ID   MRP1_HUMAN              Reviewed;        1531 AA.
AC   P33527; A3RJX2; C9JPJ4; O14819; O43333; P78419; Q59GI9; Q9UQ97; Q9UQ99;
AC   Q9UQA0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 3.
DT   08-NOV-2023, entry version 225.
DE   RecName: Full=Multidrug resistance-associated protein 1 {ECO:0000305};
DE            EC=7.6.2.2 {ECO:0000269|PubMed:9281595};
DE   AltName: Full=ATP-binding cassette sub-family C member 1;
DE   AltName: Full=Glutathione-S-conjugate-translocating ATPase ABCC1 {ECO:0000250|UniProtKB:O35379};
DE            EC=7.6.2.3 {ECO:0000250|UniProtKB:O35379};
DE   AltName: Full=Leukotriene C(4) transporter;
DE            Short=LTC4 transporter;
GN   Name=ABCC1 {ECO:0000312|HGNC:HGNC:51}; Synonyms=MRP, MRP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-117.
RX   PubMed=1360704; DOI=10.1126/science.1360704;
RA   Cole S.P.C., Bhardwaj G., Gerlach J.H., Mackie J.E., Grant C.E.,
RA   Almquist K.C., Stewart A.J., Kurz E.U., Duncan A.M.V., Deeley R.G.;
RT   "Overexpression of a transporter gene in a multidrug-resistant human lung
RT   cancer cell line.";
RL   Science 258:1650-1654(1992).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=8098549; DOI=10.1126/science.8098549;
RA   Cole S.P.C., Deeley R.G.;
RT   "Multidrug resistance-associated protein: sequence correction.";
RL   Science 260:879-879(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANT
RP   THR-117.
RX   PubMed=9344662; DOI=10.1006/geno.1997.4950;
RA   Grant C.E., Kurz E.U., Cole S.P.C., Deeley R.G.;
RT   "Analysis of the intron-exon organization of the human multidrug-resistance
RT   protein gene (MRP) and alternative splicing of its mRNA.";
RL   Genomics 45:368-378(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-671; GLN-723; THR-861;
RP   SER-1047 AND ILE-1146.
RG   NIEHS SNPs program;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-1531 (ISOFORM 9).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 516-1531.
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [8]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   FUNCTION.
RX   PubMed=7961706; DOI=10.1016/s0021-9258(18)46856-1;
RA   Leier I., Jedlitschky G., Buchholz U., Cole S.P., Deeley R.G., Keppler D.;
RT   "The MRP gene encodes an ATP-dependent export pump for leukotriene C4 and
RT   structurally related conjugates.";
RL   J. Biol. Chem. 269:27807-27810(1994).
RN   [9]
RP   TOPOLOGY, AND GLYCOSYLATION AT ASN-19; ASN-23 AND ASN-1006.
RX   PubMed=9295302; DOI=10.1074/jbc.272.38.23623;
RA   Hipfner D.R., Almquist K.C., Leslie E.M., Gerlach J.H., Grant C.E.,
RA   Deeley R.G., Cole S.P.C.;
RT   "Membrane topology of the multidrug resistance protein (MRP). A study of
RT   glycosylation-site mutants reveals an extracytosolic NH2 terminus.";
RL   J. Biol. Chem. 272:23623-23630(1997).
RN   [10]
RP   TOPOLOGY.
RX   PubMed=9334225; DOI=10.1074/jbc.272.42.26479;
RA   Kast C., Gros P.;
RT   "Topology mapping of the amino-terminal half of multidrug resistance-
RT   associated protein by epitope insertion and immunofluorescence.";
RL   J. Biol. Chem. 272:26479-26487(1997).
RN   [11]
RP   CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9281595; DOI=10.1124/mol.52.3.344;
RA   Stride B.D., Grant C.E., Loe D.W., Hipfner D.R., Cole S.P.C., Deeley R.G.;
RT   "Pharmacological characterization of the murine and human orthologs of
RT   multidrug-resistance protein in transfected human embryonic kidney cells.";
RL   Mol. Pharmacol. 52:344-353(1997).
RN   [12]
RP   TOPOLOGY.
RX   PubMed=9485377; DOI=10.1021/bi972332v;
RA   Kast C., Gros P.;
RT   "Epitope insertion favors a six transmembrane domain model for the carboxy-
RT   terminal portion of the multidrug resistance-associated protein.";
RL   Biochemistry 37:2305-2313(1998).
RN   [13]
RP   FUNCTION.
RX   PubMed=10064732;
RA   Sjoelinder M., Tornhamre S., Claesson H.-E., Hydman J., Lindgren J.A.;
RT   "Characterization of a leukotriene C4 export mechanism in human platelets:
RT   possible involvement of multidrug resistance-associated protein 1.";
RL   J. Lipid Res. 40:439-446(1999).
RN   [14]
RP   FUNCTION.
RX   PubMed=11114332; DOI=10.1016/s0092-8674(00)00179-3;
RA   Robbiani D.F., Finch R.A., Jaeger D., Muller W.A., Sartorelli A.C.,
RA   Randolph G.J.;
RT   "The leukotriene C(4) transporter MRP1 regulates CCL19 (MIP-3beta, ELC)-
RT   dependent mobilization of dendritic cells to lymph nodes.";
RL   Cell 103:757-768(2000).
RN   [15]
RP   MUTAGENESIS OF ASP-792; ASP-793; LYS-1333 AND 1454-ASP-GLU-1455.
RX   PubMed=11469806; DOI=10.1006/abbi.2001.2441;
RA   Cui L., Hou Y.-X., Riordan J.R., Chang X.-B.;
RT   "Mutations of the Walker B motif in the first nucleotide binding domain of
RT   multidrug resistance protein MRP1 prevent conformational maturation.";
RL   Arch. Biochem. Biophys. 392:153-161(2001).
RN   [16]
RP   MUTAGENESIS OF TRP-1246.
RX   PubMed=11278867; DOI=10.1074/jbc.m011246200;
RA   Ito K., Olsen S.L., Qiu W., Deeley R.G., Cole S.P.C.;
RT   "Mutation of a single conserved tryptophan in multidrug resistance protein
RT   1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of
RT   organic anion transport.";
RL   J. Biol. Chem. 276:15616-15624(2001).
RN   [17]
RP   MUTAGENESIS OF GLU-1089.
