ID PDH1_CANGA Reviewed; 1542 AA.
AC O74208; Q6FUK6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Pleiotropic ABC efflux transporter of multiple drugs PDH1 {ECO:0000303|PubMed:9661006};
DE AltName: Full=P leiomorphic drug resistance homolog 1 {ECO:0000303|PubMed:9661006};
DE AltName: Full=Pleiotropic drug resistance protein 2 {ECO:0000303|PubMed:11257032};
GN Name=PDH1 {ECO:0000303|PubMed:9661006};
GN Synonyms=CDR2 {ECO:0000303|PubMed:11257032}, CGR1;
GN OrderedLocusNames=CAGL0F02717g;
OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 90030 / DSM 11226 / NCCLS 84;
RX PubMed=9661006; DOI=10.1128/aac.42.7.1695;
RA Miyazaki H., Miyazaki Y., Geber A., Parkinson T., Hitchcock C.,
RA Falconer D.J., Ward D.J., Marsden K., Bennett J.E.;
RT "Fluconazole resistance associated with drug efflux and increased
RT transcription of a drug transporter gene, PDH1, in Candida glabrata.";
RL Antimicrob. Agents Chemother. 42:1695-1701(1998).
RN [2]
RP SEQUENCE REVISION.
RA Izumikawa K., Miyazaki Y., Miyazaki H., Bennett J.E.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11257032; DOI=10.1128/aac.45.4.1174-1183.2001;
RA Sanglard D., Ischer F., Bille J.;
RT "Role of ATP-binding-cassette transporter genes in high-frequency
RT acquisition of resistance to azole antifungals in Candida glabrata.";
RL Antimicrob. Agents Chemother. 45:1174-1183(2001).
RN [5]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=12244114; DOI=10.1074/jbc.m207817200;
RA Wada S., Niimi M., Niimi K., Holmes A.R., Monk B.C., Cannon R.D.,
RA Uehara Y.;
RT "Candida glabrata ATP-binding cassette transporters Cdr1p and Pdh1p
RT expressed in a Saccharomyces cerevisiae strain deficient in membrane
RT transporters show phosphorylation-dependent pumping properties.";
RL J. Biol. Chem. 277:46809-46821(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12557277; DOI=10.1002/yea.962;
RA Izumikawa K., Kakeya H., Tsai H.F., Grimberg B., Bennett J.E.;
RT "Function of Candida glabrata ABC transporter gene, PDH1.";
RL Yeast 20:249-261(2003).
RN [7]
RP FUNCTION.
RX PubMed=15105134; DOI=10.1128/aac.48.5.1773-1777.2004;
RA Bennett J.E., Izumikawa K., Marr K.A.;
RT "Mechanism of increased fluconazole resistance in Candida glabrata during
RT prophylaxis.";
RL Antimicrob. Agents Chemother. 48:1773-1777(2004).
RN [8]
RP FUNCTION, AND INDUCTION.
RX PubMed=15388433; DOI=10.1128/aac.48.10.3773-3781.2004;
RA Vermitsky J.P., Edlind T.D.;
RT "Azole resistance in Candida glabrata: coordinate upregulation of multidrug
RT transporters and evidence for a Pdr1-like transcription factor.";
RL Antimicrob. Agents Chemother. 48:3773-3781(2004).
RN [9]
RP FUNCTION, AND INDUCTION.
RX PubMed=16803598; DOI=10.1111/j.1365-2958.2006.05235.x;
RA Vermitsky J.P., Earhart K.D., Smith W.L., Homayouni R., Edlind T.D.,
RA Rogers P.D.;
RT "Pdr1 regulates multidrug resistance in Candida glabrata: gene disruption
RT and genome-wide expression studies.";
RL Mol. Microbiol. 61:704-722(2006).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=17581937; DOI=10.1128/jcm.00381-07;
RA Shin J.H., Chae M.J., Song J.W., Jung S.I., Cho D., Kee S.J., Kim S.H.,
RA Shin M.G., Suh S.P., Ryang D.W.;
RT "Changes in karyotype and azole susceptibility of sequential bloodstream
RT isolates from patients with Candida glabrata candidemia.";
RL J. Clin. Microbiol. 45:2385-2391(2007).
