PDR12_YEAST
ID PDR12_YEAST Reviewed; 1511 AA.
AC Q02785; D6W3V6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=ATP-dependent permease PDR12;
GN Name=PDR12; OrderedLocusNames=YPL058C; ORFNames=LPE14C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9687494; DOI=10.1093/emboj/17.15.4257;
RA Piper P.W., Mahe Y., Thompson S., Pandjaitan R., Holyoak C.D., Egner R.,
RA Muehlbauer M., Coote P.J., Kuchler K.;
RT "The pdr12 ABC transporter is required for the development of weak organic
RT acid resistance in yeast.";
RL EMBO J. 17:4257-4265(1998).
RN [4]
RP FUNCTION.
RX PubMed=10419965; DOI=10.1128/jb.181.15.4644-4652.1999;
RA Holyoak C.D., Bracey D., Piper P.W., Kuchler K., Coote P.J.;
RT "The Saccharomyces cerevisiae weak-acid-inducible ABC transporter Pdr12
RT transports fluorescein and preservative anions from the cytosol by an
RT energy-dependent mechanism.";
RL J. Bacteriol. 181:4644-4652(1999).
RN [5]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=10931353; DOI=10.1046/j.1365-2958.2000.02017.x;
RA Holyoak C.D., Thompson S., Ortiz Calderon C., Hatzixanthis K., Bauer B.E.,
RA Kuchler K., Piper P.W., Coote P.J.;
RT "Loss of Cmk1 Ca(2+)-calmodulin-dependent protein kinase in yeast results
RT in constitutive weak organic acid resistance, associated with a post-
RT transcriptional activation of the Pdr12 ATP-binding cassette transporter.";
RL Mol. Microbiol. 37:595-605(2000).
RN [6]
RP FUNCTION.
RX PubMed=12869194; DOI=10.1046/j.1432-1033.2003.03701.x;
RA Bauer B.E., Rossington D., Mollapour M., Mamnun Y.M., Kuchler K.,
RA Piper P.W.;
RT "Weak organic acid stress inhibits aromatic amino acid uptake by yeast,
RT causing a strong influence of amino acid auxotrophies on the phenotypes of
RT membrane transporter mutants.";
RL Eur. J. Biochem. 270:3189-3195(2003).
RN [7]
RP INDUCTION.
RX PubMed=12588995; DOI=10.1128/mcb.23.5.1775-1785.2003;
RA Kren A., Mamnun Y.M., Bauer B.E., Schueller C., Wolfger H.,
RA Hatzixanthis K., Mollapour M., Gregori C., Piper P.W., Kuchler K.;
RT "War1p, a novel transcription factor controlling weak acid stress response
RT in yeast.";
RL Mol. Cell. Biol. 23:1775-1785(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP INDUCTION.
RX PubMed=14617816; DOI=10.1091/mbc.e03-05-0322;
RA Schueller C., Mamnun Y.M., Mollapour M., Krapf G., Schuster M., Bauer B.E.,
RA Piper P.W., Kuchler K.;
RT "Global phenotypic analysis and transcriptional profiling defines the weak
RT acid stress response regulon in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 15:706-720(2004).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-426, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [12]
RP INDUCTION.
RX PubMed=12734796; DOI=10.1002/yea.981;
RA Hatzixanthis K., Mollapour M., Seymour I., Bauer B.E., Krapf G.,
RA Schueller C., Kuchler K., Piper P.W.;
RT "Moderately lipophilic carboxylate compounds are the selective inducers of
RT the Saccharomyces cerevisiae Pdr12p ATP-binding cassette transporter.";
RL Yeast 20:575-585(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [14]
RP FUNCTION.
RX PubMed=16911515; DOI=10.1111/j.1567-1364.2006.00094.x;
RA Hazelwood L.A., Tai S.L., Boer V.M., de Winde J.H., Pronk J.T.,
RA Daran J.-M.;
RT "A new physiological role for Pdr12p in Saccharomyces cerevisiae: export of
RT aromatic and branched-chain organic acids produced in amino acid
RT catabolism.";
RL FEMS Yeast Res. 6:937-945(2006).
RN [15]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [16]
RP INDUCTION.
RX PubMed=17509074; DOI=10.1111/j.1742-4658.2007.05837.x;
RA Gregori C., Bauer B.E., Schwartz C., Kren A., Schueller C., Kuchler K.;
RT "A genetic screen identifies mutations in the yeast WAR1 gene, linking
RT transcription factor phosphorylation to weak-acid stress adaptation.";
RL FEBS J. 274:3094-3107(2007).
RN [17]
RP FUNCTION, AND INDUCTION.
RX PubMed=17141908; DOI=10.1016/j.ijfoodmicro.2006.06.035;
RA Papadimitriou M.N.B., Resende C., Kuchler K., Brul S.;
RT "High Pdr12 levels in spoilage yeast (Saccharomyces cerevisiae) correlate
RT directly with sorbic acid levels in the culture medium but are not
RT sufficient to provide cells with acquired resistance to the food
RT preservative.";
RL Int. J. Food Microbiol. 113:173-179(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [19]
RP FUNCTION.