RX   PubMed=11278596; DOI=10.1074/jbc.m010008200;
RA   Zhang D.-W., Cole S.P.C., Deeley R.G.;
RT   "Identification of an amino acid residue in multidrug resistance protein 1
RT   critical for conferring resistance to anthracyclines.";
RL   J. Biol. Chem. 276:13231-13239(2001).
RN   [18]
RP   MUTAGENESIS OF ARG-1046; ASP-1084 AND ARG-1131.
RX   PubMed=15208328; DOI=10.1074/jbc.m403832200;
RA   Situ D., Haimeur A., Conseil G., Sparks K.E., Zhang D.-W., Deeley R.G.,
RA   Cole S.P.C.;
RT   "Mutational analysis of ionizable residues proximal to the cytoplasmic
RT   interface of membrane spanning domain 3 of the multidrug resistance
RT   protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression
RT   and catalytic activity of the transporter.";
RL   J. Biol. Chem. 279:38871-38880(2004).
RN   [19]
RP   MUTAGENESIS OF GLN-580; THR-581; SER-585; ASN-597; SER-604 AND SER-605.
RX   PubMed=15260484; DOI=10.1021/bi0495230;
RA   Zhang D.-W., Nunoya K., Vasa M., Gu H.-M., Theis A., Cole S.P.C.,
RA   Deeley R.G.;
RT   "Transmembrane helix 11 of multidrug resistance protein 1 (MRP1/ABCC1):
RT   identification of polar amino acids important for substrate specificity and
RT   binding of ATP at nucleotide binding domain 1.";
RL   Biochemistry 43:9413-9425(2004).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [21]
RP   FUNCTION, MUTAGENESIS OF ARG-1138; LYS-1141 AND ARG-1142, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16230346; DOI=10.1074/jbc.m510143200;
RA   Conseil G., Deeley R.G., Cole S.P.;
RT   "Functional importance of three basic residues clustered at the cytosolic
RT   interface of transmembrane helix 15 in the multidrug and organic anion
RT   transporter MRP1 (ABCC1).";
RL   J. Biol. Chem. 281:43-50(2006).
RN   [22]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=17050692; DOI=10.1073/pnas.0603734103;
RA   Mitra P., Oskeritzian C.A., Payne S.G., Beaven M.A., Milstien S.,
RA   Spiegel S.;
RT   "Role of ABCC1 in export of sphingosine-1-phosphate from mast cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:16394-16399(2006).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [26]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-905 AND SER-930, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [27]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [29]
RP   INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL138 (MICROBIAL INFECTION).
RX   PubMed=23580527; DOI=10.1126/science.1235047;
RA   Weekes M.P., Tan S.Y., Poole E., Talbot S., Antrobus R., Smith D.L.,
RA   Montag C., Gygi S.P., Sinclair J.H., Lehner P.J.;
RT   "Latency-associated degradation of the MRP1 drug transporter during latent
RT   human cytomegalovirus infection.";
RL   Science 340:199-202(2013).
RN   [30]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [31]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [32]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND MUTAGENESIS OF LYS-1333.
RX   PubMed=36070769; DOI=10.1016/j.immuni.2022.08.006;
RA   Maltbaek J.H., Cambier S., Snyder J.M., Stetson D.B.;
RT   "ABCC1 transporter exports the immunostimulatory cyclic dinucleotide
RT   cGAMP.";
RL   Immunity 55:1799-1812(2022).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 642-871 IN COMPLEX WITH MG-ATP.
RX   PubMed=16697012; DOI=10.1016/j.jmb.2006.04.005;
RA   Ramaen O., Leulliot N., Sizun C., Ulryck N., Pamlard O., Lallemand J.-Y.,
RA   Tilbeurgh H., Jacquet E.;
RT   "Structure of the human multidrug resistance protein 1 nucleotide binding
RT   domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site.";
RL   J. Mol. Biol. 359:940-949(2006).
RN   [34]
RP   VARIANTS GLN-633 AND VAL-671.
RX   PubMed=10835642; DOI=10.1038/76102;
RA   Le Saux O., Urban Z., Tschuch C., Csiszar K., Bacchelli B., Quaglino D.,
RA   Pasquali-Ronchetti I., Pope F.M., Richards A., Terry S., Bercovitch L.,
RA   de Paepe A., Boyd C.D.;
RT   "Mutations in a gene encoding an ABC transporter cause pseudoxanthoma
RT   elasticum.";
RL   Nat. Genet. 25:223-227(2000).
RN   [35]
RP   VARIANT VAL-671.
RX   PubMed=10811882; DOI=10.1073/pnas.100041297;
RA   Ringpfeil F., Lebwohl M.G., Christiano A.M., Uitto J.;
RT   "Pseudoxanthoma elasticum: mutations in the MRP6 gene encoding a
RT   transmembrane ATP-binding cassette (ABC) transporter.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:6001-6006(2000).
RN   [36]
RP   VARIANT SER-433, AND CHARACTERIZATION OF VARIANT VAL-671.
RX   PubMed=11721885; DOI=10.1007/s100380170017;
RA   Conrad S., Kauffmann H.-M., Ito K., Deeley R.G., Cole S.P.C., Schrenk D.;
RT   "Identification of human multidrug resistance protein 1 (MRP1) mutations
RT   and characterization of a G671V substitution.";
RL   J. Hum. Genet. 46:656-663(2001).
RN   [37]
RP   VARIANTS THR-117 AND LEU-1512.
RX   PubMed=11139250; DOI=10.1002/1098-1004(2001)17:1<74::aid-humu14>3.0.co;2-f;
RA   Perdu J., Germain D.P.;
RT   "Identification of novel polymorphisms in the pM5 and MRP1 (ABCC1) genes at
RT   locus 16p13.1 and exclusion of both genes as responsible for pseudoxanthoma
RT   elasticum.";
RL   Hum. Mutat. 17:74-75(2001).
RN   [38]
RP   VARIANTS SER-43; ILE-73; GLN-723 AND GLN-1058.
RX   PubMed=11266082; DOI=10.1097/00008571-200103000-00008;
RA   Ito S., Ieiri I., Tanabe M., Suzuki A., Higuchi S., Otsubo K.;
RT   "Polymorphism of the ABC transporter genes, MDR1, MRP1 and MRP2/cMOAT, in
RT   healthy Japanese subjects.";
RL   Pharmacogenetics 11:175-184(2001).
