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Multidrug resistance protein 1 (Benomyl resistance protein 1)

 MDR1_CANAL              Reviewed;         564 AA.
Q5ABU7; A0A1D8PQ31;
07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
12-APR-2017, sequence version 2.
23-MAY-2018, entry version 90.
RecName: Full=Multidrug resistance protein 1 {ECO:0000303|PubMed:7726508};
AltName: Full=Benomyl resistance protein 1;
Name=MDR1 {ECO:0000303|PubMed:7726508}; Synonyms=BEN, BMR1;
OrderedLocusNames=CAALFM_C603170CA; ORFNames=CaO19.13047, CaO19.5604;
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]
FUNCTION.
PubMed=2062311; DOI=10.1007/BF00259685;
Fling M.E., Kopf J., Tamarkin A., Gorman J.A., Smith H.A., Koltin Y.;
"Analysis of a Candida albicans gene that encodes a novel mechanism
for resistance to benomyl and methotrexate.";
Mol. Gen. Genet. 227:318-329(1991).
[5]
FUNCTION.
PubMed=8031026; DOI=10.1128/AAC.38.4.648;
Ben-Yaacov R., Knoller S., Caldwell G.A., Becker J.M., Koltin Y.;
"Candida albicans gene encoding resistance to benomyl and methotrexate
is a multidrug resistance gene.";
Antimicrob. Agents Chemother. 38:648-652(1994).
[6]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=7726508; DOI=10.1128/AAC.39.2.422;
Goldway M., Teff D., Schmidt R., Oppenheim A.B., Koltin Y.;
"Multidrug resistance in Candida albicans: disruption of the BENr
gene.";
Antimicrob. Agents Chemother. 39:422-426(1995).
[7]
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).
[8]
FUNCTION.
PubMed=9210670;
White T.C.;
"Increased mRNA levels of ERG16, CDR, and MDR1 correlate with
increases in azole resistance in Candida albicans isolates from a
patient infected with human immunodeficiency virus.";
Antimicrob. Agents Chemother. 41:1482-1487(1997).
[9]
IDENTIFICATION.
PubMed=9046086;
DOI=10.1002/(SICI)1097-0061(199701)13:1<43::AID-YEA56>3.0.CO;2-J;
Goffeau A., Park J., Paulsen I.T., Jonniaux J.L., Dinh T., Mordant P.,
Saier M.H. Jr.;
"Multidrug-resistant transport proteins in yeast: complete inventory
and phylogenetic characterization of yeast open reading frames with
the major facilitator superfamily.";
Yeast 13:43-54(1997).
[10]
FUNCTION.
PubMed=9756759;
Marr K.A., Lyons C.N., Rustad T.R., Bowden R.A., White T.C.,
Rustad T.;
"Rapid, transient fluconazole resistance in Candida albicans is
associated with increased mRNA levels of CDR.";
Antimicrob. Agents Chemother. 42:2584-2589(1998).
[11]
FUNCTION.
PubMed=9797228;
Lopez-Ribot J.L., McAtee R.K., Lee L.N., Kirkpatrick W.R., White T.C.,
Sanglard D., Patterson T.F.;
"Distinct patterns of gene expression associated with development of
fluconazole resistance in serial candida albicans isolates from human
immunodeficiency virus-infected patients with oropharyngeal
candidiasis.";
Antimicrob. Agents Chemother. 42:2932-2937(1998).
[12]
INDUCTION.
PubMed=9922230;
Alarco A.M., Raymond M.;
"The bZip transcription factor Cap1p is involved in multidrug
resistance and oxidative stress response in Candida albicans.";
J. Bacteriol. 181:700-708(1999).
[13]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10844673; DOI=10.1046/j.1365-2958.2000.01899.x;
Wirsching S., Michel S., Morschhauser J.;
"Targeted gene disruption in Candida albicans wild-type strains: the
role of the MDR1 gene in fluconazole resistance of clinical Candida
albicans isolates.";
Mol. Microbiol. 36:856-865(2000).
[14]
FUNCTION.
PubMed=11568478; DOI=10.1007/BF02703742;
Kohli A., Gupta V., Krishnamurthy S., Hasnain S.E., Prasad R.;
"Specificity of drug transport mediated by CaMDR1: a major facilitator
of Candida albicans.";
J. Biosci. 26:333-339(2001).
[15]
INDUCTION.
PubMed=14688046; DOI=10.1093/jac/dkh040;
Lee M.K., Williams L.E., Warnock D.W., Arthington-Skaggs B.A.;
"Drug resistance genes and trailing growth in Candida albicans
isolates.";
J. Antimicrob. Chemother. 53:217-224(2004).
[16]
INDUCTION.
