ID MRP3_HUMAN Reviewed; 1527 AA. AC O15438; B2RPA9; D3DTX9; O60265; O60922; O75621; O95078; O95289; O95290; AC Q86X85; Q9UN52; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 27-MAR-2024, entry version 209. DE RecName: Full=ATP-binding cassette sub-family C member 3; DE EC=7.6.2.- {ECO:0000269|PubMed:11581266, ECO:0000269|PubMed:15083066}; DE EC=7.6.2.2 {ECO:0000269|PubMed:10359813, ECO:0000269|PubMed:11581266, ECO:0000269|PubMed:9827529}; DE EC=7.6.2.3 {ECO:0000269|PubMed:11581266, ECO:0000269|PubMed:15083066, ECO:0000269|PubMed:9827529}; DE AltName: Full=Canalicular multispecific organic anion transporter 2 {ECO:0000303|PubMed:9813153}; DE AltName: Full=Multi-specific organic anion transporter D {ECO:0000303|PubMed:9827529}; DE Short=MOAT-D {ECO:0000303|PubMed:9827529}; DE AltName: Full=Multidrug resistance-associated protein 3; GN Name=ABCC3 {ECO:0000312|HGNC:HGNC:54}; Synonyms=CMOAT2, MLP2, MRP3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=9813153; DOI=10.1006/bbrc.1998.9546; RA Uchiumi T., Hinoshita E., Haga S., Nakamura T., Tanaka T., Toh S., RA Furukawa M., Kawabe T., Wada M., Kagotani K., Okumura K., Kohno K., RA Akiyama S., Kuwano M.; RT "Isolation of a novel human canalicular multispecific organic anion RT transporter, cMOAT2/MRP3, and its expression in cisplatin-resistant cancer RT cells with decreased ATP-dependent drug transport."; RL Biochem. Biophys. Res. Commun. 252:103-110(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=9738950; DOI=10.1016/s0014-5793(98)00899-0; RA Kiuchi Y., Suzuki H., Hirohashi T., Tyson C.A., Sugiyama Y.; RT "cDNA cloning and inducible expression of human multidrug resistance RT associated protein 3 (MRP3)."; RL FEBS Lett. 433:149-152(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9827529; DOI=10.1093/jnci/90.22.1735; RA Belinsky M.G., Bain L.J., Balsara B.B., Testa J.R., Kruh G.D.; RT "Characterization of MOAT-C and MOAT-D, new members of the MRP/cMOAT RT subfamily of transporter proteins."; RL J. Natl. Cancer Inst. 90:1735-1741(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Liver; RX PubMed=9889399; DOI=10.1016/s0005-2736(98)00233-8; RA Fromm M.F., Leake B., Roden D.M., Wilkinson G.R., Kim R.B.; RT "Human MRP3 transporter: identification of the 5'-flanking region, genomic RT organization and alternative splice variants."; RL Biochim. Biophys. Acta 1415:369-374(1999). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND INDUCTION. RC TISSUE=Liver; RX PubMed=10094960; DOI=10.1002/hep.510290404; RA Koenig J., Rost D., Cui Y., Keppler D.; RT "Characterization of the human multidrug resistance protein isoform MRP3 RT localized to the basolateral hepatocyte membrane."; RL Hepatology 29:1156-1163(1999). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND RP SUBCELLULAR LOCATION. RX PubMed=10359813; DOI=10.1073/pnas.96.12.6914; RA Kool M., van der Linden M., de Haas M., Scheffer G.L., de Vree J.M., RA Smith A.J., Jansen G., Peters G.J., Ponne N., Scheper R.J., Elferink R.P., RA Baas F., Borst P.; RT "MRP3, an organic anion transporter able to transport anti-cancer drugs."; RL Proc. Natl. Acad. Sci. U.S.A. 96:6914-6919(1999). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Colon carcinoma; RA Auclair D., Alonso E., Chen L.B.; RT "Identification of a novel splice variant of MRP3 involved in resistance to RT DNA damaging agents."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5). RC TISSUE=Blood; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1043-1527 (ISOFORM 1). RC TISSUE=Liver; RX PubMed=9270026; RA Kool M., de Haas M., Scheffer G.L., Scheper R.J., van Eijk M.J., RA Juijn J.A., Baas F., Borst P.; RT "Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues RT of the multidrug resistance-associated protein gene (MRP1), in human cancer RT cell lines."; RL Cancer Res. 57:3537-3547(1997). RN [12] RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=11581266; DOI=10.1074/jbc.m107041200; RA Zelcer N., Saeki T., Reid G., Beijnen J.H., Borst P.; RT "Characterization of drug transport by the human multidrug resistance RT protein 3 (ABCC3)."; RL J. Biol. Chem. 276:46400-46407(2001). RN [13] RP FUNCTION, CATALYTIC ACTIVITY, VARIANTS GLN-548 AND HIS-1297, RP CHARACTERIZATION OF VARIANT HIS-1297, SUBCELLULAR LOCATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15083066; DOI=10.1097/00008571-200404000-00001; RA Lee Y.M., Cui Y., Koenig J., Risch A., Jaeger B., Drings P., Bartsch H., RA Keppler D., Nies A.T.; RT "Identification and functional characterization of