RN   [39]
RP   VARIANT [LARGE SCALE ANALYSIS] SER-433.
RX   PubMed=18987736; DOI=10.1038/nature07485;
RA   Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA   Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA   Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA   Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA   Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA   Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA   Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA   Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA   DiPersio J.F., Wilson R.K.;
RT   "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT   genome.";
RL   Nature 456:66-72(2008).
RN   [40]
RP   INVOLVEMENT IN DFNA77, VARIANTS DFNA77 ASP-231; VAL-296 AND SER-590,
RP   SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT DFNA77 SER-590, AND
RP   VARIANTS CYS-242; ILE-886; ARG-1007 AND THR-1086.
RX   PubMed=31273342; DOI=10.1038/s41436-019-0594-y;
RA   Li M., Mei L., He C., Chen H., Cai X., Liu Y., Tian R., Tian Q., Song J.,
RA   Jiang L., Liu C., Wu H., Li T., Liu J., Li X., Yi Y., Yan D., Blanton S.H.,
RA   Hu Z., Liu X., Li J., Ling J., Feng Y.;
RT   "Extrusion pump ABCC1 was first linked with nonsyndromic hearing loss in
RT   humans by stepwise genetic analysis.";
RL   Genet. Med. 21:2744-2754(2019).
CC   -!- FUNCTION: Mediates export of organic anions and drugs from the
CC       cytoplasm (PubMed:7961706, PubMed:16230346, PubMed:9281595,
CC       PubMed:10064732, PubMed:11114332). Mediates ATP-dependent transport of
CC       glutathione and glutathione conjugates, leukotriene C4, estradiol-17-
CC       beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics
CC       (PubMed:7961706, PubMed:16230346, PubMed:9281595, PubMed:10064732,
CC       PubMed:11114332). Confers resistance to anticancer drugs by decreasing
CC       accumulation of drug in cells, and by mediating ATP- and GSH-dependent
CC       drug export (PubMed:9281595). Hydrolyzes ATP with low efficiency
CC       (PubMed:16230346). Catalyzes the export of sphingosine 1-phosphate from
CC       mast cells independently of their degranulation (PubMed:17050692).
CC       Participates in inflammatory response by allowing export of leukotriene
CC       C4 from leukotriene C4-synthezing cells (By similarity). Mediates ATP-
CC       dependent, GSH-independent cyclic GMP-AMP (cGAMP) export
CC       (PubMed:36070769). Thus, by limiting intracellular cGAMP concentrations
CC       negatively regulates the cGAS-STING pathway (PubMed:36070769).
CC       {ECO:0000250|UniProtKB:O35379, ECO:0000269|PubMed:10064732,
CC       ECO:0000269|PubMed:11114332, ECO:0000269|PubMed:16230346,
CC       ECO:0000269|PubMed:17050692, ECO:0000269|PubMed:36070769,
CC       ECO:0000269|PubMed:7961706, ECO:0000269|PubMed:9281595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC         xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:9281595};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC         substituted glutathione(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC         ChEBI:CHEBI:456216; EC=7.6.2.3;
CC         Evidence={ECO:0000250|UniProtKB:O35379};
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:17050692};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
CC         Evidence={ECO:0000305|PubMed:17050692};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC         C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:7961706, ECO:0000269|PubMed:9281595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC         Evidence={ECO:0000269|PubMed:7961706};
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:9281595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC         Evidence={ECO:0000269|PubMed:9281595};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+)
CC         + phosphate; Xref=Rhea:RHEA:33147, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:64677, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:9281595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33148;
CC         Evidence={ECO:0000305|PubMed:9281595};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + vincristine(in) = ADP + H(+) + phosphate +
CC         vincristine(out); Xref=Rhea:RHEA:60160, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:143658, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:9281595};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60161;
CC         Evidence={ECO:0000269|PubMed:9281595};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2',3'-cGAMP(in) + ATP + H2O = 2',3'-cGAMP(out) + ADP + H(+) +
CC         phosphate; Xref=Rhea:RHEA:74887, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:143093, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:10064732};
CC   -!- ACTIVITY REGULATION: MK 571 inhibits sphingosine 1-phosphate and
CC       leukotriene C4 export. {ECO:0000269|PubMed:17050692,
CC       ECO:0000269|PubMed:7961706}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=97 nM for leukotriene C4 {ECO:0000269|PubMed:7961706};
CC         KM=19 uM for ATP {ECO:0000269|PubMed:7961706};
CC         KM=98 nM for leukotriene C4 {ECO:0000269|PubMed:9281595};
CC         KM=4.8 uM for 17beta-estradiol 17-glucosiduronic acid
CC         {ECO:0000269|PubMed:9281595};
CC         Vmax=100 pmol/min/mg enzyme for leukotriene C4 transport
CC         {ECO:0000269|PubMed:7961706};
CC         Vmax=920 pmol/min/mg enzyme for leukotriene C4 transport
CC         {ECO:0000269|PubMed:9281595};
CC         Vmax=1.4 nmol/min/mg enzyme for 17beta-estradiol 17-glucosiduronic
CC         acid transport {ECO:0000269|PubMed:9281595};
CC   -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC       protein UL138; this interaction mediates MRP1 degradation via the
CC       lysosome. {ECO:0000269|PubMed:23580527}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16230346,
CC       ECO:0000269|PubMed:31273342}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:16230346}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=9;
CC         Comment=Additional isoforms seem to exist. Experimental confirmation
CC         may be lacking for some isoforms.;
CC       Name=1; Synonyms=Allexons;
CC         IsoId=P33527-1; Sequence=Displayed;
CC       Name=2; Synonyms=Delexon-17;
CC         IsoId=P33527-2; Sequence=VSP_000037;
CC       Name=3; Synonyms=Delexon-18;
CC         IsoId=P33527-3; Sequence=VSP_000038;
CC       Name=4; Synonyms=Delexon-30;
CC         IsoId=P33527-4; Sequence=VSP_000039;
CC       Name=5; Synonyms=Delexon-17-18;
CC         IsoId=P33527-5; Sequence=VSP_000037, VSP_000038;
CC       Name=6; Synonyms=Delexon-17-30;
CC         IsoId=P33527-6; Sequence=VSP_000037, VSP_000039;
CC       Name=7; Synonyms=Delexon-18-30;
CC         IsoId=P33527-7; Sequence=VSP_000038, VSP_000039;
CC       Name=8; Synonyms=Delexon-17-18-30;
CC         IsoId=P33527-8; Sequence=VSP_000037, VSP_000038, VSP_000039;
CC       Name=9;
CC         IsoId=P33527-9; Sequence=VSP_017014;
CC   -!- TISSUE SPECIFICITY: Lung, testis and peripheral blood mononuclear
CC       cells.
