MRP1_CHICK
ID MRP1_CHICK Reviewed; 1525 AA.
AC Q5F364;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Multidrug resistance-associated protein 1 {ECO:0000250|UniProtKB:P33527};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:P33527};
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:0000250|UniProtKB:O35379}; Synonyms=MRP1;
GN ORFNames=RCJMB04_32d20;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Mediates ATP-dependent export of organic anions and drugs
CC from the cytoplasm. Confers resistance to anticancer drugs. Hydrolyzes
CC ATP with low efficiency (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Mediates export of organic anions and drugs from the
CC cytoplasm. Mediates ATP-dependent transport of glutathione and
CC glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide
CC and other xenobiotics. Hydrolyzes ATP with low efficiency.
CC {ECO:0000250|UniProtKB:O35379, ECO:0000250|UniProtKB:P33527}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:P33527};
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:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
CC Evidence={ECO:0000250|UniProtKB:P33527};
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:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:P33527};
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:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P33527};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P33527,
CC ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AJ851786; CAH65420.1; -; mRNA.
DR RefSeq; NP_001012540.1; NM_001012522.1.
DR AlphaFoldDB; Q5F364; -.
DR SMR; Q5F364; -.
DR STRING; 9031.ENSGALP00000010735; -.
DR PaxDb; Q5F364; -.
DR GeneID; 395416; -.
DR KEGG; gga:395416; -.
DR CTD; 4363; -.
DR VEuPathDB; HostDB:geneid_395416; -.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; Q5F364; -.
DR PhylomeDB; Q5F364; -.
DR PRO; PR:Q5F364; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0034775; P:glutathione transmembrane transport; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042908; P:xenobiotic transport; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Hydrolase; Lipid transport; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1525
FT /note="Multidrug resistance-associated protein 1"
FT /id="PRO_0000093355"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 55..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 96..100
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 122..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 155..172
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 173..193
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 194..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 316..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 337..362
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 363..383
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 384..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 440..460
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 461..463
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 464..484
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 485..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 547..567
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 568..589
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 590..610
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 611..961
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 962..982
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 983..1019
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1020..1040
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1041..1083
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1084..1104
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1105
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1106..1126
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1127..1197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1198..1218
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1219..1220
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1221..1241
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1242..1525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 324..607
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 641..865
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 969..1250
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1289..1521
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 871..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 675..682
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1321..1328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 1525 AA; 170972 MW; 38724B6711B878FD CRC64;
MGIESLCSAD ASEPFWDWNL TWHTENPDFT QCFQNTVLVW VPCIYLWVCF PAYFLYLRSH
DRGYIQMSIL NKAKTALGLI LWIVCWADLF YSFWERSQNI FRAPFFLISP TVLGITMLLA
TFLIQHERLK GVQSSGVMMI FWLISLLCAT VIFRSKIMLA LNTDTEVDAF RYVTFCTYFI
LLLVQLILSC FPEKPPLFSE AVNDPKPCPE FSASFLSRIT FWWITGLMIQ GHRRPLEAKD
LWSLNKEDTS EEIVPGLAKN WAKEWAKTKR QPLNMLYSSK KQQKSSDSNG EVMEEAEALI
IKPSQRSSEA SLSKVLYKTF GPYFLMSFLF KAAHDLLMFT GPEILKLLIN FVNNKSAPNW
QGYFYTGLLF VCACLQTLIL HQYFHICFVT GMRLKTAIVG VIYRKALVIT NSARKTSTVG
EIVNLMSVDA QRFMDLATYI NMIWSAPLQV ILALYLLWRN LGPSVLAGVA VMILLVPINA
VMAMKTKTYQ VAQMKSKDNR IKLMNEILNG IKVLKLYAWE LAFREKVLEI RQKELKVLKK
SAYLAAMGTF TWVCAPFLVA LSTFAVYVKV NKNNILDAQK AFVSLALFNI LRFPLNILPM
VISSIVEASV SLKRLRVFLS HEELDPDSII RGPITNAEGS IVVKNATFSW SKTDPPSLNS
INFTVPEGSL IAVVGQVGCG KSSLLSALLG EMDKKEGYVV VKGSIAYVPQ QAWIQNATLE
DNIIFGREMN ESRYKRVIEA CALLPDLEIL PMGDRTEIGE KGVNLSGGQK QRVSLARAVY
CNADTYLFDD PLSAVDAHVG KHIFEKVIGP KGILKNKTRV LVTHAVNYLP QMDTILVMTD
GEISEMGSYQ ELLKQDGAFA EFLRTYANAE QSMESSDASS PSGKEGKPVE NGVLVNDATG
KLMHRQLSNS STYSRETGKS QHQSSTAELQ KPLAEKNSWK LTEADTAKTG RVKATVYWEY
MKAIGLYISF LSVFLFMCNH IASLASNYWL SLWTDDPVVN GTQQYTNVRL GVYGALGISQ
GIAVFGYSMA VSIGGIFASR HLHLDLLHNV LRSPMSFFER TPSGNLVSRF SKEIDTIDST
IPPIIKMFMG STFNVIGACI IILLATPIAA VVIPPLGLVY LLVQRFYVAT SRQLKRLESV
SRSPVYSHFN ETLLGVSVIR AFEEQKRFIK QNDMKVDENQ KAYYPSIVAN RWLAVRLEFV
GNCIVLFAAL FAVIARNKLS PGLIGLSVSY SLQITAYLNW LVRMTSDLET NIVAVERVKE
YAEMEKEAEW SIEETAPAST WPQEGKVEFR GFGLRYREDL DLVLKNINIT INGGEKVGIV
GRTGAGKSSL TLGLFRINEA AEGEIIIDGI NIAKIGLHDL RFKITIIPQD PILFSGSLRM
NLDPFDQHSD EDIWRSLELA HLKNFVSSLP DKLNHECSEG GENLSVGQRQ LVCLARALLR
KSKILVLDEA TAAVDLETDN LIQSTIKSQF EECTVLTIAH RLNTIMDYTR VLVLDRGEVV
ECDSPDNLLQ AKGLFYSMAK DSGLA