the natural variant RT MRP3-Arg1297His of human multidrug resistance protein 3 (MRP3/ABCC3)."; RL Pharmacogenetics 14:213-223(2004). RN [14] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908 AND SER-911, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-908, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=28408210; DOI=10.1016/j.xphs.2017.04.001; RA Keiser M., Kaltheuner L., Wildberg C., Mueller J., Grube M., Partecke L.I., RA Heidecke C.D., Oswald S.; RT "The Organic Anion-Transporting Peptide 2B1 Is Localized in the Basolateral RT Membrane of the Human Jejunum and Caco-2 Monolayers."; RL J. Pharm. Sci. 106:2657-2663(2017). RN [19] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=35307651; DOI=10.1124/dmd.121.000748; RA Hau R.K., Klein R.R., Wright S.H., Cherrington N.J.; RT "Localization of Xenobiotic Transporters Expressed at the Human Blood- RT Testis Barrier."; RL Drug Metab. Dispos. 50:770-780(2022). CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) CC family that binds and hydrolyzes ATP to enable active transport of CC various substrates including many drugs, toxicants and endogenous CC compound across cell membranes (PubMed:11581266, PubMed:15083066, CC PubMed:10359813). Transports glucuronide conjugates such as bilirubin CC diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such CC as leukotriene C4 (LTC4) (PubMed:15083066, PubMed:11581266). Transports CC also various bile salts (taurocholate, glycocholate, CC taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate) (By CC similarity). Does not contribute substantially to bile salt physiology CC but provides an alternative route for the export of bile acids and CC glucuronides from cholestatic hepatocytes (By similarity). May CC contribute to regulate the transport of organic compounds in testes CC across the blood-testis-barrier (Probable). Can confer resistance to CC various anticancer drugs, methotrexate, tenoposide and etoposide, by CC decreasing accumulation of these drugs in cells (PubMed:11581266, CC PubMed:10359813). {ECO:0000250|UniProtKB:O88563, CC ECO:0000269|PubMed:10359813, ECO:0000269|PubMed:11581266, CC ECO:0000269|PubMed:15083066, ECO:0000305|PubMed:35307651}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + CC taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:O88563}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053; CC Evidence={ECO:0000250|UniProtKB:O88563}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+) CC + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:O88563}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057; CC Evidence={ECO:0000250|UniProtKB:O88563}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) + CC phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216; CC Evidence={ECO:0000250|UniProtKB:O88563}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + taurochenodeoxycholate 3-sulfate(in) = ADP + H(+) CC + phosphate + taurochenodeoxycholate 3-sulfate(out); CC Xref=Rhea:RHEA:66176, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:166912, CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O88563}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66177; CC Evidence={ECO:0000250|UniProtKB:O88563}; 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:0000269|PubMed:11581266, ECO:0000269|PubMed:15083066, CC ECO:0000269|PubMed:9827529}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; CC Evidence={ECO:0000305|PubMed:11581266, ECO:0000305|PubMed:15083066}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate + CC xenobioticSide 2.; EC=7.6.2.2; Evidence={ECO:0000269|PubMed:10359813, CC ECO:0000269|PubMed:11581266, ECO:0000269|PubMed:9827529}; 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:0000269|PubMed:11581266, ECO:0000269|PubMed:15083066}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129; CC Evidence={ECO:0000305|PubMed:15083066}; 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:0000269|PubMed:15083066}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365; CC Evidence={ECO:0000305|PubMed:15083066}; 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:0000269|PubMed:11581266, ECO:0000269|PubMed:15083066}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; CC Evidence={ECO:0000305|PubMed:15083066}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + bilirubin-glucuronoside(in) + H2O = ADP + bilirubin- CC glucuronoside(out) + H(+) + phosphate; Xref=Rhea:RHEA:66180, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57767, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:15083066}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66181; CC