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Pleiotropic ABC efflux transporter of multiple drugs CDR1 (Pleiotropic drug resistance protein CDR1)

 CDR1_CANAL              Reviewed;        1501 AA.
Q5ANA3; A0A1D8PK55;
07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
10-MAY-2017, sequence version 2.
07-JUN-2017, entry version 114.
RecName: Full=Pleiotropic ABC efflux transporter of multiple drugs CDR1 {ECO:0000305};
AltName: Full=Pleiotropic drug resistance protein CDR1 {ECO:0000305};
Name=CDR1; OrderedLocusNames=CAALFM_C305220WA;
ORFNames=CaO19.13421, CaO19.6000;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=8891134;
Sanglard D., Ischer F., Monod M., Bille J.;
"Susceptibilities of Candida albicans multidrug transporter mutants to
various antifungal agents and other metabolic inhibitors.";
Antimicrob. Agents Chemother. 40:2300-2305(1996).
[5]
FUNCTION.
PubMed=9124851;
Albertson G.D., Niimi M., Cannon R.D., Jenkinson H.F.;
"Multiple efflux mechanisms are involved in Candida albicans
fluconazole resistance.";
Antimicrob. Agents Chemother. 40:2835-2841(1996).
[6]
FUNCTION.
PubMed=9453158; DOI=10.1111/j.1574-6968.1998.tb12802.x;
Krishnamurthy S., Gupta V., Snehlata P., Prasad R.;
"Characterisation of human steroid hormone transport mediated by
Cdr1p, a multidrug transporter of Candida albicans, belonging to the
ATP binding cassette super family.";
FEMS Microbiol. Lett. 158:69-74(1998).
[7]
INDUCTION.
PubMed=9532737; DOI=10.1111/j.1574-6968.1998.tb12910.x;
Krishnamurthy S., Gupta V., Prasad R., Panwar S.L., Prasad R.;
"Expression of CDR1, a multidrug resistance gene of Candida albicans:
transcriptional activation by heat shock, drugs and human steroid
hormones.";
FEMS Microbiol. Lett. 160:191-197(1998).
[8]
INDUCTION.
PubMed=9605502;
DOI=10.1002/(SICI)1097-0061(19980430)14:6<517::AID-YEA250>3.0.CO;2-D;
Hernaez M.L., Gil C., Pla J., Nombela C.;
"Induced expression of the Candida albicans multidrug resistance gene
CDR1 in response to fluconazole and other antifungals.";
Yeast 14:517-526(1998).
[9]
FUNCTION.
PubMed=9605504;
DOI=10.1002/(SICI)1097-0061(19980430)14:6<535::AID-YEA254>3.0.CO;2-5;
Krishnamurthy S., Chatterjee U., Gupta V., Prasad R., Das P.,
Snehlata P., Hasnain S.E., Prasad R.;
"Deletion of transmembrane domain 12 of CDR1, a multidrug transporter
from Candida albicans, leads to altered drug specificity: expression
of a yeast multidrug transporter in baculovirus expression system.";
Yeast 14:535-550(1998).
[10]
FUNCTION, AND INDUCTION.
PubMed=10428921;
Henry K.W., Cruz M.C., Katiyar S.K., Edlind T.D.;
"Antagonism of azole activity against Candida albicans following
induction of multidrug resistance genes by selected antimicrobial
agents.";
Antimicrob. Agents Chemother. 43:1968-1974(1999).
[11]
FUNCTION.
PubMed=10227177; DOI=10.1111/j.1574-6968.1999.tb13541.x;
Smriti X., Krishnamurthy S.S., Prasad R.;
"Membrane fluidity affects functions of Cdr1p, a multidrug ABC
transporter of Candida albicans.";
FEMS Microbiol. Lett. 173:475-481(1999).
[12]
INDUCTION.
PubMed=10556714; DOI=10.1111/j.1574-6968.1999.tb08798.x;
Puri N., Krishnamurthy S., Habib S., Hasnain S.E., Goswami S.K.,
Prasad R.;
"CDR1, a multidrug resistance gene from Candida albicans, contains
multiple regulatory domains in its promoter and the distal AP-1
element mediates its induction by miconazole.";
FEMS Microbiol. Lett. 180:213-219(1999).
[13]
FUNCTION.
PubMed=10029989;
DOI=10.1002/(SICI)1097-0061(19990130)15:2<111::AID-YEA350>3.0.CO;2-E;
Dogra S., Krishnamurthy S., Gupta V., Dixit B.L., Gupta C.M.,
Sanglard D., Prasad R.;
"Asymmetric distribution of phosphatidylethanolamine in C. albicans:
possible mediation by CDR1, a multidrug transporter belonging to ATP
binding cassette (ABC) superfamily.";
Yeast 15:111-121(1999).
[14]
INDUCTION.
PubMed=10952571; DOI=10.1128/AAC.44.9.2296-2303.2000;
Lyons C.N., White T.C.;
"Transcriptional analyses of antifungal drug resistance in Candida
albicans.";
Antimicrob. Agents Chemother. 44:2296-2303(2000).
[15]
FUNCTION.
PubMed=11709310; DOI=10.1128/AAC.45.12.3366-3374.2001;
Nakamura K., Niimi M., Niimi K., Holmes A.R., Yates J.E.,
Decottignies A., Monk B.C., Goffeau A., Cannon R.D.;
"Functional expression of Candida albicans drug efflux pump Cdr1p in a
Saccharomyces cerevisiae strain deficient in membrane transporters.";
Antimicrob. Agents Chemother. 45:3366-3374(2001).