CC   -!- DISEASE: Deafness, autosomal dominant, 77 (DFNA77) [MIM:618915]: A form
CC       of non-syndromic deafness characterized by adult onset of bilateral,
CC       postlingual, mild-to-severe sensorineural hearing loss. Sensorineural
CC       hearing loss results from damage to the neural receptors of the inner
CC       ear, the nerve pathways to the brain, or the area of the brain that
CC       receives sound information. {ECO:0000269|PubMed:31273342}. Note=The
CC       gene represented in this entry is involved in disease pathogenesis.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC       Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/106/abcc1";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/abcc1/";
CC   -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC       URL="http://abcm2.hegelab.org/search";
CC   ---------------------------------------------------------------------------
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DR   EMBL; L05628; AAB46616.1; -; mRNA.
DR   EMBL; AF022853; AAB83979.1; -; Genomic_DNA.
DR   EMBL; AF022827; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022828; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022829; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022831; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022833; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022835; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022837; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022839; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022841; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022850; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022849; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022848; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022847; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022846; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022845; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022844; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022843; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022842; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022852; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022851; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022840; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022838; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022836; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022834; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022832; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022826; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022825; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022824; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022830; AAB83979.1; JOINED; Genomic_DNA.
DR   EMBL; AF022853; AAB83980.1; -; Genomic_DNA.
DR   EMBL; AF022824; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022825; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022826; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022828; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022830; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022832; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022834; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022836; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022838; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022848; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022847; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022846; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022845; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022844; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022843; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022842; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022841; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022839; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022852; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022851; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022850; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022849; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022837; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022835; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022833; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022831; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022829; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022827; AAB83980.1; JOINED; Genomic_DNA.
DR   EMBL; AF022853; AAB83981.1; -; Genomic_DNA.
DR   EMBL; AF022824; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022825; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022826; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022827; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022829; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022831; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022833; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022835; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022837; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022847; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022846; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022845; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022844; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022843; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022842; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022841; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022840; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022838; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022852; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022851; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022850; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022849; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022848; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022836; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022834; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022832; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022830; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022828; AAB83981.1; JOINED; Genomic_DNA.
DR   EMBL; AF022853; AAB83983.1; -; Genomic_DNA.
DR   EMBL; AF022824; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022825; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022826; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022827; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022828; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022829; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022830; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022831; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022832; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022833; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022834; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022835; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022836; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022837; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022838; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022839; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022840; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022841; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022842; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022843; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022844; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022845; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022846; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022847; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022848; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022849; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022850; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; AF022851; AAB83983.1; JOINED; Genomic_DNA.
DR   EMBL; EF419769; ABN79590.1; -; Genomic_DNA.
DR   EMBL; AC025778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC136624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB209120; BAD92357.1; -; mRNA.
DR   EMBL; U91318; AAC15784.1; -; Genomic_DNA.
DR   EMBL; AC003026; AAC05808.1; -; Genomic_DNA.
DR   CCDS; CCDS42122.1; -. [P33527-1]
DR   CCDS; CCDS45427.1; -. [P33527-2]
DR   PIR; A44231; DVHUAR.
DR   RefSeq; NP_004987.2; NM_004996.3. [P33527-1]
DR   PDB; 2CBZ; X-ray; 1.50 A; A=642-871.
DR   PDB; 4C3Z; X-ray; 2.10 A; A=628-881.
DR   PDBsum; 2CBZ; -.
DR   PDBsum; 4C3Z; -.
DR   AlphaFoldDB; P33527; -.
DR   SMR; P33527; -.
DR   BioGRID; 110503; 162.
DR   IntAct; P33527; 26.
DR   MINT; P33527; -.
DR   STRING; 9606.ENSP00000382342; -.
DR   BindingDB; P33527; -.
DR   ChEMBL; CHEMBL3004; -.
DR   DrugBank; DB05812; Abiraterone.
DR   DrugBank; DB13783; Acemetacin.
DR   DrugBank; DB00345; Aminohippuric acid.
DR   DrugBank; DB00701; Amprenavir.
DR   DrugBank; DB01072; Atazanavir.
DR   DrugBank; DB01076; Atorvastatin.
DR   DrugBank; DB00171; ATP.
DR   DrugBank; DB15719; Belantamab mafodotin.
DR   DrugBank; DB04851; Biricodar.
DR   DrugBank; DB09061; Cannabidiol.
DR   DrugBank; DB14737; Cannabinol.
DR   DrugBank; DB02659; Cholic Acid.
DR   DrugBank; DB00845; Clofazimine.
DR   DrugBank; DB00286; Conjugated estrogens.
DR   DrugBank; DB00115; Cyanocobalamin.
DR   DrugBank; DB00970; Dactinomycin.
DR   DrugBank; DB00694; Daunorubicin.
DR   DrugBank; DB09213; Dexibuprofen.
DR   DrugBank; DB00586; Diclofenac.
DR   DrugBank; DB01248; Docetaxel.
DR   DrugBank; DB00997; Doxorubicin.
DR   DrugBank; DB00470; Dronabinol.
DR   DrugBank; DB00445; Epirubicin.
DR   DrugBank; DB00773; Etoposide.
DR   DrugBank; DB08868; Fingolimod.
DR   DrugBank; DB00693; Fluorescein.
DR   DrugBank; DB00499; Flutamide.
DR   DrugBank; DB01645; Genistein.
DR   DrugBank; DB00143; Glutathione.
DR   DrugBank; DB01016; Glyburide.
DR   DrugBank; DB00365; Grepafloxacin.
DR   DrugBank; DB01050; Ibuprofen.
DR   DrugBank; DB01177; Idarubicin.
DR   DrugBank; DB00619; Imatinib.
DR   DrugBank; DB00224; Indinavir.
DR   DrugBank; DB00328; Indomethacin.
DR   DrugBank; DB00762; Irinotecan.
DR   DrugBank; DB00602; Ivermectin.