Evidence={ECO:0000305|PubMed:15083066}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + bilirubin-bisglucuronoside(in) + H2O = ADP + bilirubin- CC bisglucuronoside(out) + H(+) + phosphate; Xref=Rhea:RHEA:66192, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58471, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:15083066}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66193; CC Evidence={ECO:0000305|PubMed:15083066}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=17.7 uM for oestradiol-17-(beta-D-glucuronide) CC {ECO:0000269|PubMed:11581266}; CC KM=24.2 uM for oestradiol-17-(beta-D-glucuronide) CC {ECO:0000269|PubMed:15083066}; CC KM=46.3 uM for dehydroepiandrosterone- 3-sulfate CC {ECO:0000269|PubMed:15083066}; CC Vmax=281 pmol/min/mg enzyme for dehydroepiandrosterone- 3-sulfate CC transport {ECO:0000269|PubMed:15083066}; CC Vmax=474 pmol/min/mg enzyme for oestradiol-17-(beta-D-glucuronide) CC transport {ECO:0000269|PubMed:11581266}; CC Vmax=71.5 pmol/min/mg enzyme for oestradiol-17-(beta-D-glucuronide) CC transport {ECO:0000269|PubMed:15083066}; CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane CC {ECO:0000269|PubMed:10094960, ECO:0000269|PubMed:10359813, CC ECO:0000269|PubMed:15083066, ECO:0000269|PubMed:28408210}; Multi-pass CC membrane protein {ECO:0000255}. Basal cell membrane CC {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein CC {ECO:0000255}. Note=Localized to the basolateral membrane of CC enterocytes (PubMed:28408210). Localized to the basal membrane of CC Sertoli cells (PubMed:35307651). {ECO:0000269|PubMed:28408210, CC ECO:0000269|PubMed:35307651}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=MRP3; CC IsoId=O15438-1; Sequence=Displayed; CC Name=2; Synonyms=MRP3A; CC IsoId=O15438-2; Sequence=VSP_000042; CC Name=3; Synonyms=MRP3B; CC IsoId=O15438-3; Sequence=VSP_000040, VSP_000041; CC Name=4; Synonyms=MRP3S1; CC IsoId=O15438-4; Sequence=VSP_043864; CC Name=5; CC IsoId=O15438-5; Sequence=VSP_039041, VSP_039042; CC -!- TISSUE SPECIFICITY: Mainly expressed in the liver. Also expressed in CC small intestine, colon, prostate, testis, brain and at a lower level in CC the kidney. In testis, localized to peritubular myoid cells, Leydig CC cells, along the basal membrane of Sertoli cells and moderately in the CC adluminal compartment of the seminiferous tubules (PubMed:35307651). CC {ECO:0000269|PubMed:10094960, ECO:0000269|PubMed:15083066, CC ECO:0000269|PubMed:28408210, ECO:0000269|PubMed:35307651, CC ECO:0000269|PubMed:9738950}. CC -!- INDUCTION: Strongly up-regulated under conditions of MRP2 deficiency. CC {ECO:0000269|PubMed:10094960}. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family. CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB71756.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAD01430.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAD38185.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF083552; AAC34668.1; -; mRNA. DR EMBL; AB010887; BAA28146.1; -; mRNA. DR EMBL; AF104943; AAD04170.1; -; mRNA. DR EMBL; AF085690; AAD02845.1; -; mRNA. DR EMBL; AF085691; AAD02846.1; -; mRNA. DR EMBL; AF085692; AAD02847.1; -; mRNA. DR EMBL; Y17151; CAA76658.2; -; mRNA. DR EMBL; AF009670; AAD01430.1; ALT_FRAME; mRNA. DR EMBL; AF154001; AAD38185.1; ALT_SEQ; mRNA. DR EMBL; AC004590; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471109; EAW94592.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94590.1; -; Genomic_DNA. DR EMBL; CH471109; EAW94593.1; -; Genomic_DNA. DR EMBL; BC046126; AAH46126.1; -; mRNA. DR EMBL; BC137347; AAI37348.1; -; mRNA. DR EMBL; BC137348; AAI37349.1; -; mRNA. DR EMBL; U83659; AAB71756.1; ALT_FRAME; mRNA. DR CCDS; CCDS32681.1; -. [O15438-1] DR CCDS; CCDS45739.1; -. [O15438-5] DR PIR; JE0336; JE0336. DR RefSeq; NP_001137542.1; NM_001144070.1. [O15438-5] DR RefSeq; NP_003777.2; NM_003786.3. [O15438-1] DR PDB; 8HVH; EM; 3.07 A; A=1-1527. DR PDB; 8HW2; EM; 3.65 A; A=1-1527. DR PDB; 8HW4; EM; 3.52 A; A=1-1527. DR PDBsum; 8HVH; -. DR PDBsum; 8HW2; -. DR PDBsum; 8HW4; -. DR AlphaFoldDB; O15438; -. DR EMDB; EMD-35043; -. DR EMDB; EMD-35049; -. DR EMDB; EMD-35050; -. DR SMR; O15438; -. DR BioGRID; 114255; 32. DR IntAct; O15438; 8. DR MINT; O15438; -. DR STRING; 9606.ENSP00000285238; -. DR BindingDB; O15438; -. DR ChEMBL; CHEMBL5918; -. DR DrugBank; DB15719; Belantamab mafodotin. DR DrugBank; DB11936; Bempedoic acid. DR DrugBank; DB02659; Cholic Acid. DR