[16]
INDUCTION.
PubMed=11918807; DOI=10.1046/j.1365-2958.2002.02814.x;
de Micheli M., Bille J., Schueller C., Sanglard D.;
"A common drug-responsive element mediates the upregulation of the
Candida albicans ABC transporters CDR1 and CDR2, two genes involved in
antifungal drug resistance.";
Mol. Microbiol. 43:1197-1214(2002).
[17]
FUNCTION.
PubMed=11870854; DOI=10.1002/yea.818;
Smriti X., Krishnamurthy S., Dixit B.L., Gupta C.M., Milewski S.,
Prasad R.;
"ABC transporters Cdr1p, Cdr2p and Cdr3p of a human pathogen Candida
albicans are general phospholipid translocators.";
Yeast 19:303-318(2002).
[18]
FUNCTION.
PubMed=12709320; DOI=10.1128/AAC.47.5.1543-1554.2003;
Gauthier C., Weber S., Alarco A.M., Alqawi O., Daoud R., Georges E.,
Raymond M.;
"Functional similarities and differences between Candida albicans
Cdr1p and Cdr2p transporters.";
Antimicrob. Agents Chemother. 47:1543-1554(2003).
[19]
INDUCTION.
PubMed=15561818; DOI=10.1128/AAC.48.12.4505-4512.2004;
Chen C.G., Yang Y.L., Shih H.I., Su C.L., Lo H.J.;
"CaNdt80 is involved in drug resistance in Candida albicans by
regulating CDR1.";
Antimicrob. Agents Chemother. 48:4505-4512(2004).
[20]
DOMAIN, AND MUTAGENESIS OF CYS-193.
PubMed=12962507; DOI=10.1021/bi0345900;
Jha S., Karnani N., Dhar S.K., Mukhopadhayay K., Shukla S., Saini P.,
Mukhopadhayay G., Prasad R.;
"Purification and characterization of the N-terminal nucleotide
binding domain of an ABC drug transporter of Candida albicans:
uncommon cysteine 193 of Walker A is critical for ATP hydrolysis.";
Biochemistry 42:10822-10832(2003).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-232; GLY-296;
PHE-774; GLY-995; GLY-1000; THR-1351; CYS-1418; THR-1449 AND VAL-1456.
PubMed=14665469; DOI=10.1128/EC.2.6.1361-1375.2003;
Shukla S., Saini P., Smriti X., Jha S., Ambudkar S.V., Prasad R.;
"Functional characterization of Candida albicans ABC transporter
Cdr1p.";
Eukaryot. Cell 2:1361-1375(2003).
[22]
INDUCTION, AND FUNCTION.
PubMed=15152937;
O'Keeffe J., Kavanagh K.;
"Adriamycin alters the expression of drug efflux pumps and confers
amphotericin B tolerance in Candida albicans.";
Anticancer Res. 24:405-408(2004).
[23]
INDUCTION.
PubMed=15273122; DOI=10.1128/AAC.48.8.3064-3079.2004;
Karababa M., Coste A.T., Rognon B., Bille J., Sanglard D.;
"Comparison of gene expression profiles of Candida albicans azole-
resistant clinical isolates and laboratory strains exposed to drugs
inducing multidrug transporters.";
Antimicrob. Agents Chemother. 48:3064-3079(2004).
[24]
INDUCTION.
PubMed=15328097; DOI=10.1128/AAC.48.9.3358-3366.2004;
Mateus C., Crow S.A. Jr., Ahearn D.G.;
"Adherence of Candida albicans to silicone induces immediate enhanced
tolerance to fluconazole.";
Antimicrob. Agents Chemother. 48:3358-3366(2004).
[25]
ENZYME REGULATION.
PubMed=15325261; DOI=10.1016/j.bbrc.2004.07.151;
Shukla S., Sauna Z.E., Prasad R., Ambudkar S.V.;
"Disulfiram is a potent modulator of multidrug transporter Cdr1p of
Candida albicans.";
Biochem. Biophys. Res. Commun. 322:520-525(2004).
[26]
INDUCTION.
PubMed=15590837; DOI=10.1128/EC.3.6.1639-1652.2004;
Coste A.T., Karababa M., Ischer F., Bille J., Sanglard D.;
"TAC1, transcriptional activator of CDR genes, is a new transcription
factor involved in the regulation of Candida albicans ABC transporters
CDR1 and CDR2.";
Eukaryot. Cell 3:1639-1652(2004).
[27]
INDUCTION.
PubMed=14734019; DOI=10.1016/S1567-1356(03)00204-6;
Gaur N.A., Puri N., Karnani N., Mukhopadhyay G., Goswami S.K.,
Prasad R.;
"Identification of a negative regulatory element which regulates basal
transcription of a multidrug resistance gene CDR1 of Candida
albicans.";
FEMS Yeast Res. 4:389-399(2004).
[28]
FUNCTION, MUTAGENESIS OF THR-1351, AND SUBCELLULAR LOCATION.
PubMed=15190023; DOI=10.1093/jac/dkh308;
Shukla S., Ambudkar S.V., Prasad R.;
"Substitution of threonine-1351 in the multidrug transporter Cdr1p of
Candida albicans results in hypersusceptibility to antifungal agents
and threonine-1351 is essential for synergic effects of calcineurin
inhibitor FK520.";
J. Antimicrob. Chemother. 54:38-45(2004).
[29]
FUNCTION.
