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Q8CG09 (MRP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multidrug resistance-associated protein 1
Alternative name(s):
ATP-binding cassette sub-family C member 1
Leukotriene C(4) transporter
Short name=LTC4 transporter
Gene names
Name:Abcc1
Synonyms:Mrp1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1532 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency. Ref.7

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.7.

Tissue specificity

Skeletal muscle, brain, heart, spleen, lung and kidney. Ref.2

Post-translational modification

Glycosylated.

Sequence similarities

Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. [View classification]

Contains 2 ABC transmembrane type-1 domains.

Contains 2 ABC transporter domains.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell chemotaxis

Inferred from mutant phenotype PubMed 17050692. Source: RGD

daunorubicin transport

Inferred from mutant phenotype PubMed 18465260. Source: RGD

drug export

Inferred from direct assay Ref.1PubMed 15198509. Source: RGD

drug transmembrane transport

Inferred from direct assay PubMed 15198509. Source: RGD

glutathione transmembrane transport

Inferred from mutant phenotype PubMed 12125073. Source: RGD

negative regulation of neuron death

Inferred from mutant phenotype PubMed 17141959. Source: RGD

phospholipid efflux

Inferred from mutant phenotype PubMed 17050692. Source: RGD

plasma membrane long-chain fatty acid transport

Inferred from direct assay Ref.2. Source: RGD

positive regulation of cell migration

Inferred from mutant phenotype PubMed 17050692. Source: RGD

response to drug

Inferred from direct assay PubMed 14641820. Source: RGD

response to oxidative stress

Inferred from mutant phenotype Ref.5. Source: RGD

transmembrane transport

Inferred from direct assay Ref.1. Source: RGD

xenobiotic transport

Inferred from mutant phenotype PubMed 12893836. Source: RGD

   Cellular_componentbasolateral plasma membrane

Inferred from direct assay PubMed 11804835PubMed 17854063. Source: RGD

cytoplasm

Inferred from direct assay PubMed 11804835. Source: RGD

integral component of plasma membrane

Inferred from direct assay PubMed 17854063. Source: RGD

membrane

Inferred from direct assay PubMed 12893836. Source: RGD

plasma membrane

Inferred from direct assay PubMed 11804835. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

drug transmembrane transporter activity

Inferred from direct assay PubMed 15198509. Source: RGD

efflux transmembrane transporter activity

Inferred from direct assay Ref.1. Source: RGD

glutathione S-conjugate-exporting ATPase activity

Inferred from mutant phenotype PubMed 19053318. Source: RGD

glutathione transmembrane transporter activity

Inferred from mutant phenotype PubMed 12125073. Source: RGD

lipid-transporting ATPase activity

Inferred from direct assay Ref.2. Source: RGD

long-chain fatty acid transporter activity

Inferred from direct assay Ref.2. Source: RGD

oxidoreductase activity

Inferred from electronic annotation. Source: InterPro

sphingolipid transporter activity

Inferred from mutant phenotype PubMed 17050692. Source: RGD

xenobiotic-transporting ATPase activity

Inferred from direct assay Ref.2. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CG09-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8CG09-2)

The sequence of this isoform differs from the canonical sequence as follows:
     912-920: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15321532Multidrug resistance-associated protein 1
PRO_0000093354