DrugBank; DB00515; Cisplatin. DR DrugBank; DB00286; Conjugated estrogens. DR DrugBank; DB05928; Dovitinib. DR DrugBank; DB00997; Doxorubicin. DR DrugBank; DB00773; Etoposide. DR DrugBank; DB00973; Ezetimibe. DR DrugBank; DB00950; Fexofenadine. DR DrugBank; DB00544; Fluorouracil. DR DrugBank; DB00158; Folic acid. DR DrugBank; DB08884; Gadoxetic acid. DR DrugBank; DB00143; Glutathione. DR DrugBank; DB01016; Glyburide. DR DrugBank; DB00328; Indomethacin. DR DrugBank; DB00709; Lamivudine. DR DrugBank; DB00563; Methotrexate. DR DrugBank; DB01011; Metyrapone. DR DrugBank; DB01115; Nifedipine. DR DrugBank; DB00338; Omeprazole. DR DrugBank; DB01174; Phenobarbital. DR DrugBank; DB06813; Pralatrexate. DR DrugBank; DB01032; Probenecid. DR DrugBank; DB01069; Promethazine. DR DrugBank; DB00481; Raloxifene. DR DrugBank; DB01045; Rifampicin. DR DrugBank; DB01138; Sulfinpyrazone. DR DrugBank; DB04348; Taurocholic acid. DR DrugBank; DB00661; Verapamil. DR DrugBank; DB00541; Vincristine. DR DrugCentral; O15438; -. DR TCDB; 3.A.1.208.9; the atp-binding cassette (abc) superfamily. DR GlyCosmos; O15438; 3 sites, No reported glycans. DR GlyGen; O15438; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; O15438; -. DR PhosphoSitePlus; O15438; -. DR SwissPalm; O15438; -. DR BioMuta; ABCC3; -. DR EPD; O15438; -. DR jPOST; O15438; -. DR MassIVE; O15438; -. DR MaxQB; O15438; -. DR PaxDb; 9606-ENSP00000285238; -. DR PeptideAtlas; O15438; -. DR ProteomicsDB; 48659; -. [O15438-1] DR ProteomicsDB; 48660; -. [O15438-2] DR ProteomicsDB; 48661; -. [O15438-3] DR ProteomicsDB; 48662; -. [O15438-4] DR ProteomicsDB; 48663; -. [O15438-5] DR Pumba; O15438; -. DR Antibodypedia; 18128; 356 antibodies from 37 providers. DR DNASU; 8714; -. DR Ensembl; ENST00000285238.13; ENSP00000285238.8; ENSG00000108846.16. [O15438-1] DR Ensembl; ENST00000427699.5; ENSP00000395160.1; ENSG00000108846.16. [O15438-5] DR Ensembl; ENST00000502426.5; ENSP00000427073.1; ENSG00000108846.16. [O15438-3] DR Ensembl; ENST00000505699.5; ENSP00000427521.1; ENSG00000108846.16. [O15438-2] DR GeneID; 8714; -. DR KEGG; hsa:8714; -. DR MANE-Select; ENST00000285238.13; ENSP00000285238.8; NM_003786.4; NP_003777.2. DR UCSC; uc002isk.5; human. [O15438-1] DR AGR; HGNC:54; -. DR CTD; 8714; -. DR DisGeNET; 8714; -. DR GeneCards; ABCC3; -. DR HGNC; HGNC:54; ABCC3. DR HPA; ENSG00000108846; Tissue enhanced (adrenal gland, liver). DR MIM; 604323; gene. DR neXtProt; NX_O15438; -. DR OpenTargets; ENSG00000108846; -. DR PharmGKB; PA376; -. DR VEuPathDB; HostDB:ENSG00000108846; -. DR eggNOG; KOG0054; Eukaryota. DR GeneTree; ENSGT00940000161624; -. DR HOGENOM; CLU_000604_27_13_1; -. DR InParanoid; O15438; -. DR OMA; FAWNCVP; -. DR OrthoDB; 3384185at2759; -. DR PhylomeDB; O15438; -. DR TreeFam; TF105199; -. DR BRENDA; 7.6.2.3; 2681. DR PathwayCommons; O15438; -. DR Reactome; R-HSA-159418; Recycling of bile acids and salts. DR Reactome; R-HSA-382556; ABC-family proteins mediated transport. DR Reactome; R-HSA-9749641; Aspirin ADME. DR Reactome; R-HSA-9753281; Paracetamol ADME. DR Reactome; R-HSA-9818032; NFE2L2 regulating MDR associated enzymes. DR SignaLink; O15438; -. DR SIGNOR; O15438; -. DR BioGRID-ORCS; 8714; 19 hits in 1148 CRISPR screens. DR ChiTaRS; ABCC3; human. DR GeneWiki; ABCC3; -. DR GenomeRNAi; 8714; -. DR Pharos; O15438; Tbio. DR PRO; PR:O15438; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O15438; Protein. DR Bgee; ENSG00000108846; Expressed in pancreatic ductal cell and 148 other cell types or tissues. DR ExpressionAtlas; O15438; baseline and differential. DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. 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; IDA:UniProtKB. DR GO; GO:0140359; F:ABC-type transporter activity; TAS:Reactome. DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0043225; F:ATPase-coupled inorganic anion transmembrane transporter activity; TAS:Reactome. DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0015164; F:glucuronoside transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0071714; F:icosanoid transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:ARUK-UCL. DR GO; GO:0015721; P:bile acid and bile salt transport; ISS:UniProtKB. DR GO; GO:0071716; P:leukotriene transport; IMP:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL. DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. DR GO; GO:0006855; P:xenobiotic transmembrane transport; IMP:UniProtKB. DR GO; GO:0042908; P:xenobiotic transport; IDA:ARUK-UCL. DR CDD; cd18595; ABC_6TM_MRP1_2_3_6_D1_like; 1. DR CDD; cd18603; ABC_6TM_MRP1_2_3_6_D2_like; 1. DR CDD; cd03250; ABCC_MRP_domain1; 1. DR CDD; cd03244; ABCC_MRP_domain2; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; MRP. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; TIGR00957; MRP_assoc_pro; 1. DR PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1. DR PANTHER; PTHR24223:SF405; ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 3; 1. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS50929; ABC_TM1F; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. DR Genevisible; O15438; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Glycoprotein; Lipid transport; Membrane; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..1527 FT /note="ATP-binding cassette sub-family C member 3" FT /id="PRO_0000093360" FT TOPO_DOM 1..32 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 33..53 FT /note="Helical; Name=1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 54..73 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 74..94 FT /note="Helical; Name=2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 95..99 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 100..120 FT /note="Helical; Name=3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 121..132 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 133..153 FT /note="Helical; Name=4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 154..171 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 172..192 FT /note="Helical; Name=5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 193..302 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 303..323 FT /note="Helical; Name=6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 324..349 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 350..370 FT /note="Helical; Name=7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 371..426 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 427..447 FT /note="Helical; Name=8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 448..450 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 451..471 FT /note="Helical; Name=9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 472..533 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 534..554 FT /note="Helical; Name=10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 555..576 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 577..597 FT /note="Helical; Name=11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 598..963 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 964..984 FT /note="Helical; Name=12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 985..1021 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 1022..1042 FT /note="Helical; Name=13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1043..1085 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 1086..1106 FT /note="Helical; Name=14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1107 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 1108..1128 FT /note="Helical; Name=15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1129..1199 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 1200..1220 FT /note="Helical; Name=16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1221..1222 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 1223..1243 FT /note="Helical; Name=17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TOPO_DOM 1244..1527 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT DOMAIN 311..594 FT /note="ABC transmembrane type-1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 629..851 FT /note="ABC transporter 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT DOMAIN 971..1252 FT /note="ABC transmembrane type-1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 1291..1523 FT /note="ABC transporter 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 910..932 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 661..668 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT BINDING 1323..1330 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT MOD_RES 908 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 911 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 18 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1006 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1007 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1 FT /note="M -> MPACTVKESPNCKRNFCKADHIVNTSGGSNLERVGKQKTIQKGQFSQ FT RSVCT (in isoform 4)" FT /evidence="ECO:0000303|Ref.7" FT /id="VSP_043864" FT VAR_SEQ 226..510 FT /note="MAIYGYRHPLEEKDLWSLKEEDRSQMVVQQLLEAWRKQEKQTARHKASAAPG FT KNASGEDEVLLGARPRPRKPSFLKALLATFGSSFLISACFKLIQDLLSFINPQLLSILI FT RFISNPMAPSWWGFLVAGLMFLCSMMQSLILQHYYHYIFVTGVKFRTGIMGVIYRKALV FT ITNSVKRASTVGEIVNLMSVDAQRFMDLAPFLNLLWSAPLQIILAIYFLWQNLGPSVLA FT GVAFMVLLIPLNGAVAVKMRAFQVKQMKLKDSRIKLMSEILNGIKVLKLYAWEPSF -> FT LLNPDPLRGCLPGFTSPQDGHLWLPASPGGEGPLVPKGRGQIPDGGAAAAGGMEEAGKA FT DGTTQGFSSTWEKCLRRGRGAAGCPAQAPEALLPEGPAGHLRLQLPHQCLLQAYPGPAL FT LHQSTAAQHPDQVYLQPHGPLLVGLPGGWADVPVLHDAVADLTTLLPLHLCDWGEVSYW FT DHGCHLQEGSGYHQLSQTCVHCGGNCQPHVSGCPALHGPCPLPQSAVVSTPADHPGDLL FT PLAEPRSLCPGWSRFHGLADSTQRSCGREDARLPGKANEIEGLAHQADE (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:9889399" FT /id="VSP_000040" FT VAR_SEQ 511..1527 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9889399" FT /id="VSP_000041" FT VAR_SEQ 547..572 FT /note="TLITLWVYVYVDPNNVLDAEKAFVSV -> RLGTGLGPCLQGSGCPGMARAH FT WTLP (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_039041" FT VAR_SEQ 573..1527 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_039042" FT VAR_SEQ 1194..1527 FT /note="WLSIGVEFVGNCVVLFAALFAVIGRSSLNPGLVGLSVSYSLQVTFALNWMIR FT MMSDLESNIVAVERVKEYSKTETEAPWVVEGSRPPEGWPPRGEVEFRNYSVRYRPGLDL FT VLRDLSLHVHGGEKVGIVGRTGAGKSSMTLCLFRILEAAKGEIRIDGLNVADIGLHDLR FT SQLTIIPQDPILFSGTLRMNLDPFGSYSEEDIWWALELSHLHTFVSSQPAGLDFQCSEG FT GENLSVGQRQLVCLARALLRKSRILVLDEATAAIDLETDNLIQATIRTQFDTCTVLTIA FT HRLNTIMDYTRVLVLDKGVVAEFDSPANLIAARGIFYGMARDAGLA -> SEAASLAPC FT SSRNSQQALWCSGSLSLLSPKQKTGPALPLPHFLLI (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9889399" FT /id="VSP_000042" FT VARIANT 11 FT /note="G -> D (in dbSNP:rs11568609)" FT /id="VAR_029119" FT VARIANT 346 FT /note="S -> F (in dbSNP:rs11568605)" FT /id="VAR_020235" FT VARIANT 548 FT /note="L -> Q (in dbSNP:rs144520783)" FT /evidence="ECO:0000269|PubMed:15083066" FT /id="VAR_084161" FT VARIANT 1286 FT /note="R -> G (in dbSNP:rs11568593)" FT /id="VAR_029120" FT VARIANT 1297 FT /note="R -> H (does not affect subcellular localizattion; FT does not affect the transport of monoglucuronosyl FT bilirubin, bisglucuronosyl bilirubin, leukotriene C4, FT dehydroepiandrosterone-3-sulfate and 17-beta-glucuronosyl FT oestradiol; dbSNP:rs11568591)" FT /evidence="ECO:0000269|PubMed:15083066" FT /id="VAR_020237" FT VARIANT 1365 FT /note="Q -> R (in dbSNP:rs11568590)" FT /id="VAR_020239" FT VARIANT 1381 FT /note="R -> S (in dbSNP:rs45461799)" FT /id="VAR_020240" FT CONFLICT 13 FT /note="K -> N (in Ref. 10; AAH46126)" FT /evidence="ECO:0000305" FT CONFLICT 42 FT /note="C -> R (in Ref. 5; CAA76658)" FT /evidence="ECO:0000305" FT CONFLICT 184 FT /note="A -> T (in Ref. 4; AAD02846)" FT /evidence="ECO:0000305" FT CONFLICT 344 FT /note="A -> G (in Ref. 1; AAC34668)" FT /evidence="ECO:0000305" FT CONFLICT 569 FT /note="F -> Y (in Ref. 2; BAA28146)" FT /evidence="ECO:0000305" FT CONFLICT 1128 FT /note="F -> C (in Ref. 11; AAB71756)" FT /evidence="ECO:0000305" FT CONFLICT 1212 FT /note="L -> I (in Ref. 11; AAB71756)" FT /evidence="ECO:0000305" FT CONFLICT 1249 FT /note="D -> E (in Ref. 11; AAB71756)" FT /evidence="ECO:0000305" FT CONFLICT 1359 FT /note="L -> F (in Ref. 11; AAB71756)" FT /evidence="ECO:0000305" FT CONFLICT 1362 FT /note="L -> V (in Ref. 1; AAC34668 and 11; AAB71756)" FT /evidence="ECO:0000305" FT CONFLICT 1364 FT /note="S -> C (in Ref. 11; AAB71756)" FT /evidence="ECO:0000305" FT CONFLICT 1366 FT /note="L -> M (in Ref. 11; AAB71756)" FT /evidence="ECO:0000305" FT CONFLICT 1371 FT /note="Q -> R (in Ref. 11; AAB71756)" FT /evidence="ECO:0000305" FT HELIX 35..48 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 50..53 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 55..57 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 68..71 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 75..92 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 93..97 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 111..114 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 115..127 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 136..152 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 159..162 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 168..173 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 176..188 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 208..211 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 215..218 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 224..232 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 237..239 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 249..252 