PubMed=15486081; DOI=10.1093/jac/dkh456;
Niimi M., Niimi K., Takano Y., Holmes A.R., Fischer F.J., Uehara Y.,
Cannon R.D.;
"Regulated overexpression of CDR1 in Candida albicans confers
multidrug resistance.";
J. Antimicrob. Chemother. 54:999-1006(2004).
[30]
INDUCTION.
PubMed=14968428; DOI=10.1002/yea.1067;
Karnani N., Gaur N.A., Jha S., Puri N., Krishnamurthy S.,
Goswami S.K., Mukhopadhyay G., Prasad R.;
"SRE1 and SRE2 are two specific steroid-responsive modules of Candida
drug resistance gene 1 (CDR1) promoter.";
Yeast 21:219-239(2004).
[31]
INDUCTION.
PubMed=15896319; DOI=10.1016/j.bbrc.2005.04.113;
Gaur N.A., Manoharlal R., Saini P., Prasad T., Mukhopadhyay G.,
Hoefer M., Morschhaeuser J., Prasad R.;
"Expression of the CDR1 efflux pump in clinical Candida albicans
isolates is controlled by a negative regulatory element.";
Biochem. Biophys. Res. Commun. 332:206-214(2005).
[32]
DOMAIN, AND MUTAGENESIS OF TRP-326.
PubMed=15850398; DOI=10.1021/bi0474160;
Rai V., Shukla S., Jha S., Komath S.S., Prasad R.;
"Functional characterization of N-terminal nucleotide binding domain
(NBD-1) of a major ABC drug transporter Cdr1p of Candida albicans:
uncommon but conserved Trp326 of Walker B is important for ATP
binding.";
Biochemistry 44:6650-6661(2005).
[33]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ALA-1346; ALA-1347;
THR-1351; THR-1355 AND LEU-1358.
PubMed=15937063; DOI=10.1093/jac/dki183;
Saini P., Prasad T., Gaur N.A., Shukla S., Jha S., Komath S.S.,
Khan L.A., Haq Q.M., Prasad R.;
"Alanine scanning of transmembrane helix 11 of Cdr1p ABC antifungal
efflux pump of Candida albicans: identification of amino acid residues
critical for drug efflux.";
J. Antimicrob. Chemother. 56:77-86(2005).
[34]
INDUCTION.
PubMed=16569846; DOI=10.1128/AAC.50.4.1311-1319.2006;
Lepak A., Nett J., Lincoln L., Marchillo K., Andes D.;
"Time course of microbiologic outcome and gene expression in Candida
albicans during and following in vitro and in vivo exposure to
fluconazole.";
Antimicrob. Agents Chemother. 50:1311-1319(2006).
[35]
FUNCTION.
PubMed=16475832; DOI=10.1021/bi0519147;
Shukla S., Rai V., Banerjee D., Prasad R.;
"Characterization of Cdr1p, a major multidrug efflux protein of
Candida albicans: purified protein is amenable to intrinsic
fluorescence analysis.";
Biochemistry 45:2425-2435(2006).
[36]
INDUCTION.
PubMed=16839415; DOI=10.1186/1471-2199-7-22;
Yang Y.L., Lin Y.H., Tsao M.Y., Chen C.G., Shih H.I., Fan J.C.,
Wang J.S., Lo H.J.;
"Serum repressing efflux pump CDR1 in Candida albicans.";
BMC Mol. Biol. 7:22-22(2006).
[37]
INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=16400181; DOI=10.1128/EC.5.1.180-191.2006;
Cheng G., Yeater K.M., Hoyer L.L.;
"Cellular and molecular biology of Candida albicans estrogen
response.";
Eukaryot. Cell 5:180-191(2006).
[38]
FUNCTION, AND MUTAGENESIS OF TRP-629.
PubMed=16782311; DOI=10.1016/j.ijantimicag.2006.02.016;
Gao P.H., Cao Y.B., Jia X.M., Cao Y.Y., Quan H., Wang Y., Jiang Y.Y.;
"Drug susceptibilities of yeast cells are affected when expressing
mutant Candida albicans drug resistance protein.";
Int. J. Antimicrob. Agents 28:69-74(2006).
[39]
INDUCTION, AND FUNCTION.
PubMed=16291868; DOI=10.1093/jac/dki402;
Tanida T., Okamoto T., Ueta E., Yamamoto T., Osaki T.;
"Antimicrobial peptides enhance the candidacidal activity of
antifungal drugs by promoting the efflux of ATP from Candida cells.";
J. Antimicrob. Chemother. 57:94-103(2006).
[40]
INDUCTION.
PubMed=17005790; DOI=10.1099/jmm.0.46650-0;
Wang J.S., Yang Y.L., Wu C.J., Ouyang K.J., Tseng K.Y., Chen C.G.,
Wang H., Lo H.J.;
"The DNA-binding domain of CaNdt80p is required to activate CDR1
involved in drug resistance in Candida albicans.";
J. Med. Microbiol. 55:1403-1411(2006).
[41]
FUNCTION, DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=16622073; DOI=10.1099/mic.0.28471-0;
Saini P., Gaur N.A., Prasad R.;
"Chimeras of the ABC drug transporter Cdr1p reveal functional
indispensability of transmembrane domains and nucleotide-binding
domains, but transmembrane segment 12 is replaceable with the
corresponding homologous region of the non-drug transporter Cdr3p.";
Microbiology 152:1559-1573(2006).
