MRP3_HUMAN
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 03-AUG-2022, entry version 200.
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).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that bind and hydrolyze 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). Can confers
CC resistance to various anticancer drugs, methotrexate, tenoposide and
CC etoposide, by decreasing accumulation of these drugs in cells
CC (PubMed:11581266, PubMed:10359813). {ECO:0000250|UniProtKB:O88563,
CC ECO:0000269|PubMed:10359813, ECO:0000269|PubMed:11581266,
CC ECO:0000269|PubMed:15083066}.
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}; Multi-pass membrane protein
CC {ECO:0000255}.
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. {ECO:0000269|PubMed:10094960, 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";
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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 AlphaFoldDB; O15438; -.
DR SMR; O15438; -.
DR BioGRID; 114255; 28.
DR IntAct; O15438; 6.
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; 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 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; O15438; -.
DR PeptideAtlas; O15438; -.
DR PRIDE; 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 Antibodypedia; 18128; 324 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 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; MDLMTFL; -.
DR OrthoDB; 138195at2759; -.
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 SignaLink; O15438; -.
DR SIGNOR; O15438; -.
DR BioGRID-ORCS; 8714; 14 hits in 1070 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 146 other tissues.
DR ExpressionAtlas; O15438; baseline and differential.
DR Genevisible; O15438; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
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: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 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein;
KW Lipid transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW 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"
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