DR   DrugBank; DB00709; Lamivudine.
DR   DrugBank; DB08855; Leukotriene C4.
DR   DrugBank; DB14009; Medical Cannabis.
DR   DrugBank; DB00563; Methotrexate.
DR   DrugBank; DB00834; Mifepristone.
DR   DrugBank; DB01204; Mitoxantrone.
DR   DrugBank; DB02375; Myricetin.
DR   DrugBank; DB14011; Nabiximols.
DR   DrugBank; DB03467; Naringenin.
DR   DrugBank; DB01165; Ofloxacin.
DR   DrugBank; DB01229; Paclitaxel.
DR   DrugBank; DB01174; Phenobarbital.
DR   DrugBank; DB01708; Prasterone.
DR   DrugBank; DB01032; Probenecid.
DR   DrugBank; DB00396; Progesterone.
DR   DrugBank; DB04216; Quercetin.
DR   DrugBank; DB03825; Rhodamine 6G.
DR   DrugBank; DB01045; Rifampicin.
DR   DrugBank; DB00503; Ritonavir.
DR   DrugBank; DB06176; Romidepsin.
DR   DrugBank; DB01232; Saquinavir.
DR   DrugBank; DB06335; Saxagliptin.
DR   DrugBank; DB01138; Sulfinpyrazone.
DR   DrugBank; DB04348; Taurocholic acid.
DR   DrugBank; DB09161; Technetium Tc-99m sestamibi.
DR   DrugBank; DB14962; Trastuzumab deruxtecan.
DR   DrugBank; DB05294; Vandetanib.
DR   DrugBank; DB08881; Vemurafenib.
DR   DrugBank; DB00661; Verapamil.
DR   DrugBank; DB00570; Vinblastine.
DR   DrugBank; DB00541; Vincristine.
DR   DrugBank; DB00399; Zoledronic acid.
DR   DrugCentral; P33527; -.
DR   GuidetoPHARMACOLOGY; 779; -.
DR   SwissLipids; SLP:000000404; -.
DR   TCDB; 3.A.1.208.8; the atp-binding cassette (abc) superfamily.
DR   GlyCosmos; P33527; 3 sites, No reported glycans.
DR   GlyGen; P33527; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P33527; -.
DR   MetOSite; P33527; -.
DR   PhosphoSitePlus; P33527; -.
DR   SwissPalm; P33527; -.
DR   BioMuta; ABCC1; -.
DR   DMDM; 296439301; -.
DR   EPD; P33527; -.
DR   jPOST; P33527; -.
DR   MassIVE; P33527; -.
DR   MaxQB; P33527; -.
DR   PaxDb; 9606-ENSP00000382342; -.
DR   PeptideAtlas; P33527; -.
DR   ProteomicsDB; 54912; -. [P33527-1]
DR   ProteomicsDB; 54913; -. [P33527-2]
DR   ProteomicsDB; 54914; -. [P33527-3]
DR   ProteomicsDB; 54915; -. [P33527-4]
DR   ProteomicsDB; 54916; -. [P33527-5]
DR   ProteomicsDB; 54917; -. [P33527-6]
DR   ProteomicsDB; 54918; -. [P33527-7]
DR   ProteomicsDB; 54919; -. [P33527-8]
DR   ProteomicsDB; 54920; -. [P33527-9]
DR   Pumba; P33527; -.
DR   ABCD; P33527; 1 sequenced antibody.
DR   Antibodypedia; 4235; 604 antibodies from 50 providers.
DR   DNASU; 4363; -.
DR   Ensembl; ENST00000399408.7; ENSP00000382340.4; ENSG00000103222.20. [P33527-9]
DR   Ensembl; ENST00000399410.8; ENSP00000382342.3; ENSG00000103222.20. [P33527-1]
DR   Ensembl; ENST00000572882.3; ENSP00000461615.2; ENSG00000103222.20. [P33527-2]
DR   Ensembl; ENST00000621144.4; ENSP00000483316.1; ENSG00000278183.4. [P33527-1]
DR   GeneID; 4363; -.
DR   KEGG; hsa:4363; -.
DR   MANE-Select; ENST00000399410.8; ENSP00000382342.3; NM_004996.4; NP_004987.2.
DR   UCSC; uc010bvi.4; human. [P33527-1]
DR   AGR; HGNC:51; -.
DR   CTD; 4363; -.
DR   DisGeNET; 4363; -.
DR   GeneCards; ABCC1; -.
DR   HGNC; HGNC:51; ABCC1.
DR   HPA; ENSG00000103222; Low tissue specificity.
DR   MalaCards; ABCC1; -.
DR   MIM; 158343; gene.
DR   MIM; 618915; phenotype.
DR   neXtProt; NX_P33527; -.
DR   OpenTargets; ENSG00000103222; -.
DR   Orphanet; 90635; Rare autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR   PharmGKB; PA244; -.
DR   VEuPathDB; HostDB:ENSG00000103222; -.
DR   eggNOG; KOG0054; Eukaryota.
DR   GeneTree; ENSGT00940000160271; -.
DR   InParanoid; P33527; -.
DR   OMA; IRYDFTP; -.
DR   OrthoDB; 3384185at2759; -.
DR   PhylomeDB; P33527; -.
DR   TreeFam; TF105199; -.
DR   BioCyc; MetaCyc:ENSG00000103222-MONOMER; -.
DR   BRENDA; 7.6.2.2; 2681.
DR   BRENDA; 7.6.2.3; 2681.
DR   PathwayCommons; P33527; -.
DR   Reactome; R-HSA-189483; Heme degradation.
DR   Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR   Reactome; R-HSA-9753281; Paracetamol ADME.
DR   Reactome; R-HSA-9758890; Transport of RCbl within the body.
DR   SignaLink; P33527; -.
DR   SIGNOR; P33527; -.
DR   BioGRID-ORCS; 4363; 16 hits in 1168 CRISPR screens.
DR   ChiTaRS; ABCC1; human.
DR   EvolutionaryTrace; P33527; -.
DR   GeneWiki; ABCC1; -.
DR   GenomeRNAi; 4363; -.
DR   Pharos; P33527; Tchem.
DR   PRO; PR:P33527; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P33527; Protein.
DR   Bgee; ENSG00000103222; Expressed in lower esophagus mucosa and 95 other tissues.
DR   ExpressionAtlas; P33527; baseline and differential.