PubMed=15980350; DOI=10.1128/AAC.49.7.2785-2792.2005;
Harry J.B., Oliver B.G., Song J.L., Silver P.M., Little J.T.,
Choiniere J., White T.C.;
"Drug-induced regulation of the MDR1 promoter in Candida albicans.";
Antimicrob. Agents Chemother. 49:2785-2792(2005).
[17]
FUNCTION.
PubMed=16569853; DOI=10.1128/AAC.50.4.1365-1371.2006;
Hiller D., Sanglard D., Morschhaeuser J.;
"Overexpression of the MDR1 gene is sufficient to confer increased
resistance to toxic compounds in Candida albicans.";
Antimicrob. Agents Chemother. 50:1365-1371(2006).
[18]
INDUCTION.
PubMed=16801405; DOI=10.1128/AAC.00196-06;
Hiller D., Stahl S., Morschhaeuser J.;
"Multiple cis-acting sequences mediate upregulation of the MDR1 efflux
pump in a fluconazole-resistant clinical Candida albicans isolate.";
Antimicrob. Agents Chemother. 50:2300-2308(2006).
[19]
INDUCTION.
PubMed=17041190; DOI=10.1128/EC.00243-06;
Riggle P.J., Kumamoto C.A.;
"Transcriptional regulation of MDR1, encoding a drug efflux
determinant, in fluconazole-resistant Candida albicans strains through
an Mcm1p binding site.";
Eukaryot. Cell 5:1957-1968(2006).
[20]
INDUCTION.
PubMed=17159223; DOI=10.1099/mic.0.29277-0;
Rognon B., Kozovska Z., Coste A.T., Pardini G., Sanglard D.;
"Identification of promoter elements responsible for the regulation of
MDR1 from Candida albicans, a major facilitator transporter involved
in azole resistance.";
Microbiology 152:3701-3722(2006).
[21]
FUNCTION.
PubMed=17325226; DOI=10.1128/AAC.00182-07;
Cheng S., Clancy C.J., Nguyen K.T., Clapp W., Nguyen M.H.;
"A Candida albicans petite mutant strain with uncoupled oxidative
phosphorylation overexpresses MDR1 and has diminished susceptibility
to fluconazole and voriconazole.";
Antimicrob. Agents Chemother. 51:1855-1858(2007).
[22]
INDUCTION, AND FUNCTION.
PubMed=17983269; DOI=10.1371/journal.ppat.0030164;
Morschhauser J., Barker K.S., Liu T.T., Blass-Warmuth J.,
Homayouni R., Rogers P.D.;
"The transcription factor Mrr1p controls expression of the MDR1 efflux
pump and mediates multidrug resistance in Candida albicans.";
PLoS Pathog. 3:E164-E164(2007).
[23]
INDUCTION.
PubMed=18238892; DOI=10.1093/jac/dkm513;
Vogel M., Hartmann T., Koeberle M., Treiber M., Autenrieth I.B.,
Schumacher U.K.;
"Rifampicin induces MDR1 expression in Candida albicans.";
J. Antimicrob. Chemother. 61:541-547(2008).
[24]
INDUCTION.
PubMed=18390649; DOI=10.1128/EC.00070-08;
Znaidi S., Weber S., Al-Abdin O.Z., Bomme P., Saidane S., Drouin S.,
Lemieux S., De Deken X., Robert F., Raymond M.;
"Genomewide location analysis of Candida albicans Upc2p, a regulator
of sterol metabolism and azole drug resistance.";
Eukaryot. Cell 7:836-847(2008).
[25]
INDUCTION.
PubMed=19395663; DOI=10.1128/EC.00002-09;
Znaidi S., Barker K.S., Weber S., Alarco A.M., Liu T.T., Boucher G.,
Rogers P.D., Raymond M.;
"Identification of the Candida albicans Cap1p regulon.";
Eukaryot. Cell 8:806-820(2009).
[26]
INDUCTION.
PubMed=19527793; DOI=10.1016/j.fgb.2009.06.003;
Chen C.G., Yang Y.L., Tseng K.Y., Shih H.I., Liou C.H., Lin C.C.,
Lo H.J.;
"Rep1p negatively regulating MDR1 efflux pump involved in drug
resistance in Candida albicans.";
Fungal Genet. Biol. 46:714-720(2009).
[27]
INDUCTION.
PubMed=21136999; DOI=10.1002/prca.200800252;
Hoehamer C.F., Cummings E.D., Hilliard G.M., Morschhaeuser J.,
Rogers P.D.;
"Proteomic analysis of Mrr1p- and Tac1p-associated differential
protein expression in azole-resistant clinical isolates of Candida
albicans.";
Proteomics Clin. Appl. 3:968-978(2009).
