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3.A.1.208.9
Canicular multispecific organic anion MDR transporter, MRP3 (also called ABCC3) (most similar in sequence to MRP2). MRP3 exports epipodophyllotoxins, etoposide and teniposide, estradiol 17-β-D-glucuronide, leukotriene C4, dinitrophenyl S-glutathione, epoposide glucuronide, methotrexate, bilirubin-glucuronides, bile acids, GSH-X (LTC4, DNP-SG) and sulfate-X (taurolithocholate-3-sulfate).  Substrate translocation and stimulated ATP hydrolysis show positive cooperativity (Hill coefficient = 2) and are half-coupled (Seelheim et al. 2012).  ABCC3 is overexpressed in various types of cancer including carcinogenic stem cells, and plays a role in liver cancer progression (Carrasco-Torres et al. 2015).

Accession Number:O15438
Protein Name:MRP3 aka ABCC3 aka CMOAT2 aka MLP2
Length:1527
Molecular Weight:169343.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:17
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate Canicular organoanions, epipodophyllotoxins, etoposide, teniposide, estradiol 17-beta-D-glucuronide, Leukotriene C4, epoposide glucuronide, methotrexate, bilirubin-glucuronides, bile acids, GSH-X, Sulfate-X

Cross database links:

Genevestigator: O15438
eggNOG: prNOG10663
RefSeq: NP_001137542.1    NP_003777.2   
Entrez Gene ID: 8714   
Pfam: PF00664    PF00005   
OMIM: 604323  gene

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:0008514 F:organic anion transmembrane transporter act...
GO:0055085 P:transmembrane transport

References (9)

[1] “Isolation of a novel human canalicular multispecific organic anion transporter, cMOAT2/MRP3, and its expression in cisplatin-resistant cancer cells with decreased ATP-dependent drug transport.”  Uchiumi T.et.al.   9813153
[2] “cDNA cloning and inducible expression of human multidrug resistance associated protein 3 (MRP3).”  Kiuchi Y.et.al.   9738950
[3] “Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT subfamily of transporter proteins.”  Belinsky M.G.et.al.   9827529
[4] “Human MRP3 transporter: identification of the 5'-flanking region, genomic organization and alternative splice variants.”  Fromm M.F.et.al.   9889399
[5] “Characterization of the human multidrug resistance protein isoform MRP3 localized to the basolateral hepatocyte membrane.”  Koenig J.et.al.   10094960
[6] “DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.”  Zody M.C.et.al.   16625196
[7] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[8] “Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines.”  Kool M.et.al.   9270026
[9] “An unappreciated role for RNA surveillance.”  Hillman R.T.et.al.   14759258

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MDALCGSGEL GSKFWDSNLS VHTENPDLTP CFQNSLLAWV PCIYLWVALP CYLLYLRHHC 
61:	RGYIILSHLS KLKMVLGVLL WCVSWADLFY SFHGLVHGRA PAPVFFVTPL VVGVTMLLAT 
121:	LLIQYERLQG VQSSGVLIIF WFLCVVCAIV PFRSKILLAK AEGEISDPFR FTTFYIHFAL 
181:	VLSALILACF REKPPFFSAK NVDPNPYPET SAGFLSRLFF WWFTKMAIYG YRHPLEEKDL 
241:	WSLKEEDRSQ MVVQQLLEAW RKQEKQTARH KASAAPGKNA SGEDEVLLGA RPRPRKPSFL 
301:	KALLATFGSS FLISACFKLI QDLLSFINPQ LLSILIRFIS NPMAPSWWGF LVAGLMFLCS 
361:	MMQSLILQHY YHYIFVTGVK FRTGIMGVIY RKALVITNSV KRASTVGEIV NLMSVDAQRF 
421:	MDLAPFLNLL WSAPLQIILA IYFLWQNLGP SVLAGVAFMV LLIPLNGAVA VKMRAFQVKQ 
481:	MKLKDSRIKL MSEILNGIKV LKLYAWEPSF LKQVEGIRQG ELQLLRTAAY LHTTTTFTWM 
541:	CSPFLVTLIT LWVYVYVDPN NVLDAEKAFV SVSLFNILRL PLNMLPQLIS NLTQASVSLK 
601:	RIQQFLSQEE LDPQSVERKT ISPGYAITIH SGTFTWAQDL PPTLHSLDIQ VPKGALVAVV 
661:	GPVGCGKSSL VSALLGEMEK LEGKVHMKGS VAYVPQQAWI QNCTLQENVL FGKALNPKRY 
721:	QQTLEACALL ADLEMLPGGD QTEIGEKGIN LSGGQRQRVS LARAVYSDAD IFLLDDPLSA 
781:	VDSHVAKHIF DHVIGPEGVL AGKTRVLVTH GISFLPQTDF IIVLADGQVS EMGPYPALLQ 
841:	RNGSFANFLC NYAPDEDQGH LEDSWTALEG AEDKEALLIE DTLSNHTDLT DNDPVTYVVQ 
901:	KQFMRQLSAL SSDGEGQGRP VPRRHLGPSE KVQVTEAKAD GALTQEEKAA IGTVELSVFW 
961:	DYAKAVGLCT TLAICLLYVG QSAAAIGANV WLSAWTNDAM ADSRQNNTSL RLGVYAALGI 
1021:	LQGFLVMLAA MAMAAGGIQA ARVLHQALLH NKIRSPQSFF DTTPSGRILN CFSKDIYVVD 
1081:	EVLAPVILML LNSFFNAIST LVVIMASTPL FTVVILPLAV LYTLVQRFYA ATSRQLKRLE 
1141:	SVSRSPIYSH FSETVTGASV IRAYNRSRDF EIISDTKVDA NQRSCYPYII SNRWLSIGVE 
1201:	FVGNCVVLFA ALFAVIGRSS LNPGLVGLSV SYSLQVTFAL NWMIRMMSDL ESNIVAVERV 
1261:	KEYSKTETEA PWVVEGSRPP EGWPPRGEVE FRNYSVRYRP GLDLVLRDLS LHVHGGEKVG 
1321:	IVGRTGAGKS SMTLCLFRIL EAAKGEIRID GLNVADIGLH DLRSQLTIIP QDPILFSGTL 
1381:	RMNLDPFGSY SEEDIWWALE LSHLHTFVSS QPAGLDFQCS EGGENLSVGQ RQLVCLARAL 
1441:	LRKSRILVLD EATAAIDLET DNLIQATIRT QFDTCTVLTI AHRLNTIMDY TRVLVLDKGV 
1501:	VAEFDSPANL IAARGIFYGM ARDAGLA