Regions

Topological domain1 – 3333Extracellular By similarity
Transmembrane34 – 5421Helical; Name=1; By similarity
Topological domain55 – 7420Cytoplasmic By similarity
Transmembrane75 – 9521Helical; Name=2; By similarity
Topological domain96 – 1005Extracellular By similarity
Transmembrane101 – 12121Helical; Name=3; By similarity
Topological domain122 – 13312Cytoplasmic By similarity
Transmembrane134 – 15421Helical; Name=4; By similarity
Topological domain155 – 17218Extracellular By similarity
Transmembrane173 – 19321Helical; Name=5; By similarity
Topological domain194 – 317124Cytoplasmic By similarity
Transmembrane318 – 33821Helical; Name=6; By similarity
Topological domain339 – 36426Extracellular By similarity
Transmembrane365 – 38521Helical; Name=7; By similarity
Topological domain386 – 44156Cytoplasmic By similarity
Transmembrane442 – 46221Helical; Name=8; By similarity
Topological domain463 – 4653Extracellular By similarity
Transmembrane466 – 48621Helical; Name=9; By similarity
Topological domain487 – 54862Cytoplasmic By similarity
Transmembrane549 – 56921Helical; Name=10; By similarity
Topological domain570 – 59122Extracellular By similarity
Transmembrane592 – 61221Helical; Name=11; By similarity
Topological domain613 – 967355Cytoplasmic By similarity
Transmembrane968 – 98821Helical; Name=12; By similarity
Topological domain989 – 102638Extracellular By similarity
Transmembrane1027 – 104721Helical; Name=13; By similarity
Topological domain1048 – 109043Cytoplasmic By similarity
Transmembrane1091 – 111121Helical; Name=14; By similarity
Topological domain11121Extracellular By similarity
Transmembrane1113 – 113321Helical; Name=15; By similarity
Topological domain1134 – 120471Cytoplasmic By similarity
Transmembrane1205 – 122521Helical; Name=16; By similarity
Topological domain1226 – 12272Extracellular By similarity
Transmembrane1228 – 124821Helical; Name=17; By similarity
Topological domain1249 – 1532284Cytoplasmic By similarity
Domain326 – 609284ABC transmembrane type-1 1
Domain645 – 869225ABC transporter 1
Domain975 – 1257283ABC transmembrane type-1 2
Domain1294 – 1528235ABC transporter 2
Nucleotide binding679 – 6868ATP 1 Potential
Nucleotide binding1328 – 13358ATP 2 Potential

Amino acid modifications

Modified residue5041N6-succinyllysine By similarity
Modified residue8791Phosphoserine By similarity
Modified residue8831Phosphoserine By similarity
Modified residue9161Phosphoserine By similarity
Modified residue9311Phosphoserine By similarity
Glycosylation191N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence912 – 9209Missing in isoform 2.
VSP_017015

Experimental info

Mutagenesis9831L → M: No effect on estradiol glucuronide transport. Ref.2
Mutagenesis10901Q → E: 7.6-fold increase of the estradiol glucuronide transport; when associated with T-1243. Increases doxorubicin inhibition. Ref.2
Mutagenesis11011S → N: 50% increase of estradiol glucuronide transport. Ref.2
Mutagenesis11061V → C: No effect on estradiol glucuronide transport. Ref.2
Mutagenesis12431A → T: 7.6-fold increase of the estradiol glucuronide transport; when associated with E-1090. Ref.2
Sequence conflict41S → R in AAN86532. Ref.1
Sequence conflict41S → R in AAO44983. Ref.4
Sequence conflict4801F → S in AAO44983. Ref.4
Sequence conflict8201N → S in CAB97204. Ref.5
Sequence conflict8681R → P in CAB97204. Ref.5
Sequence conflict9161S → G in CAB97204. Ref.5
Sequence conflict11221P → T in CAB97204. Ref.5
Sequence conflict13821S → P in AAN86532. Ref.1
Sequence conflict14731I → V in AAN86532. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 2E6939F63F5A3F68

FASTA1,532171,493
        10         20         30         40         50         60 
MALSSFCSSD GSDPLWDWNV TWHTSNPDFT KCFQNTVLTW VPCFYLWSCF PLYFLYLSRH 

        70         80         90        100        110        120 
DRGYIQMTHL NKAKTALGFF LWIICWADLF YSFWERSQGM LLAPVLLVSP TLLGITMLLA 