[28]
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).
[29]
FUNCTION.
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).
[30]
INDUCTION.
PubMed=21343453; DOI=10.1128/AAC.01467-10;
Mogavero S., Tavanti A., Senesi S., Rogers P.D., Morschhaeuser J.;
"Differential requirement of the transcription factor Mcm1 for
activation of the Candida albicans multidrug efflux pump MDR1 by its
regulators Mrr1 and Cap1.";
Antimicrob. Agents Chemother. 55:2061-2066(2011).
[31]
INDUCTION.
PubMed=21402859; DOI=10.1128/AAC.01343-10;
Schubert S., Barker K.S., Znaidi S., Schneider S., Dierolf F.,
Dunkel N., Aid M., Boucher G., Rogers P.D., Raymond M.,
Morschhaeuser J.;
"Regulation of efflux pump expression and drug resistance by the
transcription factors Mrr1, Upc2, and Cap1 in Candida albicans.";
Antimicrob. Agents Chemother. 55:2212-2223(2011).
[32]
INDUCTION.
PubMed=21685320; DOI=10.1128/EC.05100-11;
Schubert S., Popp C., Rogers P.D., Morschhauser J.;
"Functional dissection of a Candida albicans zinc cluster
transcription factor, the multidrug resistance regulator Mrr1.";
Eukaryot. Cell 10:1110-1121(2011).
[33]
SUBCELLULAR LOCATION, FUNCTION, DOMAIN, AND MUTAGENESIS OF GLU-296;
LYS-300; LYS-306; LYS-308; ARG-309; ASP-317; ARG-318; GLU-322;
GLU-324; GLU-326 AND LYS-329.
PubMed=22587419; DOI=10.1042/BJ20120190;
Mandal A., Kumar A., Singh A., Lynn A.M., Kapoor K., Prasad R.;
"A key structural domain of the Candida albicans Mdr1 protein.";
Biochem. J. 445:313-322(2012).
[34]
INDUCTION.
PubMed=22615278; DOI=10.1128/AAC.00264-12;
Sasse C., Schillig R., Reimund A., Merk J., Morschhauser J.;
"Inducible and constitutive activation of two polymorphic promoter
alleles of the Candida albicans multidrug efflux pump MDR1.";
Antimicrob. Agents Chemother. 56:4490-4494(2012).
[35]
INDUCTION.
PubMed=24051054; DOI=10.1016/j.ijantimicag.2013.07.013;
Morio F., Pagniez F., Besse M., Gay-andrieu F., Miegeville M.,
Le Pape P.;
"Deciphering azole resistance mechanisms with a focus on transcription
factor-encoding genes TAC1, MRR1 and UPC2 in a set of fluconazole-
resistant clinical isolates of Candida albicans.";
Int. J. Antimicrob. Agents 42:410-415(2013).
[36]
INDUCTION.
PubMed=23527892; DOI=10.3109/13880209.2013.764537;
Zhang X., Guo H., Gao L., Song Y., Li S., Zhang H.;
"Molecular mechanisms underlying the tetrandrine-mediated reversal of
the fluconazole resistance of Candida albicans.";
Pharm. Biol. 51:749-752(2013).
[37]
INDUCTION.
PubMed=24936593; DOI=10.1128/AAC.03065-14;
Ramirez-Zavala B., Mogavero S., Schoeller E., Sasse C., Rogers P.D.,
Morschhaeuser J.;
"SAGA/ADA complex subunit Ada2 is required for Cap1- but not Mrr1-
mediated upregulation of the Candida albicans multidrug efflux pump
MDR1.";
Antimicrob. Agents Chemother. 58:5102-5110(2014).
[38]
INDUCTION.
PubMed=24723295; DOI=10.1007/s00253-014-5719-2;
Shafreen R.M., Raja Mohamed B.S., Muthamil S., Subramanian M.,
Pandian S.K., Shunmugiah K.P.;
"Inhibition of Candida albicans virulence factors by novel
levofloxacin derivatives.";
Appl. Microbiol. Biotechnol. 98:6775-6785(2014).
-!- FUNCTION: Plasma membrane multidrug efflux pump that confers
resistance to numerous chemicals including azoles such as
fluconazole, voriconazole, and benztriazoles, as well as to
benomyl, cycloheximide, methotrexate, 4-nitroquinoline-N-oxide,
sulfometuron methyl, cerulenin, and brefeldin A.