DR   Genevisible; P33527; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:CACAO.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISS:UniProtKB.
DR   GO; GO:0140359; F:ABC-type transporter activity; IDA:UniProtKB.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; EXP:Reactome.
DR   GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IBA: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:0043225; F:ATPase-coupled inorganic anion transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IMP:BHF-UCL.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; IMP:ARUK-UCL.
DR   GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:ARUK-UCL.
DR   GO; GO:0034634; F:glutathione transmembrane transporter activity; ISS:ARUK-UCL.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:1905039; P:carboxylic acid transmembrane transport; IMP:ARUK-UCL.
DR   GO; GO:0060326; P:cell chemotaxis; ISS:BHF-UCL.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; ISS:ARUK-UCL.
DR   GO; GO:0034599; P:cellular response to oxidative stress; TAS:Reactome.
DR   GO; GO:0015889; P:cobalamin transport; TAS:Reactome.
DR   GO; GO:0070729; P:cyclic nucleotide transport; IMP:UniProtKB.
DR   GO; GO:0140115; P:export across plasma membrane; IMP:ARUK-UCL.
DR   GO; GO:0034775; P:glutathione transmembrane transport; IBA:GO_Central.
DR   GO; GO:0042167; P:heme catabolic process; TAS:Reactome.
DR   GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
DR   GO; GO:0071716; P:leukotriene transport; ISS:UniProtKB.
DR   GO; GO:0045332; P:phospholipid translocation; IMP:BHF-UCL.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR   GO; GO:0099039; P:sphingolipid translocation; IMP:BHF-UCL.
DR   GO; GO:0070633; P:transepithelial transport; IMP:ARUK-UCL.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   GO; GO:0042908; P:xenobiotic transport; ISS:ARUK-UCL.
DR   GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; IMP:ARUK-UCL.
DR   CDD; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1.
DR   CDD; cd18603; ABC_6TM_MRP1_2_3_6_D2_like; 1.
DR   CDD; cd03250; ABCC_MRP_domain1; 1.
DR   CDD; cd03244; ABCC_MRP_domain2; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR005292; MRP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00957; MRP_assoc_pro; 1.
DR   PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR   PANTHER; PTHR24223:SF241; MULTIDRUG RESISTANCE-ASSOCIATED PROTEIN 1; 1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell membrane; Deafness;
KW   Glycoprotein; Hydrolase; Lipid transport; Membrane; Non-syndromic deafness;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1531
FT                   /note="Multidrug resistance-associated protein 1"
FT                   /id="PRO_0000093351"
FT   TOPO_DOM        1..33
FT                   /note="Extracellular"
FT   TRANSMEM        34..54
FT                   /note="Helical; Name=1"
FT   TOPO_DOM        55..74
FT                   /note="Cytoplasmic"
FT   TRANSMEM        75..95
FT                   /note="Helical; Name=2"
FT   TOPO_DOM        96..100
FT                   /note="Extracellular"
FT   TRANSMEM        101..121
FT                   /note="Helical; Name=3"
FT   TOPO_DOM        122..133
FT                   /note="Cytoplasmic"
FT   TRANSMEM        134..154
FT                   /note="Helical; Name=4"
FT   TOPO_DOM        155..172
FT                   /note="Extracellular"
FT   TRANSMEM        173..193
FT                   /note="Helical; Name=5"
FT   TOPO_DOM        194..316
FT                   /note="Cytoplasmic"
FT   TRANSMEM        317..337
FT                   /note="Helical; Name=6"
FT   TOPO_DOM        338..363
FT                   /note="Extracellular"
FT   TRANSMEM        364..384
FT                   /note="Helical; Name=7"
FT   TOPO_DOM        385..440
FT                   /note="Cytoplasmic"
FT   TRANSMEM        441..461
FT                   /note="Helical; Name=8"
FT   TOPO_DOM        462..464
FT                   /note="Extracellular"
FT   TRANSMEM        465..485
FT                   /note="Helical; Name=9"
FT   TOPO_DOM        486..547
FT                   /note="Cytoplasmic"
FT   TRANSMEM        548..568
FT                   /note="Helical; Name=10"
FT   TOPO_DOM        569..590
FT                   /note="Extracellular"
FT   TRANSMEM        591..611
FT                   /note="Helical; Name=11"
FT   TOPO_DOM        612..967
FT                   /note="Cytoplasmic"
FT   TRANSMEM        968..988
FT                   /note="Helical; Name=12"
FT   TOPO_DOM        989..1025
FT                   /note="Extracellular"
FT   TRANSMEM        1026..1046
FT                   /note="Helical; Name=13"
FT   TOPO_DOM        1047..1089
FT                   /note="Cytoplasmic"
FT   TRANSMEM        1090..1110
FT                   /note="Helical; Name=14"
FT   TOPO_DOM        1111
FT                   /note="Extracellular"
FT   TRANSMEM        1112..1132
FT                   /note="Helical; Name=15"
FT   TOPO_DOM        1133..1203
FT                   /note="Cytoplasmic"
FT   TRANSMEM        1204..1224
FT                   /note="Helical; Name=16"
FT   TOPO_DOM        1225..1226
FT                   /note="Extracellular"
FT   TRANSMEM        1227..1247
FT                   /note="Helical; Name=17"
FT   TOPO_DOM        1248..1531
FT                   /note="Cytoplasmic"
FT   DOMAIN          325..608
FT                   /note="ABC transmembrane type-1 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          644..868
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          975..1256
FT                   /note="ABC transmembrane type-1 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1293..1527
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         653
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   BINDING         678..685
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   BINDING         713
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT   BINDING         1327..1334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         277
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:O35379"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35379"
FT   MOD_RES         503
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O35379"
FT   MOD_RES         905
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         915
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         930
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9295302"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9295302"
FT   CARBOHYD        1006
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9295302"
FT   VAR_SEQ         706..764
FT                   /note="Missing (in isoform 2, isoform 5, isoform 6 and
FT                   isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000037"
FT   VAR_SEQ         765..820