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 253..264 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 300..307 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 308..310 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 311..313 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 314..322 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 323..325 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 327..339 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 342..344 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 346..358 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 359..365 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 367..374 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 375..383 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 386..389 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 390..393 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 398..402 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 411..414 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 415..418 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 420..422 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 423..426 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 429..431 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 432..448 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 449..452 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 453..461 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 464..466 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 467..469 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 470..472 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 475..496 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 499..503 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 507..525 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 526..528 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 529..532 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 533..535 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 537..540 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 542..556 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 565..582 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 585..594 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 597..606 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 616..619 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 625..637 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 643..652 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 656..660 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 667..675 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 678..682 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 685..687 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 691..694 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 702..704 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 705..710 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 711..713 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 717..726 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 732..735 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 737..740 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 741..749 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 753..767 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 770..775 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 777..780 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 783..792 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 801..808 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 819..825 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 828..833 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 835..840 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 844..848 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 956..966 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 968..970 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 972..975 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 978..995 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1008..1019 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 1021..1026 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1027..1052 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1057..1062 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1065..1071 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1074..1081 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1083..1094 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 1095..1098 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1099..1107 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1109..1114 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1117..1152 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 1153..1157 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1158..1163 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1167..1185 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1193..1199 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1202..1216 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 1217..1220 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1225..1231 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1234..1236 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1238..1253 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1255..1263 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1275..1277 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1289..1296 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1305..1313 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1318..1322 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1329..1333 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 1334..1338 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1344..1351 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1354..1356 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1359..1362 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1363..1365 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1366..1369 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1377..1379 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 1380..1384 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1392..1401 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1405..1410 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1411..1413 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1414..1416 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1423..1426 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1428..1442 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1445..1450 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1454..1456 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1458..1471 FT /evidence="ECO:0007829|PDB:8HVH" FT TURN 1472..1474 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1475..1480 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1484..1487 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1490..1497 FT /evidence="ECO:0007829|PDB:8HVH" FT STRAND 1500..1505 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1507..1512 FT /evidence="ECO:0007829|PDB:8HVH" FT HELIX 1516..1522 FT /evidence="ECO:0007829|PDB:8HVH" SQ SEQUENCE 1527 AA; 169343 MW; 0D1F879B6F18370C CRC64; MDALCGSGEL GSKFWDSNLS VHTENPDLTP CFQNSLLAWV PCIYLWVALP CYLLYLRHHC RGYIILSHLS KLKMVLGVLL WCVSWADLFY SFHGLVHGRA PAPVFFVTPL VVGVTMLLAT LLIQYERLQG VQSSGVLIIF WFLCVVCAIV PFRSKILLAK AEGEISDPFR FTTFYIHFAL VLSALILACF REKPPFFSAK NVDPNPYPET SAGFLSRLFF WWFTKMAIYG YRHPLEEKDL WSLKEEDRSQ MVVQQLLEAW RKQEKQTARH KASAAPGKNA SGEDEVLLGA RPRPRKPSFL KALLATFGSS FLISACFKLI QDLLSFINPQ LLSILIRFIS NPMAPSWWGF LVAGLMFLCS MMQSLILQHY YHYIFVTGVK FRTGIMGVIY RKALVITNSV KRASTVGEIV NLMSVDAQRF MDLAPFLNLL WSAPLQIILA IYFLWQNLGP SVLAGVAFMV LLIPLNGAVA VKMRAFQVKQ MKLKDSRIKL MSEILNGIKV LKLYAWEPSF LKQVEGIRQG ELQLLRTAAY LHTTTTFTWM CSPFLVTLIT LWVYVYVDPN NVLDAEKAFV SVSLFNILRL PLNMLPQLIS NLTQASVSLK RIQQFLSQEE LDPQSVERKT ISPGYAITIH SGTFTWAQDL PPTLHSLDIQ VPKGALVAVV GPVGCGKSSL VSALLGEMEK LEGKVHMKGS VAYVPQQAWI QNCTLQENVL FGKALNPKRY QQTLEACALL ADLEMLPGGD QTEIGEKGIN LSGGQRQRVS LARAVYSDAD IFLLDDPLSA VDSHVAKHIF DHVIGPEGVL AGKTRVLVTH GISFLPQTDF IIVLADGQVS EMGPYPALLQ RNGSFANFLC NYAPDEDQGH LEDSWTALEG AEDKEALLIE DTLSNHTDLT DNDPVTYVVQ KQFMRQLSAL SSDGEGQGRP VPRRHLGPSE KVQVTEAKAD GALTQEEKAA IGTVELSVFW DYAKAVGLCT TLAICLLYVG QSAAAIGANV WLSAWTNDAM ADSRQNNTSL RLGVYAALGI LQGFLVMLAA MAMAAGGIQA ARVLHQALLH NKIRSPQSFF DTTPSGRILN CFSKDIYVVD EVLAPVILML LNSFFNAIST LVVIMASTPL FTVVILPLAV LYTLVQRFYA ATSRQLKRLE SVSRSPIYSH FSETVTGASV IRAYNRSRDF EIISDTKVDA NQRSCYPYII SNRWLSIGVE FVGNCVVLFA ALFAVIGRSS LNPGLVGLSV SYSLQVTFAL NWMIRMMSDL ESNIVAVERV KEYSKTETEA PWVVEGSRPP EGWPPRGEVE FRNYSVRYRP GLDLVLRDLS LHVHGGEKVG IVGRTGAGKS SMTLCLFRIL EAAKGEIRID GLNVADIGLH DLRSQLTIIP QDPILFSGTL RMNLDPFGSY SEEDIWWALE LSHLHTFVSS QPAGLDFQCS EGGENLSVGQ RQLVCLARAL LRKSRILVLD EATAAIDLET DNLIQATIRT QFDTCTVLTI AHRLNTIMDY TRVLVLDKGV VAEFDSPANL IAARGIFYGM ARDAGLA //