[42]
INDUCTION.
PubMed=16921553; DOI=10.1002/yea.1394;
Larsen B., Anderson S., Brockman A., Essmann M., Schmidt M.;
"Key physiological differences in Candida albicans CDR1 induction by
steroid hormones and antifungal drugs.";
Yeast 23:795-802(2006).
[43]
FUNCTION.
PubMed=17924650; DOI=10.1021/bi700453e;
Shukla S., Rai V., Saini P., Banerjee D., Menon A.K., Prasad R.;
"Candida drug resistance protein 1, a major multidrug ATP binding
cassette transporter of Candida albicans, translocates fluorescent
phospholipids in a reconstituted system.";
Biochemistry 46:12081-12090(2007).
[44]
INDUCTION, AND FUNCTION.
PubMed=17202662; DOI=10.1248/bpb.30.68;
Shen H., An M.M., Wang D.J., Xu Z., Zhang J.D., Gao P.H., Cao Y.Y.,
Cao Y.B., Jiang Y.Y.;
"Fcr1p inhibits development of fluconazole resistance in Candida
albicans by abolishing CDR1 induction.";
Biol. Pharm. Bull. 30:68-73(2007).
[45]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=18056285; DOI=10.1128/AAC.00861-07;
Pasrija R., Panwar S.L., Prasad R.;
"Multidrug transporters CaCdr1p and CaMdr1p of Candida albicans
display different lipid specificities: both ergosterol and
sphingolipids are essential for targeting of CaCdr1p to membrane
rafts.";
Antimicrob. Agents Chemother. 52:694-704(2008).
[46]
INDUCTION, AND FUNCTION.
PubMed=18268086; DOI=10.1128/AAC.01106-07;
Manoharlal R., Gaur N.A., Panwar S.L., Morschhaeuser J., Prasad R.;
"Transcriptional activation and increased mRNA stability contribute to
overexpression of CDR1 in azole-resistant Candida albicans.";
Antimicrob. Agents Chemother. 52:1481-1492(2008).
[47]
FUNCTION.
PubMed=18710914; DOI=10.1128/AAC.00463-08;
Holmes A.R., Lin Y.H., Niimi K., Lamping E., Keniya M., Niimi M.,
Tanabe K., Monk B.C., Cannon R.D.;
"ABC transporter Cdr1p contributes more than Cdr2p does to fluconazole
efflux in fluconazole-resistant Candida albicans clinical isolates.";
Antimicrob. Agents Chemother. 52:3851-3862(2008).
[48]
FUNCTION.
PubMed=19223631; DOI=10.1128/AAC.00926-08;
Tsao S., Rahkhoodaee F., Raymond M.;
"Relative contributions of the Candida albicans ABC transporters Cdr1p
and Cdr2p to clinical azole resistance.";
Antimicrob. Agents Chemother. 53:1344-1352(2009).
[49]
FUNCTION, AND MUTAGENESIS OF THR-658; PRO-659; ALA-660; THR-661;
VAL-662; LEU-663; LEU-664; LEU-665; MET-667; VAL-668; ILE-669;
TYR-670; THR-671; GLY-672; PHE-673; VAL-674; ILE-675; PRO-676; THR-677
AND PRO-678.
PubMed=19393219; DOI=10.1016/j.bbamem.2009.04.009;
Puri N., Gaur M., Sharma M., Shukla S., Ambudkar S.V., Prasad R.;
"The amino acid residues of transmembrane helix 5 of multidrug
resistance protein CaCdr1p of Candida albicans are involved in
substrate specificity and drug transport.";
Biochim. Biophys. Acta 1788:1752-1761(2009).
[50]
INDUCTION.
PubMed=19420894; DOI=10.1248/yakushi.129.623;
Zhang H., Gao A., Li F., Zhang G., Ho H.I., Liao W.;
"Mechanism of action of tetrandrine, a natural inhibitor of Candida
albicans drug efflux pumps.";
Yakugaku Zasshi 129:623-630(2009).
[51]
DOMAIN.
PubMed=20546701; DOI=10.1016/j.bbamem.2010.05.017;
Kumar A., Shukla S., Mandal A., Shukla S., Ambudkar S.V., Prasad R.;
"Divergent signature motifs of nucleotide binding domains of ABC
multidrug transporter, CaCdr1p of pathogenic Candida albicans, are
functionally asymmetric and noninterchangeable.";
Biochim. Biophys. Acta 1798:1757-1766(2010).
[52]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=20348384; DOI=10.1128/EC.00355-09;
Basso L.R. Jr., Gast C.E., Mao Y., Wong B.;
"Fluconazole transport into Candida albicans secretory vesicles by the
membrane proteins Cdr1p, Cdr2p, and Mdr1p.";
Eukaryot. Cell 9:960-970(2010).
[53]
FUNCTION.
PubMed=20876623; DOI=10.1093/jac/dkq354;
Siikala E., Rautemaa R., Richardson M., Saxen H., Bowyer P.,
Sanglard D.;
"Persistent Candida albicans colonization and molecular mechanisms of
azole resistance in autoimmune polyendocrinopathy-candidiasis-
ectodermal dystrophy (APECED) patients.";
J. Antimicrob. Chemother. 65:2505-2513(2010).
[54]
INDUCTION, AND FUNCTION.
