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Accession Number: | P33527 |
Protein Name: | MRP1 aka ABCC1 aka MRP |
Length: | 1531 |
Molecular Weight: | 171591.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 17 |
Location1 / Topology2 / Orientation3: | Cell membrane1 / Multi-pass membrane protein2 |
Substrate | mercury(2+), arsenate(3-), arsenite(3-), glutathione, folic acid, methotrexate, leukotriene C4, glutathione conjugate, cobalamin, bis(2-chloroethyl) sulfide, antimony(0), estrone 3-sulfate, mechlorethamine |
Cross database links:
RefSeq: | NP_004987.2 |
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Entrez Gene ID: | 4363 |
Pfam: | PF00664 PF00005 |
OMIM: |
158343 gene |
KEGG: | hsa:4363 |
Gene Ontology
GO:0005887
C:integral to plasma membrane
GO:0005624
C:membrane fraction
GO:0005524
F:ATP binding
GO:0042626
F:ATPase activity, coupled to transmembrane m...
GO:0042493
P:response to drug
GO:0055085
P:transmembrane transport
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References (27)[1] “Overexpression of a transporter gene in a multidrug-resistant human lung cancer cell line.” Cole S.P.C.et.al. 1360704 [2] “Multidrug resistance-associated protein: sequence correction.” Cole S.P.C.et.al. 8098549 [3] “Analysis of the intron-exon organization of the human multidrug-resistance protein gene (MRP) and alternative splicing of its mRNA.” Grant C.E.et.al. 9344662 [4] “The sequence and analysis of duplication-rich human chromosome 16.” Martin J.et.al. 15616553 [5] “Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q.” Loftus B.J.et.al. 10493829 [6] “Membrane topology of the multidrug resistance protein (MRP). A study of glycosylation-site mutants reveals an extracytosolic NH2 terminus.” Hipfner D.R.et.al. 9295302 [7] “Topology mapping of the amino-terminal half of multidrug resistance-associated protein by epitope insertion and immunofluorescence.” Kast C.et.al. 9334225 [8] “Epitope insertion favors a six transmembrane domain model for the carboxy-terminal portion of the multidrug resistance-associated protein.” Kast C.et.al. 9485377 [9] “Characterization of a leukotriene C4 export mechanism in human platelets: possible involvement of multidrug resistance-associated protein 1.” Sjoelinder M.et.al. 10064732 [10] “The leukotriene C(4) transporter MRP1 regulates CCL19 (MIP-3beta, ELC)-dependent mobilization of dendritic cells to lymph nodes.” Robbiani D.F.et.al. 11114332 [11] “Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation.” Cui L.et.al. 11469806 [12] “Mutation of a single conserved tryptophan in multidrug resistance protein 1 (MRP1/ABCC1) results in loss of drug resistance and selective loss of organic anion transport.” Ito K.et.al. 11278867 [13] “Identification of an amino acid residue in multidrug resistance protein 1 critical for conferring resistance to anthracyclines.” Zhang D.-W.et.al. 11278596 [14] “Mutational analysis of ionizable residues proximal to the cytoplasmic interface of membrane spanning domain 3 of the multidrug resistance protein, MRP1 (ABCC1): glutamate 1204 is important for both the expression and catalytic activity of the transporter.” Situ D.et.al. 15208328 [15] “Transmembrane helix 11 of multidrug resistance protein 1 (MRP1/ABCC1): identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1.” Zhang D.