MRP1_HUMAN
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 03-AUG-2022, entry version 218.
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 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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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).
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:7961706,
CC 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 -!- 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 -!- 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="http://atlasgeneticsoncology.org/Genes/MRPID106.html";
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 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; 158.
DR IntAct; P33527; 24.
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; 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; DB00445; Epirubicin.
DR DrugBank; DB00773; Etoposide.
DR DrugBank; DB08868; Fingolimod.
DR DrugBank; DB00693; Fluorescein.
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; 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 GlyGen; P33527; 3 sites.
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; P33527; -.
DR PeptideAtlas; P33527; -.
DR PRIDE; 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 ABCD; P33527; 1 sequenced antibody.
DR Antibodypedia; 4235; 578 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 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; 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; 138195at2759; -.
DR PhylomeDB; P33527; -.
DR TreeFam; TF105199; -.
DR BioCyc; MetaCyc:ENSG00000103222-MON; -.
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; 15 hits in 1080 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:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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; TAS: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: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; IBA:GO_Central.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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:0009235; P:cobalamin metabolic process; TAS:Reactome.
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; IBA:GO_Central.
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 Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 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; Multidrug-R_assoc.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
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 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