PubMed=20002912; DOI=10.1111/j.1365-2672.2009.04429.x;
Sun L.M., Cheng A.X., Wu X.Z., Zhang H.J., Lou H.X.;
"Synergistic mechanisms of retigeric acid B and azoles against Candida
albicans.";
J. Appl. Microbiol. 108:341-348(2010).
[55]
INDUCTION.
PubMed=20377529; DOI=10.1042/BSR20100015;
Manoharlal R., Sharma M., Prasad R.;
"Molecular determinants of transient and reversible induced up-
regulation of CaCDR1 in azole susceptible clinical isolates of Candida
albicans.";
Biosci. Rep. 31:31-43(2011).
[56]
INDUCTION.
PubMed=21856931; DOI=10.1128/EC.05041-11;
Shukla S., Yadav V., Mukhopadhyay G., Prasad R.;
"Ncb2 is involved in activated transcription of CDR1 in azole-
resistant clinical isolates of Candida albicans.";
Eukaryot. Cell 10:1357-1366(2011).
[57]
INDUCTION.
PubMed=21474609; DOI=10.1099/jmm.0.030692-0;
Watamoto T., Samaranayake L.P., Egusa H., Yatani H., Seneviratne C.J.;
"Transcriptional regulation of drug-resistance genes in Candida
albicans biofilms in response to antifungals.";
J. Med. Microbiol. 60:1241-1247(2011).
[58]
INDUCTION.
PubMed=20818920; DOI=10.3109/13693786.2010.512022;
Kofla G., Turner V., Schulz B., Storch U., Froelich D., Rognon B.,
Coste A.T., Sanglard D., Ruhnke M.;
"Doxorubicin induces drug efflux pumps in Candida albicans.";
Med. Mycol. 49:132-142(2011).
[59]
FUNCTION.
PubMed=22205973; DOI=10.1371/journal.pone.0028830;
Zhu J., Krom B.P., Sanglard D., Intapa C., Dawson C.C., Peters B.M.,
Shirtliff M.E., Jabra-Rizk M.A.;
"Farnesol-induced apoptosis in Candida albicans is mediated by Cdr1-p
extrusion and depletion of intracellular glutathione.";
PLoS ONE 6:E28830-E28830(2011).
[60]
FUNCTION, AND MUTAGENESIS OF CYS-1056; CYS-1091; CYS-1106; CYS-1294
AND CYS-1336.
PubMed=22166216; DOI=10.1016/j.bbrc.2011.11.150;
Prasad R., Shah A.H., Sanwal H., Kapoor K.;
"Alanine scanning of all cysteines and construction of a functional
cysteine-less Cdr1p, a multidrug ABC transporter of Candida
albicans.";
Biochem. Biophys. Res. Commun. 417:508-513(2012).
[61]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=23979757; DOI=10.1128/AAC.00889-13;
Thomas E., Roman E., Claypool S., Manzoor N., Pla J., Panwar S.L.;
"Mitochondria influence CDR1 efflux pump activity, Hog1-mediated
oxidative stress pathway, iron homeostasis, and ergosterol levels in
Candida albicans.";
Antimicrob. Agents Chemother. 57:5580-5599(2013).
[62]
SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF PHE-551; PHE-552;
PHE-559; SER-561; GLU-564; MET-604; ASN-609; ARG-644; PHE-1230;
THR-1331; CYS-1336 AND PHE-1360.
PubMed=23824183; DOI=10.1074/jbc.M113.488353;
Rawal M.K., Khan M.F., Kapoor K., Goyal N., Sen S., Saxena A.K.,
Lynn A.M., Tyndall J.D., Monk B.C., Cannon R.D., Komath S.S.,
Prasad R.;
"Insight into pleiotropic drug resistance ATP-binding cassette pump
drug transport through mutagenesis of Cdr1p transmembrane domains.";
J. Biol. Chem. 288:24480-24493(2013).
-!- FUNCTION: Pleiotropic ABC efflux transporter that confers
resistance to numerous chemicals including anisomycin,
cycloheximide, fluconazole, miconazole, ketoconazole,
itriconazole, nystatin, terbinafine, amorolfine, brefeldin A,
amphotericin B, fluphenazine, as well as estrogen. Plays a role in
farnesol-induced apoptotic process through glutathione efflux
activity. Mediates in-to-out transloaction of membrane
phospholipids including aminophospholipids and thus regulates
asymmetric distribution of phosphatidylethanolamine. Exhibits
nucleoside triphosphatase activity. {ECO:0000269|PubMed:10029989,
ECO:0000269|PubMed:10227177, ECO:0000269|PubMed:10428921,
ECO:0000269|PubMed:11709310, ECO:0000269|PubMed:11870854,
ECO:0000269|PubMed:12709320, ECO:0000269|PubMed:14665469,
ECO:0000269|PubMed:15152937, ECO:0000269|PubMed:15190023,
ECO:0000269|PubMed:15486081, ECO:0000269|PubMed:15937063,
ECO:0000269|PubMed:16291868, ECO:0000269|PubMed:16475832,
ECO:0000269|PubMed:16622073, ECO:0000269|PubMed:16782311,
ECO:0000269|PubMed:17202662, ECO:0000269|PubMed:18056285,
ECO:0000269|PubMed:18268086, ECO:0000269|PubMed:18710914,
ECO:0000269|PubMed:19223631, ECO:0000269|PubMed:19393219,
ECO:0000269|PubMed:20002912, ECO:0000269|PubMed:20348384,
ECO:0000269|PubMed:20876623, ECO:0000269|PubMed:22166216,
ECO:0000269|PubMed:22205973, ECO:0000269|PubMed:23824183,
ECO:0000269|PubMed:23979757, ECO:0000269|PubMed:8891134,
ECO:0000269|PubMed:9124851, ECO:0000269|PubMed:9453158,
ECO:0000269|PubMed:9605504}.