       130        140        150        160        170        180 
TFLIQFERRK GVQSSGIMLT FWLVALLCAL AILRSKIISA LKKDAQVDMF RDSAFYLYFT 

       190        200        210        220        230        240 
LVFIQLVLSC FSDSSPLFSE TVRDPNPCPE SSASFLSRIT FWWITGMMVQ GYRQPLKSSD 

       250        260        270        280        290        300 
LWSLNKEDTS EEVVPVLVNN WKKECVKSRK QPVRIVYAPP KDPTKPKGSS QLDVNEEVEA 

       310        320        330        340        350        360 
LIVKSSHKDR DPSLFKVLYK TFGPYFLMSF LYKALHDLMM FAGPEILELI INFVNDREAP 

       370        380        390        400        410        420 
DWQGYLYTAL LFVSACLQTL ALHQYFHICF VTGMRIKTAV VGAVYRKALV ITNSARKSST 

       430        440        450        460        470        480 
VGEIVNLMSV DAQRFMDLAT YINMIWSAPL QVTLALYFLW LNLGPSVLAG VAVMILMVPF 

       490        500        510        520        530        540 
NAVMAMKTKT YQVAHMKSKD NRIKLMNEIL NGIKVLKLYA WELAFQDKVM NIRQEELKVL 

       550        560        570        580        590        600 
KKSAYLAAVG TFTWVCTPFL VALSTFAVFV TVDEKNILDA KKAFVSLALF NILRFPLNIL 

       610        620        630        640        650        660 
PMVISSIVQA SVSLKRLRIF LSHEELEPDS IERWSIKDGG GMNSITVKNA TFTWARDEPP 

       670        680        690        700        710        720 
TLNGITFAIP DGALVAVVGQ VGCGKSSLLS ALLAEMDKVE GHVTLKGSVA YVPQQAWIQN 

       730        740        750        760        770        780 
DSLRENILFG RPLQEHCYKA VMEACALLPD LEILPSGDLT EIGEKGVNLS GGQKQRVSLA 

       790        800        810        820        830        840 
RAVYCNSDIY LLDDPLSAVD AHVGKHIFEK VVGPMGLLKN KTRILVTHGI SYLPQVDVII 

       850        860        870        880        890        900 
VMSGGKISEM GSYQELLDRD GAFAEFVRTY ANTEQDLASE DDSKNGVSGL GKESKPVENG 

       910        920        930        940        950        960 
ILVTDAVGKP LQRHLSNSSS HSVVTNQQHS STAELQKSGV KEETWKLMEA DKAQTGQVKL 

       970        980        990       1000       1010       1020 
SVYWNYMKAI GLCISFLSIF LFLCNHVSAL ASNYWLSLWT DDRPAVNGTQ ENRNFRLSVY 

      1030       1040       1050       1060       1070       1080 
GALGILQGVA VFGYSMAVSI GGIFASRRLH LDLLQNVLRS PMSFFERTPS GNLVNRFSKE 

      1090       1100       1110       1120       1130       1140 
LDTVDSMIPQ VIKMFMGSLF SVIGAVIIIL LATPIAAVII PPLGLVYFFV QRFYVASSRQ 

      1150       1160       1170       1180       1190       1200 
LKRLESVSRS PVYSHFNETL LGVSVIRAFE EQERFIRQSD LKVDENQKAY YPSIVANRWL 

      1210       1220       1230       1240       1250       1260 
AVRLECVGNC IVLFAALFAV ISRHSLSAGL VGLSVSYSLQ ITAYLNWLVR MSSEMETNIV 

      1270       1280       1290       1300       1310       1320 
AVERLKEYSE TEKEASWQIQ ETAPPSTWPH SGRVEFRDYC LRYREDLDLV LKHINVTIEG 

      1330       1340       1350       1360       1370       1380 
GEKVGIVGRT GAGKSSLTLG LFRINESAEG EIIIDGINIA KIGLHNLRFK ITIIPQDPVL 

      1390       1400       1410       1420       1430       1440 
FSGSLRMNLD PFSQYSDEEV WMALELAHLK GFVSALPDKL NHECAEGGEN LSVGQRQLVC 

      1450       1460       1470       1480       1490       1500 
LARALLRKTK ILVLDEATAA VDLETDDLIQ STIRTQFEDS TVLTIAHRLN TIMDYTRVIV 

      1510       1520       1530 
LDKGEIRECG APSELLQQRG VFYSMAKDAG LV 

« Hide

Isoform 2 [UniParc].

