALGYFESA GYHCEAYNNP ADFFLDIING DSTAVALNRE EDFKATEIIE PSKQDKPLIE KLAEIYVNSS FYKETKAELH QLSGGEKKKK ITVFKEISYT TSFCHQLRWV SKRSFKNLLG NPQASIAQII VTVVLGLVIG AIYFGLKNDS TGIQNRAGVL FFLTTNQCFS SVSAVELFVV EKKLFIHEYI SGYYRVSSYF LGKLLSDLLP MRMLPSIIFT CIVYFMLGLK PKADAFFVMM FTLMMVAYSA SSMALAIAAG QSVVSVATLL MTICFVFMMI FSGLLVNLTT IASWLSWLQY FSIPRYGFTA LQHNEFLGQN FCPGLNATGN NPCNYATCTG EEYLVKQGID LSPWGLWKNH VALACMIVIF LTIAYLKLLF LKKYS //