-!- ENZYME REGULATION: Disulfiram reverses CDR1-mediated drug
resistance by interaction with both ATP and substrate-binding
sites of the transporter and may be useful for antifungal therapy.
{ECO:0000269|PubMed:15325261}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.8 uM for fluconazole {ECO:0000269|PubMed:20348384};
Vmax=0.91 pmol/min/mg enzyme for fluconazole transport
{ECO:0000269|PubMed:20348384};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14665469,
ECO:0000269|PubMed:15190023, ECO:0000269|PubMed:15937063,
ECO:0000269|PubMed:16622073, ECO:0000269|PubMed:18056285,
ECO:0000269|PubMed:23824183}; Multi-pass membrane protein
{ECO:0000255}. Note=Accumulates at membrane rafts. Both ergosterol
and sphingolipids are essential for targeting to membrane rafts.
Mislocalizes to the vacuole in absence of FZO1.
{ECO:0000269|PubMed:18056285, ECO:0000269|PubMed:23979757}.
-!- INDUCTION: The distal promoter mediates the miconazole response
whereas the proximal promoter (-345/+1) contains all the
regulatory domains required for its induction by various other
stresses. The promoter also contains a steroid responsive region
(SRR) conferring beta-oestradiol and progesterone inducibility.
Transcription is positively regulated by NCB2, NTD80 and TAC1 and
repressed by FCR1. Expression is up-regulated during biofilm
development, by heat-shock, and by benomyl, doxorubicin,
miconazole, vinblastine, adriamycin, fluphenazine, cycloheximide,
calcofluor, canavanine, 5'-fluorcytosine, cilofungin and caffeine.
Expression is repressed by serum and inhibited by tetrandrine.
Transcription is also reduced during in vitro fluconazole exposure
but in the postexposure period, the mRNA abundance increases.
{ECO:0000269|PubMed:10428921, ECO:0000269|PubMed:10556714,
ECO:0000269|PubMed:10952571, ECO:0000269|PubMed:11918807,
ECO:0000269|PubMed:14734019, ECO:0000269|PubMed:14968428,
ECO:0000269|PubMed:15273122, ECO:0000269|PubMed:15328097,
ECO:0000269|PubMed:15561818, ECO:0000269|PubMed:15590837,
ECO:0000269|PubMed:15896319, ECO:0000269|PubMed:16291868,
ECO:0000269|PubMed:16400181, ECO:0000269|PubMed:16569846,
ECO:0000269|PubMed:16839415, ECO:0000269|PubMed:16921553,
ECO:0000269|PubMed:17005790, ECO:0000269|PubMed:17202662,
ECO:0000269|PubMed:18268086, ECO:0000269|PubMed:19420894,
ECO:0000269|PubMed:20002912, ECO:0000269|PubMed:20377529,
ECO:0000269|PubMed:20818920, ECO:0000269|PubMed:21474609,
ECO:0000269|PubMed:21856931, ECO:0000269|PubMed:9532737,
ECO:0000269|PubMed:9605502}.
-!- DOMAIN: Contains 2 cytoplasmic nucleotide binding domains (NBDs).
The N-terminal NBD has ATPase activity. The 2 NBDs are asymmetric
and non-exchangeable and the drug efflux by CDR1 involves complex
interactions between the two halves of the protein.
{ECO:0000269|PubMed:12962507, ECO:0000269|PubMed:15850398,
ECO:0000269|PubMed:16622073, ECO:0000269|PubMed:20546701}.
-!- DISRUPTION PHENOTYPE: Leads to hypersusceptibility to the
antifungal agents terbinafine and amorolfine, and to the metabolic
inhibitors cycloheximide, brefeldin A, and fluphenazine. Shows a
decreased number of germ tube-forming cells in the presence of
estradiol when CDR2 is also deleted. {ECO:0000269|PubMed:16400181,
ECO:0000269|PubMed:8891134}.
-!- SIMILARITY: Belongs to the ABC transporter superfamily.
{ECO:0000255|PROSITE-ProRule:PRU01700}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CP017625; AOW28537.1; -; Genomic_DNA.
RefSeq; XP_723209.2; XM_718116.2.
ProteinModelPortal; Q5ANA3; -.
SMR; Q5ANA3; -.
PRIDE; Q5ANA3; -.
GeneID; 3635237; -.
KEGG; cal:CAALFM_C305220WA; -.
CGD; CAL0000186516; CDR1.
OrthoDB; EOG092C1HKF; -.
PRO; PR:Q5ANA3; -.
Proteomes; UP000000559; Chromosome 3.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0016021; C:integral component of membrane; IDA:CGD.
GO; GO:0016020; C:membrane; NAS:CGD.
GO; GO:0045121; C:membrane raft; IGI:CGD.
GO; GO:0005886; C:plasma membrane; IDA:CGD.
GO; GO:0005524; F:ATP binding; IDA:CGD.
GO; GO:0016887; F:ATPase activity; IDA:CGD.
GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:GO_Central.
GO; GO:0045118; F:azole transporter activity; IDA:CGD.
GO; GO:0015238; F:drug transmembrane transporter activity; IMP:CGD.
GO; GO:0015244; F:fluconazole transporter activity; IDA:CGD.
GO; GO:0017111; F:nucleoside-triphosphatase activity; IDA:CGD.
GO; GO:0000166; F:nucleotide binding; IDA:CGD.
GO; GO:0005548; F:phospholipid transporter activity; IDA:CGD.
GO; GO:0004012; F:phospholipid-translocating ATPase activity; IDA:CGD.
GO; GO:0045117; P:azole transport; IDA:CGD.
GO; GO:0035690; P:cellular response to drug; IMP:CGD.
GO; GO:0034599; P:cellular response to oxidative stress; IGI:CGD.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; IGI:CGD.
GO; GO:0046618; P:drug export; IDA:CGD.
GO; GO:0006855; P:drug transmembrane transport; IGI:CGD.
GO; GO:0015903; P:fluconazole transport; IDA:CGD.
GO; GO:0045332; P:phospholipid translocation; IDA:CGD.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
GO; GO:0046898; P:response to cycloheximide; IEA:UniProtKB-KW.
CDD; cd03233; ABCG_PDR_domain1; 1.
CDD; cd03232; ABCG_PDR_domain2; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR013525; ABC_2_trans.
InterPro; IPR029481; ABC_trans_N.
InterPro; IPR003439; ABC_transporter-like.
InterPro; IPR017871; ABC_transporter_CS.
InterPro; IPR034001; ABCG_PDR_1.
InterPro; IPR034003; ABCG_PDR_2.
InterPro; IPR005285; Drug-R_PDR/CDR.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR010929; PDR_CDR_ABC.
Pfam; PF01061; ABC2_membrane; 2.
Pfam; PF00005; ABC_tran; 2.
Pfam; PF14510; ABC_trans_N; 1.
Pfam; PF06422; PDR_CDR; 1.
SMART; SM00382; AAA; 2.
SUPFAM; SSF52540; SSF52540; 2.
TIGRFAMs; TIGR00956; 3a01205; 1.
PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
1: Evidence at protein level;
Antibiotic resistance; ATP-binding; Cell membrane; Coiled coil;
Complete proteome; Cycloheximide resistance; Membrane;
Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1501 Pleiotropic ABC efflux transporter of
multiple drugs CDR1.
/FTId=PRO_0000431582.
TOPO_DOM 1 513 Cytoplasmic. {ECO:0000305}.
TRANSMEM 514 534 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 535 548 Extracellular. {ECO:0000305}.
TRANSMEM 549 569 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 570 597 Cytoplasmic. {ECO:0000305}.
TRANSMEM 598 618 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 619 622 Extracellular. {ECO:0000305}.
TRANSMEM 623 643 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 644 654 Cytoplasmic. {ECO:0000305}.
TRANSMEM 655 675 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 676 764 Extracellular. {ECO:0000305}.
TRANSMEM 765 785 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 786 1195 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1196 1216 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 1217 1229 Extracellular. {ECO:0000305}.
TRANSMEM 1230 1250 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 1251 1280 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1281 1301 Helical; Name=9. {ECO:0000255}.
TOPO_DOM 1302 1314 Extracellular. {ECO:0000305}.
TRANSMEM 1315 1335 Helical; Name=10. {ECO:0000255}.
TOPO_DOM 1336 1355 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1356 1376 Helical; Name=11. {ECO:0000255}.
TOPO_DOM 1377 1466 Extracellular. {ECO:0000305}.
TRANSMEM 1467 1487 Helical; Name=12. {ECO:0000255}.
TOPO_DOM 1488 1501 Cytoplasmic. {ECO:0000305}.
DOMAIN 150 404 ABC transporter 1. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
DOMAIN 859 1103 ABC transporter 2. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
NP_BIND 895 902 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00434}.
REGION 2 512 NBD1. {ECO:0000303|PubMed:20546701}.
REGION 786 1195 NBD2. {ECO:0000303|PubMed:20546701}.
COILED 1137 1164 {ECO:0000255}.
MUTAGEN 193 193 C->A: Impairs NBD-mediated ATP
hydrolysis.
{ECO:0000269|PubMed:12962507}.
MUTAGEN 232 232 D->K: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:14665469}.
MUTAGEN 296 296 G->D: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:14665469}.
MUTAGEN 326 326 W->A: Impairs NBD ATP-binding.
{ECO:0000269|PubMed:15850398}.
MUTAGEN 551 551 F->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 552 552 F->A: Leads to reduced drug efflux but
shows normal ATPase activity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 559 559 F->A: Leads to reduced drug efflux and
ATPase activity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 561 561 S->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 564 564 E->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 604 604 M->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 609 609 N->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 629 629 W->L: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:16782311}.
MUTAGEN 644 644 R->A: Leads to reduced drug efflux but
shows normal ATPase activity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 658 658 T->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 659 659 P->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 660 660 A->G: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 661 661 T->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 662 662 V->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 663 663 L->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 664 664 L->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 665 665 L->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 667 667 M->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 668 668 V->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 669 669 I->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 670 670 Y->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 671 671 T->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 672 672 G->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 673 673 F->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 674 674 V->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 675 675 I->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 676 676 P->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 677 677 T->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 678 678 P->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:19393219}.