Checksum: 15FB4E9C99B7B9AC
Show »

FASTA1,523170,496

References

[1]"Cloning and characterization of the rat multidrug resistance-associated protein 1."
Yang Z., Li C.S.W., Shen D.D., Ho R.J.Y.
AAPS PharmSci 4:E15-E15(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Molecular cloning and pharmacological characterization of rat multidrug resistance protein 1 (mrp1)."
Nunoya K., Grant C.E., Zhang D.-W., Cole S.P.C., Deeley R.G.
Drug Metab. Dispos. 31:1016-1026(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF LEU-983; GLN-1090; SER-1101; VAL-1106 AND ALA-1243.
Strain: Sprague-Dawley.
Tissue: Skeletal muscle.
[3]Yabuuchi H., Takayanagi S., Ishikawa T.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Spleen.
[4]Takayanagi S., Ishikawa T.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: Sprague-Dawley.
Tissue: Spleen.
[5]"The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress."
Hirrlinger J., Koenig J., Keppler D., Lindenau J., Schulz J.B., Dringen R.
J. Neurochem. 76:627-636(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 711-1532 (ISOFORM 1).
[6]"cDNA cloning of the hepatocyte canalicular isoform of the multidrug resistance protein, cMrp, reveals a novel conjugate export pump deficient in hyperbilirubinemic mutant rats."
Buechler M., Koenig J., Brom M., Kartenbeck J., Spring H., Horie T., Keppler D.
J. Biol. Chem. 271:15091-15098(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1426-1532 (ISOFORMS 1/2).
[7]"Multidrug resistance protein 1-mediated transport of saquinavir by microglia."
Dallas S., Ronaldson P.T., Bendayan M., Bendayan R.
NeuroReport 15:1183-1186(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY170916 mRNA. Translation: AAN86532.1.
AF487549 mRNA. Translation: AAO85437.1.
AY174892 mRNA. Translation: AAO44983.1.
AJ277881 mRNA. Translation: CAB97204.1.
X96394 mRNA. Translation: CAA65258.1.
RefSeqNP_071617.2. NM_022281.2.
UniGeneRn.10495.

3D structure databases

ProteinModelPortalQ8CG09.
SMRQ8CG09. Positions 643-872.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000045518.

Chemistry

ChEMBLCHEMBL5680.

PTM databases

PhosphoSiteQ8CG09.

Proteomic databases

PaxDbQ8CG09.
PRIDEQ8CG09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24565.
KEGGrno:24565.
UCSCRGD:3112. rat. [Q8CG09-1]

Organism-specific databases

CTD4363.
RGD3112. Abcc1.

Phylogenomic databases

eggNOGCOG1132.
HOVERGENHBG108314.
KOK05665.
PhylomeDBQ8CG09.

Gene expression databases

GenevestigatorQ8CG09.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR001140. ABC_transptr_TM_dom.
IPR018170. Aldo/ket_reductase_CS.
IPR005292. Multidrug-R_assoc.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 2 hits.
TIGRFAMsTIGR00957. MRP_assoc_pro. 1 hit.
PROSITEPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603696.
PROQ8CG09.

Entry information

Entry nameMRP1_RAT
AccessionPrimary (citable) accession number: Q8CG09
Secondary accession number(s): Q63346 expand/collapse secondary AC list , Q810E4, Q810G9, Q9JHS0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families