FT                   /note="Missing (in isoform 3, isoform 5, isoform 7 and
FT                   isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000038"
FT   VAR_SEQ         882
FT                   /note="G -> GSTVMDEEEAG (in isoform 9)"
FT                   /evidence="ECO:0000303|Ref.6"
FT                   /id="VSP_017014"
FT   VAR_SEQ         1431..1495
FT                   /note="Missing (in isoform 4, isoform 6, isoform 7 and
FT                   isoform 8)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000039"
FT   VARIANT         43
FT                   /note="C -> S (in dbSNP:rs41395947)"
FT                   /evidence="ECO:0000269|PubMed:11266082"
FT                   /id="VAR_013317"
FT   VARIANT         73
FT                   /note="T -> I (in dbSNP:rs41494447)"
FT                   /evidence="ECO:0000269|PubMed:11266082"
FT                   /id="VAR_013318"
FT   VARIANT         117
FT                   /note="M -> T"
FT                   /evidence="ECO:0000269|PubMed:11139250,
FT                   ECO:0000269|PubMed:1360704, ECO:0000269|PubMed:9344662"
FT                   /id="VAR_013319"
FT   VARIANT         231
FT                   /note="G -> D (in DFNA77; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:31273342"
FT                   /id="VAR_083988"
FT   VARIANT         242
FT                   /note="W -> C"
FT                   /evidence="ECO:0000269|PubMed:31273342"
FT                   /id="VAR_083989"
FT   VARIANT         296
FT                   /note="E -> V (in DFNA77; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:31273342"
FT                   /id="VAR_083990"
FT   VARIANT         433
FT                   /note="R -> S (in dbSNP:rs60782127)"
FT                   /evidence="ECO:0000269|PubMed:11721885,
FT                   ECO:0000269|PubMed:18987736"
FT                   /id="VAR_013320"
FT   VARIANT         590
FT                   /note="N -> S (in DFNA77; changes protein subcellular
FT                   localization expressed in both membrane and cytoplasm;
FT                   produces unstable mRNA)"
FT                   /evidence="ECO:0000269|PubMed:31273342"
FT                   /id="VAR_083991"
FT   VARIANT         633
FT                   /note="R -> Q (in dbSNP:rs112282109)"
FT                   /evidence="ECO:0000269|PubMed:10835642"
FT                   /id="VAR_011488"
FT   VARIANT         671
FT                   /note="G -> V (no effect on leukotriene C4 and estradiol
FT                   glucuronide transport; dbSNP:rs45511401)"
FT                   /evidence="ECO:0000269|PubMed:10811882,
FT                   ECO:0000269|PubMed:10835642, ECO:0000269|PubMed:11721885,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_011489"
FT   VARIANT         723
FT                   /note="R -> Q (in dbSNP:rs4148356)"
FT                   /evidence="ECO:0000269|PubMed:11266082, ECO:0000269|Ref.4"
FT                   /id="VAR_013321"
FT   VARIANT         861
FT                   /note="A -> T (in dbSNP:rs45517537)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_055384"
FT   VARIANT         886
FT                   /note="V -> I"
FT                   /evidence="ECO:0000269|PubMed:31273342"
FT                   /id="VAR_083992"
FT   VARIANT         1007
FT                   /note="G -> R"
FT                   /evidence="ECO:0000269|PubMed:31273342"
FT                   /id="VAR_083993"
FT   VARIANT         1047
FT                   /note="C -> S (in dbSNP:rs13337489)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_055385"
FT   VARIANT         1058
FT                   /note="R -> Q (in dbSNP:rs41410450)"
FT                   /evidence="ECO:0000269|PubMed:11266082"
FT                   /id="VAR_013322"
FT   VARIANT         1086
FT                   /note="M -> T"
FT                   /evidence="ECO:0000269|PubMed:31273342"
FT                   /id="VAR_083994"
FT   VARIANT         1146
FT                   /note="V -> I (in dbSNP:rs28706727)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_055386"
FT   VARIANT         1512
FT                   /note="S -> L (in dbSNP:rs369410659)"
FT                   /evidence="ECO:0000269|PubMed:11139250"
FT                   /id="VAR_013323"
FT   MUTAGEN         580
FT                   /note="Q->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:15260484"
FT   MUTAGEN         581
FT                   /note="T->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:15260484"
FT   MUTAGEN         585
FT                   /note="S->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:15260484"
FT   MUTAGEN         597
FT                   /note="N->A: Increases resistance to vincristine and
FT                   decreases resistance to VP-16."
FT                   /evidence="ECO:0000269|PubMed:15260484"
FT   MUTAGEN         604
FT                   /note="S->A: Increases estradiol glucuronide transport."
FT                   /evidence="ECO:0000269|PubMed:15260484"
FT   MUTAGEN         605
FT                   /note="S->A: Decreases resistance to vincristine, VP-16 and
FT                   doxorubicin."
FT                   /evidence="ECO:0000269|PubMed:15260484"
FT   MUTAGEN         792
FT                   /note="D->A: Only partially affects protein maturation;
FT                   impairs leukotriene C4 transport."
FT                   /evidence="ECO:0000269|PubMed:11469806"
FT   MUTAGEN         792
FT                   /note="D->L: Impairs protein maturation and leukotriene C4
FT                   transport."
FT                   /evidence="ECO:0000269|PubMed:11469806"
FT   MUTAGEN         793
FT                   /note="D->L: No effect on protein maturation and
FT                   leukotriene C4 transport."
FT                   /evidence="ECO:0000269|PubMed:11469806"
FT   MUTAGEN         1046
FT                   /note="R->D: Slightly impairs leukotriene C4 and estradiol
FT                   glucuronide transport."
FT                   /evidence="ECO:0000269|PubMed:15208328"
FT   MUTAGEN         1084
FT                   /note="D->R: Impairs leukotriene C4 and estradiol
FT                   glucuronide transport."
FT                   /evidence="ECO:0000269|PubMed:15208328"
FT   MUTAGEN         1089
FT                   /note="E->A,L,N,Q: Decreases resistance to anthracyclines."
FT                   /evidence="ECO:0000269|PubMed:11278596"
FT   MUTAGEN         1089
FT                   /note="E->D: No effect."
FT                   /evidence="ECO:0000269|PubMed:11278596"
FT   MUTAGEN         1089
FT                   /note="E->K: Abolishes resistance to anthracyclines."
FT                   /evidence="ECO:0000269|PubMed:11278596"
FT   MUTAGEN         1131
FT                   /note="R->E: Slightly impairs leukotriene C4 and estradiol
FT                   glucuronide transport."