RN [11]
RP INDUCTION.
RX PubMed=18782778; DOI=10.1093/jac/dkn381;
RA Tumbarello M., Sanguinetti M., Trecarichi E.M., La Sorda M., Rossi M.,
RA de Carolis E., de Gaetano Donati K., Fadda G., Cauda R., Posteraro B.;
RT "Fungaemia caused by Candida glabrata with reduced susceptibility to
RT fluconazole due to altered gene expression: risk factors, antifungal
RT treatment and outcome.";
RL J. Antimicrob. Chemother. 62:1379-1385(2008).
RN [12]
RP INDUCTION.
RX PubMed=19196495; DOI=10.1016/j.ijantimicag.2008.11.011;
RA Berila N., Borecka S., Dzugasova V., Bojnansky J., Subik J.;
RT "Mutations in the CgPDR1 and CgERG11 genes in azole-resistant Candida
RT glabrata clinical isolates from Slovakia.";
RL Int. J. Antimicrob. Agents 33:574-578(2009).
RN [13]
RP INDUCTION, AND FUNCTION.
RX PubMed=18651314; DOI=10.1080/13693780802210726;
RA Song J.W., Shin J.H., Kee S.J., Kim S.H., Shin M.G., Suh S.P., Ryang D.W.;
RT "Expression of CgCDR1, CgCDR2, and CgERG11 in Candida glabrata biofilms
RT formed by bloodstream isolates.";
RL Med. Mycol. 47:545-548(2009).
RN [14]
RP INDUCTION.
RX PubMed=19148266; DOI=10.1371/journal.ppat.1000268;
RA Ferrari S., Ischer F., Calabrese D., Posteraro B., Sanguinetti M.,
RA Fadda G., Rohde B., Bauser C., Bader O., Sanglard D.;
RT "Gain of function mutations in CgPDR1 of Candida glabrata not only mediate
RT antifungal resistance but also enhance virulence.";
RL PLoS Pathog. 5:E1000268-E1000268(2009).
RN [15]
RP FUNCTION, AND INDUCTION.
RX PubMed=20038613; DOI=10.1128/aac.01138-09;
RA Chapeland-Leclerc F., Hennequin C., Papon N., Noel T., Girard A., Socie G.,
RA Ribaud P., Lacroix C.;
RT "Acquisition of flucytosine, azole, and caspofungin resistance in Candida
RT glabrata bloodstream isolates serially obtained from a hematopoietic stem
RT cell transplant recipient.";
RL Antimicrob. Agents Chemother. 54:1360-1362(2010).
RN [16]
RP INDUCTION.
RX PubMed=21282443; DOI=10.1128/aac.00791-10;
RA Lignell A., Loewdin E., Cars O., Sanglard D., Sjoelin J.;
RT "Voriconazole-induced inhibition of the fungicidal activity of amphotericin
RT B in Candida strains with reduced susceptibility to voriconazole: an effect
RT not predicted by the MIC value alone.";
RL Antimicrob. Agents Chemother. 55:1629-1637(2011).
RN [17]
RP INDUCTION.
RX PubMed=21321146; DOI=10.1128/aac.01271-10;
RA Ferrari S., Sanguinetti M., De Bernardis F., Torelli R., Posteraro B.,
RA Vandeputte P., Sanglard D.;
RT "Loss of mitochondrial functions associated with azole resistance in
RT Candida glabrata results in enhanced virulence in mice.";
RL Antimicrob. Agents Chemother. 55:1852-1860(2011).
RN [18]
RP INDUCTION.
RX PubMed=23229483; DOI=10.1128/aac.01278-12;
RA Noble J.A., Tsai H.F., Suffis S.D., Su Q., Myers T.G., Bennett J.E.;
RT "STB5 is a negative regulator of azole resistance in Candida glabrata.";
RL Antimicrob. Agents Chemother. 57:959-967(2013).
RN [19]
RP FUNCTION.
RX PubMed=24273749; DOI=10.3389/fcimb.2013.00074;
RA Abbes S., Mary C., Sellami H., Michel-Nguyen A., Ayadi A., Ranque S.;
RT "Interactions between copy number and expression level of genes involved in
RT fluconazole resistance in Candida glabrata.";
RL Front. Cell. Infect. Microbiol. 3:74-74(2013).