{ECO:0000269|PubMed:10844673, ECO:0000269|PubMed:11568478,
ECO:0000269|PubMed:16569853, ECO:0000269|PubMed:17325226,
ECO:0000269|PubMed:17983269, ECO:0000269|PubMed:20348384,
ECO:0000269|PubMed:2062311, ECO:0000269|PubMed:22587419,
ECO:0000269|PubMed:7726508, ECO:0000269|PubMed:8031026,
ECO:0000269|PubMed:8891134, ECO:0000269|PubMed:9210670,
ECO:0000269|PubMed:9756759, ECO:0000269|PubMed:9797228,
ECO:0000303|PubMed:9046086}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22587419};
Multi-pass membrane protein {ECO:0000255}.
-!- INDUCTION: Constitutive, high-level transcription is commonly
observed in laboratory and clinical strains of Candida albicans
that are resistant to the antifungal drug fluconazole. Multiple
cis-acting sequences within the promoter mediate its activation.
One, a benomyl response element (BRE), is situated at position
-296 to -260. It is required for benomyl-dependent MDR1 up-
regulation and is also necessary for constitutive high expression
of MDR1. A second element, termed H(2)O(2) response element (HRE),
is situated at position -561 to -520. The HRE is required for
H(2)O(2)-dependent MDR1 up-regulation, but dispensable for
constitutive high expression. Two potential binding sites
(TTAG/CTAA) for the transcription factor CAP1 lie within the HRE.
Expression is induced by fluconazole, rifampicin, methotrexate,
diethylmaleate, diamide, 4-nitroquinoline-N-oxide, benomyl, o-
phenanthroline (OP), hydrogen peroxide, methyl methanesulfonate,
and sulfometuron methyl. Expression is down-regulated by
tetrandrine and levofloxacin derivatives. Transcription is
positiveley regulated by ADA2, CAP1, MRR1, UPC2, and TAC1; and
negatively regulated by REP1. Transcription is also regulated by
the general transcription factor MCM1. MCM1 is dispensable for up-
regulation by H(2)O(2) but is required for full induction by
benomyl. {ECO:0000269|PubMed:14688046,
ECO:0000269|PubMed:15980350, ECO:0000269|PubMed:16801405,
ECO:0000269|PubMed:17041190, ECO:0000269|PubMed:17159223,
ECO:0000269|PubMed:17983269, ECO:0000269|PubMed:18238892,
ECO:0000269|PubMed:18390649, ECO:0000269|PubMed:19395663,
ECO:0000269|PubMed:19420894, ECO:0000269|PubMed:19527793,
ECO:0000269|PubMed:21136999, ECO:0000269|PubMed:21343453,
ECO:0000269|PubMed:21402859, ECO:0000269|PubMed:21685320,
ECO:0000269|PubMed:22615278, ECO:0000269|PubMed:23527892,
ECO:0000269|PubMed:24051054, ECO:0000269|PubMed:24723295,
ECO:0000269|PubMed:24936593, ECO:0000269|PubMed:9922230}.
-!- DOMAIN: The central cytoplasmic loop (residues 295 to 350) is
critical for the function, but unlike other homologous proteins,
has no apparent role in imparting substrate specificity or in the
recruitment of the transporter protein.
{ECO:0000269|PubMed:22587419}.
-!- DISRUPTION PHENOTYPE: Leads to enhanced susceptibility against
fluconazole, methotrexate, 4-nitroquinoline-N-oxide, and
cycloheximide. {ECO:0000269|PubMed:10844673,
ECO:0000269|PubMed:7726508, ECO:0000269|PubMed:8891134}.
-!- MISCELLANEOUS: The overexpression of MDR1 is a frequent cause of
resistance to the widely used antimycotic agent fluconazole and
other toxic compounds in the pathogenic yeast Candida albicans.
{ECO:0000305}.
-!- SIMILARITY: Belongs to the major facilitator superfamily. CAR1
family. {ECO:0000305}.
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EMBL; CP017628; AOW30248.1; -; Genomic_DNA.
RefSeq; XP_719165.2; XM_714072.2.
ProteinModelPortal; Q5ABU7; -.
ChEMBL; CHEMBL5336; -.
EnsemblFungi; AOW30248; AOW30248; CAALFM_C603170CA.
GeneID; 3639260; -.
KEGG; cal:CAALFM_C603170CA; -.
CGD; CAL0000173998; MDR1.
HOGENOM; HOG000160689; -.
KO; K08158; -.
OrthoDB; EOG092C2079; -.
PRO; PR:Q5ABU7; -.
Proteomes; UP000000559; Chromosome 6.
GO; GO:0005887; C:integral component of plasma membrane; IDA:CGD.
