MRP4_RAT
ID MRP4_RAT Reviewed; 1325 AA.
AC F1M3J4; Q6QMG6;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 3.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=ATP-binding cassette subfamily C member 4;
DE EC=7.6.2.- {ECO:0000250|UniProtKB:O15439};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:O15439};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:O15439};
DE AltName: Full=Multidrug resistance-associated protein 4;
GN Name=Abcc4 {ECO:0000312|RGD:620266};
GN Synonyms=Mrp4 {ECO:0000303|PubMed:15047146};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=15047146; DOI=10.1016/j.bbrc.2004.03.014;
RA Chen C., Klaassen C.D.;
RT "Rat multidrug resistance protein 4 (Mrp4, Abcc4): molecular cloning, organ
RT distribution, postnatal renal expression, and chemical inducibility.";
RL Biochem. Biophys. Res. Commun. 317:46-53(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=12883481; DOI=10.1053/jhep.2003.50331;
RA Rius M., Nies A.T., Hummel-Eisenbeiss J., Jedlitschky G., Keppler D.;
RT "Cotransport of reduced glutathione with bile salts by MRP4 (ABCC4)
RT localized to the basolateral hepatocyte membrane.";
RL Hepatology 38:374-384(2003).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that actively extrudes physiological compounds and xenobiotics
CC from cells. Transports a range of endogenous molecules that have a key
CC role in cellular communication and signaling, including cyclic
CC nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile
CC acids, steroid conjugates, urate, and prostaglandins. Mediates also the
CC ATP-dependent efflux of glutathione conjugates such as leukotriene C4
CC (LTC4) and leukotriene B4 (LTB4). The presence of GSH is necessary for
CC the ATP-dependent transport of LTB4, whereas GSH is not required for
CC the transport of LTC4. Mediates the cotransport of bile acids with
CC reduced glutathione (GSH). Transports a wide range of drugs and their
CC metabolites, including anticancer, antiviral and antibiotics molecules.
CC {ECO:0000250|UniProtKB:O15439}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:O15439};
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:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:O15439};
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:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP +
CC dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365;
CC Evidence={ECO:0000250|UniProtKB:O15439};
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:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene B4(in) = ADP + H(+) + leukotriene
CC B4(out) + phosphate; Xref=Rhea:RHEA:66424, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57461, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + urate(in) = ADP + H(+) + phosphate + urate(out);
CC Xref=Rhea:RHEA:16461, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17775, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16462;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic GMP(in) + ATP + H2O = 3',5'-cyclic GMP(out) + ADP
CC + H(+) + phosphate; Xref=Rhea:RHEA:66188, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57746, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66189;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP(in) + ATP + H2O = 3',5'-cyclic AMP(out) + ADP
CC + H(+) + phosphate; Xref=Rhea:RHEA:66184, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58165, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66185;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + prostaglandin E2(in) = ADP + H(+) + phosphate +
CC prostaglandin E2(out); Xref=Rhea:RHEA:66388, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216, ChEBI:CHEBI:606564;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66389;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + prostaglandin E1(in) = ADP + H(+) + phosphate +
CC prostaglandin E1(out); Xref=Rhea:RHEA:66392, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57397, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66393;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione(in) + glycodeoxycholate(in) + H2O = ADP +
CC glutathione(out) + glycodeoxycholate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:66380, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:82982, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66381;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholate(in) + glutathione(in) + H2O = ADP + cholate(out)
CC + glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:66396,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66397;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione(in) + glycocholate(in) + H2O = ADP +
CC glutathione(out) + glycocholate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:66400, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66401;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione(in) + H2O + taurocholate(in) = ADP +
CC glutathione(out) + H(+) + phosphate + taurocholate(out);
CC Xref=Rhea:RHEA:66404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66405;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione(in) + glycochenodeoxycholate(in) + H2O = ADP
CC + glutathione(out) + glycochenodeoxycholate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:66408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:36252, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66409;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione(in) + H2O + taurochenodeoxycholate(in) = ADP
CC + glutathione(out) + H(+) + phosphate + taurochenodeoxycholate(out);
CC Xref=Rhea:RHEA:66412, ChEBI:CHEBI:9407, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66413;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione(in) + glycoursodeoxycholate(in) + H2O = ADP
CC + glutathione(out) + glycoursodeoxycholate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:66416, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132030, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66417;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glutathione(in) + H2O + tauroursodeoxycholate(in) = ADP
CC + glutathione(out) + H(+) + phosphate + tauroursodeoxycholate(out);
CC Xref=Rhea:RHEA:66420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:132028, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66421;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O15439};
CC -!- SUBUNIT: Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain);
CC this interaction accelerates MRP4 internalization.
CC {ECO:0000250|UniProtKB:O15439}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:12883481}; Multi-pass membrane protein
CC {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O15439};
CC Multi-pass membrane protein {ECO:0000255}. Note=Its localization to the
CC basolateral or apical membranes is tissue-dependent.
CC {ECO:0000250|UniProtKB:O15439}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with high levels in kidney.
CC {ECO:0000269|PubMed:15047146}.
CC -!- PTM: N-glycosylated; leading to substrate-selective effects on its
CC transport activity. {ECO:0000250|UniProtKB:O15439}.
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DR EMBL; AY533524; AAS78928.1; -; mRNA.
DR EMBL; AABR07019392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07019393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07019394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07019395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_596902.1; NM_133411.1.
DR AlphaFoldDB; F1M3J4; -.
DR SMR; F1M3J4; -.
DR STRING; 10116.ENSRNOP00000033826; -.
DR ChEMBL; CHEMBL2073711; -.
DR iPTMnet; Q6QMG6; -.
DR jPOST; F1M3J4; -.
DR PaxDb; F1M3J4; -.