RN [20]
RP INDUCTION.
RX PubMed=25199772; DOI=10.1128/aac.03921-14;
RA Paul S., Bair T.B., Moye-Rowley W.S.;
RT "Identification of genomic binding sites for Candida glabrata Pdr1
RT transcription factor in wild-type and rho0 cells.";
RL Antimicrob. Agents Chemother. 58:6904-6912(2014).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24838041; DOI=10.1111/1567-1364.12164;
RA Walker B., Izumikawa K., Tsai H.F., Bennett J.E.;
RT "Milbemycin A4 oxime as a probe of azole transport in Candida glabrata.";
RL FEMS Yeast Res. 14:755-761(2014).
RN [22]
RP FUNCTION.
RX PubMed=26482310; DOI=10.1128/aac.02157-15;
RA Sanglard D., Coste A.T.;
RT "Activity of isavuconazole and other azoles against Candida clinical
RT isolates and yeast model systems with known azole resistance mechanisms.";
RL Antimicrob. Agents Chemother. 60:229-238(2016).
RN [23]
RP FUNCTION, AND INDUCTION.
RX PubMed=27486188; DOI=10.1128/mbio.00655-16;
RA Ben-Ami R., Zimmerman O., Finn T., Amit S., Novikov A., Wertheimer N.,
RA Lurie-Weinberger M., Berman J.;
RT "Heteroresistance to Fluconazole Is a Continuously Distributed Phenotype
RT among Candida glabrata Clinical Strains Associated with In Vivo
RT Persistence.";
RL MBio 7:0-0(2016).
RN [24]
RP FUNCTION, AND INDUCTION.
RX PubMed=29371812; DOI=10.5941/myco.2017.45.4.426;
RA Kim M., Lee H., Hwang S.Y., Lee I., Jung W.H.;
RT "Isolated from the urinary tract of a dog with diabetes mellitus.";
RL Mycobiology 45:426-429(2017).
RN [25]
RP INDUCTION.
RX PubMed=29507891; DOI=10.1128/msphere.00466-17;
RA Whaley S.G., Caudle K.E., Simonicova L., Zhang Q., Moye-Rowley W.S.,
RA Rogers P.D.;
RT "Jjj1 is a negative regulator of Pdr1-mediated fluconazole resistance in
RT Candida glabrata.";
RL MSphere 3:0-0(2018).
RN [26]
RP INDUCTION.
RX PubMed=29464833; DOI=10.1111/myc.12756;
RA Ni Q., Wang C., Tian Y., Dong D., Jiang C., Mao E., Peng Y.;
RT "CgPDR1 gain-of-function mutations lead to azole-resistance and increased
RT adhesion in clinical Candida glabrata strains.";
RL Mycoses 61:430-440(2018).
CC -!- FUNCTION: Pleiotropic ABC efflux transporter that confers resistance to
CC structurally and functionally unrelated compounds including caspofungin
CC or azoles such as fluconazole, itraconazole, posaconazole,
CC voriconazole, and isavuconazole (PubMed:11257032, PubMed:12244114,
CC PubMed:12557277, PubMed:15105134, PubMed:15388433, PubMed:16803598,
CC PubMed:17581937, PubMed:20038613, PubMed:24273749, PubMed:24838041,
CC PubMed:26482310, PubMed:27486188, PubMed:29371812). Does not play a
CC role in the azole resistance in mature biofilms (PubMed:18651314).
CC {ECO:0000269|PubMed:11257032, ECO:0000269|PubMed:12244114,
CC ECO:0000269|PubMed:12557277, ECO:0000269|PubMed:15105134,
CC ECO:0000269|PubMed:15388433, ECO:0000269|PubMed:16803598,
CC ECO:0000269|PubMed:17581937, ECO:0000269|PubMed:18651314,
CC ECO:0000269|PubMed:20038613, ECO:0000269|PubMed:24273749,
CC ECO:0000269|PubMed:24838041, ECO:0000269|PubMed:26482310,
CC ECO:0000269|PubMed:27486188, ECO:0000269|PubMed:29371812}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12244114};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Azole exposure induced expression via regulation by the
CC transcription factor PDR1 that stimulates gene expression via binding
CC to elements called pleiotropic drug response elements (PDREs)
CC (PubMed:15388433, PubMed:19148266, PubMed:25199772, PubMed:29464833).