GO; GO:0015238; F:drug transmembrane transporter activity; IDA:CGD.
GO; GO:0015244; F:fluconazole transmembrane transporter activity; IDA:CGD.
GO; GO:0035690; P:cellular response to drug; IMP:CGD.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
GO; GO:0046618; P:drug export; IGI:CGD.
GO; GO:0006855; P:drug transmembrane transport; IDA:CGD.
GO; GO:0015903; P:fluconazole transport; IDA:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:0046898; P:response to cycloheximide; IEA:UniProtKB-KW.
GO; GO:0042493; P:response to drug; IDA:CGD.
CDD; cd06174; MFS; 1.
InterPro; IPR011701; MFS.
InterPro; IPR020846; MFS_dom.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR004734; Multidrug-R.
Pfam; PF07690; MFS_1; 1.
SUPFAM; SSF103473; SSF103473; 1.
TIGRFAMs; TIGR00880; 2_A_01_02; 1.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
Antibiotic resistance; Cell membrane; Complete proteome;
Cycloheximide resistance; Glycoprotein; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 564 Multidrug resistance protein 1.
/FTId=PRO_0000431619.
TOPO_DOM 1 115 Cytoplasmic. {ECO:0000305}.
TRANSMEM 116 136 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 137 151 Extracellular. {ECO:0000305}.
TRANSMEM 152 172 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 173 183 Cytoplasmic. {ECO:0000305}.
TRANSMEM 184 204 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 205 206 Extracellular. {ECO:0000305}.
TRANSMEM 207 227 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 228 242 Cytoplasmic. {ECO:0000305}.
TRANSMEM 243 263 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 264 273 Extracellular. {ECO:0000305}.
TRANSMEM 274 294 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 295 350 Cytoplasmic. {ECO:0000305}.
TRANSMEM 351 371 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 372 390 Extracellular. {ECO:0000305}.
TRANSMEM 391 411 Helical; Name=8. {ECO:0000255}.
TOPO_DOM 412 428 Cytoplasmic. {ECO:0000305}.
TRANSMEM 429 449 Helical; Name=9. {ECO:0000255}.
TOPO_DOM 450 455 Extracellular. {ECO:0000305}.
TRANSMEM 456 476 Helical; Name=10. {ECO:0000255}.
TOPO_DOM 477 503 Cytoplasmic. {ECO:0000305}.
TRANSMEM 504 524 Helical; Name=11. {ECO:0000255}.
TOPO_DOM 525 528 Extracellular. {ECO:0000305}.
TRANSMEM 529 549 Helical; Name=12. {ECO:0000255}.
TOPO_DOM 550 564 Cytoplasmic. {ECO:0000305}.
COMPBIAS 68 74 Poly-Ser. {ECO:0000255}.
COMPBIAS 81 87 Poly-Asn. {ECO:0000255}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 296 296 E->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 300 300 K->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 306 306 K->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 308 308 K->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 309 309 R->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 317 317 D->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 318 318 R->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 322 322 E->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 324 324 E->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 326 326 E->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
MUTAGEN 329 329 K->A: Leads to general drug-sensitivity.
{ECO:0000269|PubMed:22587419}.
SEQUENCE 564 AA; 62904 MW; BC0DF5BEA61D5C4F CRC64;
MHYRFLRDSF VGRVTYHLSK HKYFAHPEEA KDYIVPEKYL ADYKPTLADD TSINFEKEEI
DNQGEPNSSQ SSSSNNTIVD NNNNNDNDVD GDKIVVTWDG DDDPENPQNW PTLQKAFFIF
QISFLTTSVY MGSAVYTPGI EELMHDFGIG RVVATLPLTL FVIGYGVGPL VFSPMSENAI
FGRTSIYIIT LFLFVILQIP TALVNNIAGL CILRFLGGFF ASPCLATGGA SVADVVKFWN
LPVGLAAWSL GAVCGPSFGP FFGSILTVKA SWRWTFWFMC IISGFSFVML CFTLPETFGK
TLLYRKAKRL RAITGNDRIT SEGEVENSKM TSHELIIDTL WRPLEITVME PVVLLINIYI
AMVYSILYLF FEVFPIYFVG VKHFTLVELG TTYMSIVIGI VIAAFIYIPV IRQKFTKPIL
RQEQVFPEVF IPIAIVGGIL LTSGLFIFGW SANRTTHWVG PLFGAATTAS GAFLIFQTLF
NFMGASFKPH YIASVFASND LFRSVIASVF PLFGAPLFDN LATPEYPVAW GSSVLGFITL
VMIAIPVLFY LNGPKLRARS KYAN


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