DR PeptideAtlas; F1M3J4; -.
DR PRIDE; F1M3J4; -.
DR GeneID; 170924; -.
DR KEGG; rno:170924; -.
DR CTD; 10257; -.
DR RGD; 620266; Abcc4.
DR VEuPathDB; HostDB:ENSRNOG00000010064; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; F1M3J4; -.
DR OMA; PWYLLNT; -.
DR OrthoDB; 138195at2759; -.
DR TreeFam; TF105202; -.
DR BRENDA; 7.6.2.3; 5301.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-9748787; Azathioprine ADME.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000010064; Expressed in adult mammalian kidney and 18 other tissues.
DR ExpressionAtlas; F1M3J4; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0098591; C:external side of apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0031088; C:platelet dense granule membrane; ISO:RGD.
DR GO; GO:0015432; F:ABC-type bile acid transporter activity; ISS:UniProtKB.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISS:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:RGD.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0001409; F:guanine nucleotide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015132; F:prostaglandin transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015216; F:purine nucleotide transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015143; F:urate transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015721; P:bile acid and bile salt transport; ISS:UniProtKB.
DR GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR GO; GO:0070730; P:cAMP transport; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0140115; P:export across plasma membrane; ISO:RGD.
DR GO; GO:0071716; P:leukotriene transport; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0032310; P:prostaglandin secretion; ISO:RGD.
DR GO; GO:0015732; P:prostaglandin transport; ISS:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0015747; P:urate transport; ISS:UniProtKB.
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; IPR030240; ABCC4.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24223:SF357; PTHR24223:SF357; 1.
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 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 ATP-binding; Cell membrane; Lipid transport; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1325
FT /note="ATP-binding cassette subfamily C member 4"
FT /id="PRO_0000452320"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 710..730
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 761..781
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 954..974
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 977..997
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT DOMAIN 93..377
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 410..633
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 715..1005
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1041..1274
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 658..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 445..452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1075..1082
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 273
FT /note="I -> F (in Ref. 1; AAS78928)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="A -> S (in Ref. 1; AAS78928)"
FT /evidence="ECO:0000305"
FT CONFLICT 517
FT /note="F -> L (in Ref. 1; AAS78928)"
FT /evidence="ECO:0000305"
FT CONFLICT 525..526
FT /note="RL -> LT (in Ref. 1; AAS78928)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="R -> T (in Ref. 1; AAS78928)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="T -> R (in Ref. 1; AAS78928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1325 AA; 148904 MW; F9DBE9399C1502FE CRC64;
MLPVHTEVKP NPLQDANLCS RLFFWWLNPL FKAGHKRRLE EDDMFSVLPE DRSKHLGEEL
QGYWDKEVLR AKKDARKPSL TKAIVKCYWK SYLILGIFTL IEETTRVVQP IFLGKIIDYF
EKYDSDDSAA LHTAYGYAAV LSLCTLILAI LHHLYFYHVQ CAGMRIRVAM CHMIYRKALR
LSNSAMGKTT TGQIVNLLSN DVNKFDQVTI FLHFLWAGPL QAIGVTILLW VEIGISCLAG
LAILVILLPL QSCIGKLFSS LRSKTAAFTD ARIRTMNEVI TGMRIIKMYA WEKSFADLIT
NLRKKEISKI LGSSYLRGMN MASFFIANKV ILFVTFTTYV LLGNKITASH VFVAMTLYGA
VRLTVTLFFP SAIERVSEAV VSVRRIKNFL LLDELPERKA QEPSDGKAIV HVQDFTAFWD
KALDTPTLQG LSFTARPGEL LAVVGPVGAG KSSLLSAVLG ELPPTSGLVS VHGRIAYVSQ
QPWVFSGTVR SNILFGRKYE KERYEKVIKA CALKKDFQLL EDGDRLVIGD RGARLSGGQK
ARVNLATAVY QDADIYLLDD PLSAVDAEVG KHLFQLCICQ TLHEKITILV THQLQYLKAA
SHILILKDGE MVQKGTYTEF LKSGVDFGSL LKKENEEAEP SPVPGTPTLR NRTFSEASIW
SQQSSRPSLK DGVPDAQDAE NTQAAQPEES RSEGRIGFKA YKNYFSAGAS WFFIIFLVLL
NLMGQVFYVL QDWWLSHWAN RQGALNDTKN ANGNVTGTLD LSWYLGIYTG LTAVTVLFGI
ARSLLVFYVL VNASQTLHNR MFESILKAPV LFFDRNPIGR ILNRFSKDIG HMDDLLPLTF
LDFIQTLLLV VSVIAVAAAV IPWILIPLVP LSIIFVVLRR YFLETSRDVK RLESTTRSPV
FSHLSSSLQG LWTIRAYKAE ERCQELFDAH QDLHSEAWFL FLTTSRWFAV RLDAICAVFV
IVVAFGSLVL AKTLDAGQVG LALSYSLTLM GMFQWSVRQS AEVENMMISV ERVIEYTDLE
KEAPWECRKR PPPGWPHEGV IVFDNVNFTY SLDGPLVLKH LTALIKSREK VGIVGRTGAG
KSSLISALFR LSEPEGKIWI DKILTTEIGL HDLRKKMSII PQEPVLFTGT MRKNLDPFNE
HSDEELWKAL EEVQLKEAIE DLPGKMDTEL AESGSNFSVG QRQLVCLARA ILKKNRILII
DEATANVDPR TDELIQQKIR EKFAQCTVLT IAHRLNTIID SDKIMVLDSG RLREYDEPYV
LLQNPESLFY KMVQQLGKGE AAALTETAKQ VYFRRNYPDI AFSSPAVMST SNGQPSALTI
FETAL