CC Expression is up-regulated in azole-resistant isolates and in presence
CC of fluconazole (PubMed:9661006, PubMed:16803598, PubMed:17581937,
CC PubMed:18782778, PubMed:19196495, PubMed:20038613, PubMed:27486188,
CC PubMed:29371812). Loss of mitochondrial functions leads to increased
CC expression (PubMed:21321146). Expression is temporary increased during
CC the intermediate phase of biofilm development (PubMed:18651314).
CC Expression is down-regulated by the transcription factor STB5
CC (PubMed:23229483). Expression is negatively regulated by the
CC transcription factor JJJ1 via inactivation of the PDR1 transcriptional
CC pathway (PubMed:29507891). Expression is also decreased by amphotericin
CC B in voriconazole-resistant strains (PubMed:21282443).
CC {ECO:0000269|PubMed:15388433, ECO:0000269|PubMed:16803598,
CC ECO:0000269|PubMed:17581937, ECO:0000269|PubMed:18651314,
CC ECO:0000269|PubMed:18782778, ECO:0000269|PubMed:19148266,
CC ECO:0000269|PubMed:19196495, ECO:0000269|PubMed:20038613,
CC ECO:0000269|PubMed:21282443, ECO:0000269|PubMed:21321146,
CC ECO:0000269|PubMed:23229483, ECO:0000269|PubMed:25199772,
CC ECO:0000269|PubMed:27486188, ECO:0000269|PubMed:29371812,
CC ECO:0000269|PubMed:29464833, ECO:0000269|PubMed:29507891,
CC ECO:0000269|PubMed:9661006}.
CC -!- PTM: Phosphorylated by PKA. Dephosphorylated on glucose depletion and
CC independently rephosphorylated during glucose exposure or under stress.
CC {ECO:0000269|PubMed:12244114}.
CC -!- DISRUPTION PHENOTYPE: Increases the susceptibility to rhodamine 6G,
CC cycloheximide and chloramphenicol, and also increases rhodamine 6G
CC accumulation (PubMed:12557277). Suppresses the development of high-
CC frequency azole resistance (HFAR) in a medium containing fluconazole
CC (PubMed:11257032). Impairs the blockage of the efflux of fluconazole by
CC milbemycin A4 oxime when CDR1 is also deleted (PubMed:24838041).
CC {ECO:0000269|PubMed:11257032, ECO:0000269|PubMed:12557277,
CC ECO:0000269|PubMed:24838041}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; AF046120; AAC31800.2; -; Genomic_DNA.
DR EMBL; CR380952; CAG59012.1; -; Genomic_DNA.
DR RefSeq; XP_446088.1; XM_446088.1.
DR AlphaFoldDB; O74208; -.
DR SMR; O74208; -.
DR STRING; 284593.O74208; -.
DR EnsemblFungi; CAGL0F02717g-T; CAGL0F02717g-T-p1; CAGL0F02717g.
DR GeneID; 2887804; -.
DR KEGG; cgr:CAGL0F02717g; -.
DR CGD; CAL0129834; PDH1.
DR VEuPathDB; FungiDB:CAGL0F02717g; -.
DR eggNOG; KOG0065; Eukaryota.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; O74208; -.
DR OMA; WHDVCYE; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0005886; C:plasma membrane; IGI:CGD.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:CGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:EnsemblFungi.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR005285; Drug-R_PDR/CDR.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
DR NCBIfam; TIGR00956; 3a01205; 1.
DR PANTHER; PTHR19241; ATP-BINDING CASSETTE TRANSPORTER; 1.
DR PANTHER; PTHR19241:SF625; ATP-DEPENDENT PERMEASE PDR10-RELATED; 1.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF14510; ABC_trans_N; 1.