-W.et.al. 15260484 [16] “Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1).” Conseil G.et.al. 16230346 [17] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.” Daub H.et.al. 18691976 [18] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.” Gauci S.et.al. 19413330 [19] “Large-scale proteomics analysis of the human kinome.” Oppermann F.S.et.al. 19369195 [20] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.” Mayya V.et.al. 19690332 [21] “Structure of the human multidrug resistance protein 1 nucleotide binding domain 1 bound to Mg2+/ATP reveals a non-productive catalytic site.” Ramaen O.et.al. 16697012 [22] “Mutations in a gene encoding an ABC transporter cause pseudoxanthoma elasticum.” Le Saux O.et.al. 10835642 [23] “Pseudoxanthoma elasticum: mutations in the MRP6 gene encoding a transmembrane ATP-binding cassette (ABC) transporter.” Ringpfeil F.et.al. 10811882 [24] “Identification of human multidrug resistance protein 1 (MRP1) mutations and characterization of a G671V substitution.” Conrad S.et.al. 11721885 [25] “Identification of novel polymorphisms in the pM5 and MRP1 (ABCC1) genes at locus 16p13.1 and exclusion of both genes as responsible for pseudoxanthoma elasticum.” Perdu J.et.al. 11139250 | |
Structure: | |
External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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1: MALRGFCSAD GSDPLWDWNV TWNTSNPDFT KCFQNTVLVW VPCFYLWACF PFYFLYLSRH 61: DRGYIQMTPL NKTKTALGFL LWIVCWADLF YSFWERSRGI FLAPVFLVSP TLLGITMLLA 121: TFLIQLERRK GVQSSGIMLT FWLVALVCAL AILRSKIMTA LKEDAQVDLF RDITFYVYFS 181: LLLIQLVLSC FSDRSPLFSE TIHDPNPCPE SSASFLSRIT FWWITGLIVR GYRQPLEGSD 241: LWSLNKEDTS EQVVPVLVKN WKKECAKTRK QPVKVVYSSK DPAQPKESSK VDANEEVEAL 301: IVKSPQKEWN PSLFKVLYKT FGPYFLMSFF FKAIHDLMMF SGPQILKLLI KFVNDTKAPD 361: WQGYFYTVLL FVTACLQTLV LHQYFHICFV SGMRIKTAVI GAVYRKALVI TNSARKSSTV 421: GEIVNLMSVD AQRFMDLATY INMIWSAPLQ VILALYLLWL NLGPSVLAGV AVMVLMVPVN 481: AVMAMKTKTY QVAHMKSKDN RIKLMNEILN GIKVLKLYAW ELAFKDKVLA IRQEELKVLK 541: KSAYLSAVGT FTWVCTPFLV ALCTFAVYVT IDENNILDAQ TAFVSLALFN ILRFPLNILP 601: MVISSIVQAS VSLKRLRIFL SHEELEPDSI ERRPVKDGGG TNSITVRNAT FTWARSDPPT 661: LNGITFSIPE GALVAVVGQV GCGKSSLLSA LLAEMDKVEG HVAIKGSVAY VPQQAWIQND 721: SLRENILFGC QLEEPYYRSV IQACALLPDL EILPSGDRTE IGEKGVNLSG GQKQRVSLAR 781: AVYSNADIYL FDDPLSAVDA HVGKHIFENV IGPKGMLKNK TRILVTHSMS YLPQVDVIIV 841: MSGGKISEMG SYQELLARDG AFAEFLRTYA STEQEQDAEE NGVTGVSGPG KEAKQMENGM 901: LVTDSAGKQL QRQLSSSSSY SGDISRHHNS TAELQKAEAK KEETWKLMEA DKAQTGQVKL 961: SVYWDYMKAI GLFISFLSIF LFMCNHVSAL ASNYWLSLWT DDPIVNGTQE HTKVRLSVYG 1021: ALGISQGIAV FGYSMAVSIG GILASRCLHV DLLHSILRSP MSFFERTPSG NLVNRFSKEL 1081: DTVDSMIPEV IKMFMGSLFN VIGACIVILL ATPIAAIIIP PLGLIYFFVQ RFYVASSRQL 1141: KRLESVSRSP VYSHFNETLL GVSVIRAFEE QERFIHQSDL KVDENQKAYY PSIVANRWLA 1201: VRLECVGNCI VLFAALFAVI SRHSLSAGLV GLSVSYSLQV TTYLNWLVRM SSEMETNIVA 1261: VERLKEYSET EKEAPWQIQE TAPPSSWPQV GRVEFRNYCL RYREDLDFVL RHINVTINGG 1321: EKVGIVGRTG AGKSSLTLGL FRINESAEGE IIIDGINIAK IGLHDLRFKI TIIPQDPVLF 1381: SGSLRMNLDP FSQYSDEEVW TSLELAHLKD FVSALPDKLD HECAEGGENL SVGQRQLVCL 1441: ARALLRKTKI LVLDEATAAV DLETDDLIQS TIRTQFEDCT VLTIAHRLNT IMDYTRVIVL 1501: DKGEIQEYGA PSDLLQQRGL FYSMAKDAGL V