MUTAGEN 774 774 F->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:14665469}.
MUTAGEN 774 774 Missing: Leads to mislocalization and
general drug-sensitivity.
{ECO:0000269|PubMed:14665469}.
MUTAGEN 995 995 G->S: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:14665469}.
MUTAGEN 1000 1000 G->C: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:14665469}.
MUTAGEN 1056 1056 C->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22166216}.
MUTAGEN 1091 1091 C->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22166216}.
MUTAGEN 1106 1106 C->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22166216}.
MUTAGEN 1230 1230 F->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 1294 1294 C->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22166216}.
MUTAGEN 1331 1331 T->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 1336 1336 C->A: Leads to reduced drug efflux and
ATPase activity.
{ECO:0000269|PubMed:22166216,
ECO:0000269|PubMed:23824183}.
MUTAGEN 1346 1346 A->G: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:15937063}.
MUTAGEN 1347 1347 A->G: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:15937063}.
MUTAGEN 1351 1351 T->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:15937063}.
MUTAGEN 1351 1351 T->F: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:14665469,
ECO:0000269|PubMed:15190023}.
MUTAGEN 1355 1355 T->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:15937063}.
MUTAGEN 1358 1358 L->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:15937063}.
MUTAGEN 1360 1360 F->A: Leads to reduced drug efflux but
shows normal ATPase activity.
{ECO:0000269|PubMed:23824183}.
MUTAGEN 1418 1418 C->Y: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:14665469}.
MUTAGEN 1449 1449 T->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:14665469}.
MUTAGEN 1456 1456 V->A: Leads to selective drug-
sensitivity.
{ECO:0000269|PubMed:14665469}.
SEQUENCE 1501 AA; 169984 MW; 2403EBE361B3A332 CRC64;
MSDSKMSSQD ESKLEKAISQ DSSSENHSIN EYHGFDAHTS ENIQNLARTF THDSFKDDSS
AGLLKYLTHM SEVPGVNPYE HEEINNDQLN PDSENFNAKF WVKNLRKLFE SDPEYYKPSK
LGIGYRNLRA YGVANDSDYQ PTVTNALWKL ATEGFRHFQK DDDSRYFDIL KSMDAIMRPG
ELTVVLGRPG AGCSTLLKTI AVNTYGFHIG KESQITYDGL SPHDIERHYR GDVIYSAETD
VHFPHLSVGD TLEFAARLRT PQNRGEGIDR ETYAKHMASV YMATYGLSHT RNTNVGNDFV
RGVSGGERKR VSIAEASLSG ANIQCWDNAT RGLDSATALE FIRALKTSAV ILDTTPLIAI
YQCSQDAYDL FDKVVVLYEG YQIFFGKATK AKEYFEKMGW KCPQRQTTAD FLTSLTNPAE
REPLPGYEDK VPRTAQEFET YWKNSPEYAE LTKEIDEYFV ECERSNTRET YRESHVAKQS
NNTRPASPYT VSFFMQVRYG VARNFLRMKG DPSIPIFSVF GQLVMGLILS SVFYNLSQTT
GSFYYRGAAM FFAVLFNAFS SLLEIMSLFE ARPIVEKHKK YALYRPSADA LASIISELPV
KLAMSMSFNF VFYFMVNFRR NPGRFFFYWL MCIWCTFVMS HLFRSIGAVS TSISGAMTPA
TVLLLAMVIY TGFVIPTPSM LGWSRWINYI NPVGYVFESL MVNEFHGREF QCAQYVPSGP
GYENISRSNQ VCTAVGSVPG NEMVSGTNYL AGAYQYYNSH KWRNLGITIG FAVFFLAIYI
ALTEFNKGAM QKGEIVLFLK GSLKKHKRKT AASNKGDIEA GPVAGKLDYQ DEAEAVNNEK
FTEKGSTGSV DFPENREIFF WRDLTYQVKI KKEDRVILDH VDGWVKPGQI TALMGASGAG
KTTLLNCLSE RVTTGIITDG ERLVNGHALD SSFQRSIGYV QQQDVHLETT TVREALQFSA
YLRQSNKISK KEKDDYVDYV IDLLEMTDYA DALVGVAGEG LNVEQRKRLT IGVELVAKPK
LLLFLDEPTS GLDSQTAWSI CKLMRKLADH GQAILCTIHQ PSALIMAEFD RLLFLQKGGR
TAYFGELGEN CQTMINYFEK YGADPCPKEA NPAEWMLQVV GAAPGSHAKQ DYFEVWRNSS
EYQAVREEIN RMEAELSKLP RDNDPEALLK YAAPLWKQYL LVSWRTIVQD WRSPGYIYSK
IFLVVSAALF NGFSFFKAKN NMQGLQNQMF SVFMFFIPFN TLVQQMLPYF VKQRDVYEVR
EAPSRTFSWF AFIAGQITSE IPYQVAVGTI AFFCWYYPLG LYNNATPTDS VNPRGVLMWM
LVTAFYVYTA TMGQLCMSFS ELADNAANLA TLLFTMCLNF CGVLAGPDVL PGFWIFMYRC
NPFTYLVQAM LSTGLANTFV KCAEREYVSV KPPNGESCST YLDPYIKFAG GYFETRNDGS
CAFCQMSSTN TFLKSVNSLY SERWRNFGIF IAFIAINIIL TVIFYWLARV PKGNREKKNK
K


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