DR Pfam; PF06422; PDR_CDR; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1542
FT /note="Pleiotropic ABC efflux transporter of multiple drugs
FT PDH1"
FT /id="PRO_0000093439"
FT TOPO_DOM 1..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..652
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 662..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..1220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1221..1241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1256..1276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1296..1316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1342..1362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1370..1390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1495..1515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1516..1542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 153..409
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 885..1128
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 921..928
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 438
FT /note="K -> Q (in Ref. 1; AAC31800)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="E -> D (in Ref. 1; AAC31800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1542 AA; 175026 MW; 2EE22149FD09F669 CRC64;
MNTPDDSSVS SVDSHQPYMG FDDNVEKRIR ELARSLTQQS LTSSNRSVNK EAPADGSAPL
DRVSTRASSI FSADFKGVNP VFSDEEEDDY DARLDPNSDE FSSKAWVQNM AKITTGDPEF
YKPYSIGCCW KDLSASGESA DVSYQSTFLN LPVKLLNAVW RKARPARESD TFRILKPMDG
LLKPGELLVV LGRPGSGCTT LLKSISSTTH GFQISKDSVI SYNGLTPNEI KKHYRGEVVY
NAEADIHLPH LTVYQTLVTV ARLKTPQNRV KGVTREDFAN HVTDVAMATY GLSHTRDTKV
GNDLVRGVSG GERKRVSIAE VWICGSKFQC WDNATRGLDS ATALEFVRAL KTQAHIAKNV
ATVAIYQCSQ DAYNLFNKVS VLYEGYQIYF GDAQHAKVYF QKMGYFCPKR QTIPDFLTSI
TSPAERRINK EYLDKGIKVP QTPLDMVEYW HNSEEYKQLR EEIDETLAHQ SEDDKEEIKE
AHIAKQSKRA RPSSPYVVSY MMQVKYILIR NFWRIKNSAS VTLFQVFGNS AMAFILGSMF
YKIQKGSSAD TFYFRGAAMF FAILFNAFSS LLEIFSLYEA RPITEKHRTY SLYHPSADAF
ASVISEIPPK IVTAILFNII FYFLVNFRRD AGRFFFYFLI NVIAVFAMSH LFRCVGSLTK
TLQEAMVPAS MLLLALSMYT GFAIPRTKML GWSKWIWYIN PLAYLFESLM VNEFHDRRFP
CNTYIPRGGA YNDVTGTERV CASVGARPGN DYVLGDDFLK ESYDYENKHK WRGFGVGMAY
VIFFFFVYLI LCEFNEGAKQ KGEMLVFPHS VVKRMKKEGK IRDKTKMHTD KNDIENNSES
ITSNATNEKN MLQDTYDENA DSESITSGSR GGSPQVGLSK SEAIFHWQNL CYDVPIKTEV
RRILNNVDGW VKPGTLTALM GASGAGKTTL LDCLAERTTM GVITGDVMVN GRPRDTSFSR
SIGYCQQQDL HLKTATVRES LRFSAYLRQP SSVSIEEKNE YVEAVIKILE METYADAVVG
VPGEGLNVEQ RKRLTIGVEL AAKPKLLVFL DEPTSGLDSQ TAWATCQLMK KLANHGQAIL
CTIHQPSAML MQEFDRLLFL QKGGQTVYFG DLGKGCKTMI KYFEDHGAHK CPPDANPAEW
MLEVVGAAPG SHANQDYHEV WRNSEQFKQV KQELEQMEKE LSQKELDNDE DANKEFATSL
WYQFQLVCVR LFQQYWRTPD YLWSKYILTI FNQLFIGFTF FKADHTLQGL QNQMLSIFMY
TVIFNPLLQQ YLPTFVQQRD LYEARERPSR TFSWKAFILA QIVVEVPWNI VAGTLAYCIY
YYSVGFYANA SQAHQLHERG ALFWLFSIAF YVYVGSLGLF VISFNEVAET AAHIGSLMFT
MALSFCGVMA TPDAMPRFWI FMYRVSPLTY LIDALLSTGV ANVDIRCSNT ELVTFTPPQG
LTCGQYMTPY LNVAGTGYLT DPSATDECHF CQFSYTNDFL ATVSSKYYRR WRNYGIFICF
IVFDYVAGIF LYWLARVPKT NGKIAKNGKT AKVNFIRRLI PF
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