FT                   /evidence="ECO:0000269|PubMed:15208328"
FT   MUTAGEN         1138
FT                   /note="R->E,K: Strongly reduced transport of leukotriene
FT                   C4, estradiol glucuronide and of glutathione."
FT                   /evidence="ECO:0000269|PubMed:16230346"
FT   MUTAGEN         1141
FT                   /note="K->E: Reduced transport of leukotriene C4 and of
FT                   glutathione."
FT                   /evidence="ECO:0000269|PubMed:16230346"
FT   MUTAGEN         1141
FT                   /note="K->R: Reduced transport of glutathione."
FT                   /evidence="ECO:0000269|PubMed:16230346"
FT   MUTAGEN         1142
FT                   /note="R->E,K: Reduced transport of leukotriene C4,
FT                   estradiol glucuronide and of glutathione."
FT                   /evidence="ECO:0000269|PubMed:16230346"
FT   MUTAGEN         1246
FT                   /note="W->A,F,Y: Impairs estradiol glucuronide transport."
FT                   /evidence="ECO:0000269|PubMed:11278867"
FT   MUTAGEN         1246
FT                   /note="W->C: Impairs estradiol glucuronide transport; loss
FT                   of resistance to alkaloid vincristine, cationic
FT                   anthracyclines, epipodophyllotoxin VP-16, but not potassium
FT                   antimony tartrate; partial loss of resistance to sodium
FT                   arsenite."
FT                   /evidence="ECO:0000269|PubMed:11278867"
FT   MUTAGEN         1333
FT                   /note="K->L: Impairs leukotriene C4 transport."
FT                   /evidence="ECO:0000269|PubMed:11469806"
FT   MUTAGEN         1333
FT                   /note="K->M: Reduced cGAMP export."
FT                   /evidence="ECO:0000269|PubMed:36070769"
FT   MUTAGEN         1454..1455
FT                   /note="DE->LL: Impairs leukotriene C4 transport."
FT                   /evidence="ECO:0000269|PubMed:11469806"
FT   STRAND          644..653
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          660..668
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          673..677
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           684..691
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          695..704
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          708..711
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          719..721
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           722..727
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           736..743
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           747..750
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           756..758
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          759..762
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           770..784
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          787..793
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   TURN            794..797
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           800..809
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   TURN            816..819
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          820..825
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           832..834
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          835..842
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   STRAND          845..850
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           852..858
FT                   /evidence="ECO:0007829|PDB:2CBZ"
FT   HELIX           861..868
FT                   /evidence="ECO:0007829|PDB:2CBZ"
SQ   SEQUENCE   1531 AA;  171591 MW;  46A7CB643B9478C4 CRC64;
     MALRGFCSAD GSDPLWDWNV TWNTSNPDFT KCFQNTVLVW VPCFYLWACF PFYFLYLSRH
     DRGYIQMTPL NKTKTALGFL LWIVCWADLF YSFWERSRGI FLAPVFLVSP TLLGITMLLA
     TFLIQLERRK GVQSSGIMLT FWLVALVCAL AILRSKIMTA LKEDAQVDLF RDITFYVYFS
     LLLIQLVLSC FSDRSPLFSE TIHDPNPCPE SSASFLSRIT FWWITGLIVR GYRQPLEGSD
     LWSLNKEDTS EQVVPVLVKN WKKECAKTRK QPVKVVYSSK DPAQPKESSK VDANEEVEAL
     IVKSPQKEWN PSLFKVLYKT FGPYFLMSFF FKAIHDLMMF SGPQILKLLI KFVNDTKAPD
     WQGYFYTVLL FVTACLQTLV LHQYFHICFV SGMRIKTAVI GAVYRKALVI TNSARKSSTV
     GEIVNLMSVD AQRFMDLATY INMIWSAPLQ VILALYLLWL NLGPSVLAGV AVMVLMVPVN
     AVMAMKTKTY QVAHMKSKDN RIKLMNEILN GIKVLKLYAW ELAFKDKVLA IRQEELKVLK
     KSAYLSAVGT FTWVCTPFLV ALCTFAVYVT IDENNILDAQ TAFVSLALFN ILRFPLNILP
     MVISSIVQAS VSLKRLRIFL SHEELEPDSI ERRPVKDGGG TNSITVRNAT FTWARSDPPT
     LNGITFSIPE GALVAVVGQV GCGKSSLLSA LLAEMDKVEG HVAIKGSVAY VPQQAWIQND
     SLRENILFGC QLEEPYYRSV IQACALLPDL EILPSGDRTE IGEKGVNLSG GQKQRVSLAR
     AVYSNADIYL FDDPLSAVDA HVGKHIFENV IGPKGMLKNK TRILVTHSMS YLPQVDVIIV
     MSGGKISEMG SYQELLARDG AFAEFLRTYA STEQEQDAEE NGVTGVSGPG KEAKQMENGM
     LVTDSAGKQL QRQLSSSSSY SGDISRHHNS TAELQKAEAK KEETWKLMEA DKAQTGQVKL
     SVYWDYMKAI GLFISFLSIF LFMCNHVSAL ASNYWLSLWT DDPIVNGTQE HTKVRLSVYG
     ALGISQGIAV FGYSMAVSIG GILASRCLHV DLLHSILRSP MSFFERTPSG NLVNRFSKEL
     DTVDSMIPEV IKMFMGSLFN VIGACIVILL ATPIAAIIIP PLGLIYFFVQ RFYVASSRQL
     KRLESVSRSP VYSHFNETLL GVSVIRAFEE QERFIHQSDL KVDENQKAYY PSIVANRWLA
     VRLECVGNCI VLFAALFAVI SRHSLSAGLV GLSVSYSLQV TTYLNWLVRM SSEMETNIVA
     VERLKEYSET EKEAPWQIQE TAPPSSWPQV GRVEFRNYCL RYREDLDFVL RHINVTINGG
     EKVGIVGRTG AGKSSLTLGL FRINESAEGE IIIDGINIAK IGLHDLRFKI TIIPQDPVLF
     SGSLRMNLDP FSQYSDEEVW TSLELAHLKD FVSALPDKLD HECAEGGENL SVGQRQLVCL
     ARALLRKTKI LVLDEATAAV DLETDDLIQS TIRTQFEDCT VLTIAHRLNT IMDYTRVIVL
     DKGEIQEYGA PSDLLQQRGL FYSMAKDAGL V
//