RX PubMed=18800175;
RA Lushchak V., Abrat O., Miedzobrodzki J., Semchyshyn H.;
RT "Pdr12p-dependent and -independent fluorescein extrusion from baker's yeast
RT cells.";
RL Acta Biochim. Pol. 55:595-601(2008).
RN [20]
RP INDUCTION.
RX PubMed=18621731; DOI=10.1074/jbc.m803095200;
RA Gregori C., Schueller C., Frohner I.E., Ammerer G., Kuchler K.;
RT "Weak organic acids trigger conformational changes of the yeast
RT transcription factor War1 in vivo to elicit stress adaptation.";
RL J. Biol. Chem. 283:25752-25764(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-52 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-56, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plasma membrane transporter which mediates resistance to
CC water-soluble, monocarboxylic acids with chain lengths of from C1 to C7
CC by active extrusion of the preservative anions from the cytosol. Also
CC involved in the export of aromatic and branched-chain organic acids
CC produced in amino acid catabolism. {ECO:0000269|PubMed:10419965,
CC ECO:0000269|PubMed:10931353, ECO:0000269|PubMed:12869194,
CC ECO:0000269|PubMed:16911515, ECO:0000269|PubMed:17141908,
CC ECO:0000269|PubMed:18800175, ECO:0000269|PubMed:9687494}.
CC -!- INTERACTION:
CC Q02785; P33302: PDR5; NbExp=3; IntAct=EBI-13065, EBI-13038;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9687494}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9687494}.
CC -!- INDUCTION: By weak acids like sorbate through the WAR1 transcription
CC activator. {ECO:0000269|PubMed:12588995, ECO:0000269|PubMed:12734796,
CC ECO:0000269|PubMed:14617816, ECO:0000269|PubMed:17141908,
CC ECO:0000269|PubMed:17509074, ECO:0000269|PubMed:18621731,
CC ECO:0000269|PubMed:9687494}.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; U39205; AAB68307.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11372.1; -; Genomic_DNA.
DR PIR; S60932; S60932.
DR RefSeq; NP_015267.1; NM_001183872.1.
DR AlphaFoldDB; Q02785; -.
DR SMR; Q02785; -.
DR BioGRID; 36122; 121.
DR IntAct; Q02785; 76.
DR MINT; Q02785; -.
DR STRING; 4932.YPL058C; -.
DR TCDB; 3.A.1.205.3; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q02785; -.
DR MaxQB; Q02785; -.
DR PaxDb; Q02785; -.
DR PRIDE; Q02785; -.
DR EnsemblFungi; YPL058C_mRNA; YPL058C; YPL058C.
DR GeneID; 856049; -.
DR KEGG; sce:YPL058C; -.
DR SGD; S000005979; PDR12.
DR VEuPathDB; FungiDB:YPL058C; -.
DR eggNOG; KOG0065; Eukaryota.
DR GeneTree; ENSGT00940000176297; -.
DR HOGENOM; CLU_000604_35_0_1; -.
DR InParanoid; Q02785; -.
DR OMA; GEMHHWI; -.
DR BioCyc; YEAST:G3O-33969-MON; -.
DR PRO; PR:Q02785; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02785; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005342; F:organic acid transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015849; P:organic acid transport; IDA:SGD.
DR CDD; cd03233; ABCG_PDR_domain1; 1.
DR CDD; cd03232; ABCG_PDR_domain2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR029481; ABC_trans_N.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR034001; ABCG_PDR_1.
DR InterPro; IPR034003; ABCG_PDR_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010929; PDR_CDR_ABC.
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; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Glycoprotein; Isopeptide bond;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1511
FT /note="ATP-dependent permease PDR12"
FT /id="PRO_0000093445"
FT TOPO_DOM 2..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..548
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..597
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619..622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 658..678
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 679..765
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 766..786
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 787..1182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1204
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1205..1225
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1226..1254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1255..1275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1276..1291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1292..1312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1313..1318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1319..1339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1340..1444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1445..1465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1466..1511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 144..397
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 836..1084
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 878..885
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 972..979
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 1405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CROSSLNK 426
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
SQ SEQUENCE 1511 AA; 171065 MW; 4962762AAE1997FC CRC64;
MSSTDEHIEK DISSRSNHDD DYANSVQSYA ASEGQVDNED LAATSQLSRH LSNILSNEEG
IERLESMARV ISHKTKKEMD SFEINDLDFD LRSLLHYLRS RQLEQGIEPG DSGIAFKNLT
AVGVDASAAY GPSVEEMFRN IASIPAHLIS KFTKKSDVPL RNIIQNCTGV VESGEMLFVV
GRPGAGCSTF LKCLSGETSE LVDVQGEFSY DGLDQSEMMS KYKGYVIYCP ELDFHFPKIT
VKETIDFALK CKTPRVRIDK MTRKQYVDNI RDMWCTVFGL RHTYATKVGN DFVRGVSGGE
RKRVSLVEAQ AMNASIYSWD NATRGLDAST ALEFAQAIRT ATNMVNNSAI VAIYQAGENI
YELFDKTTVL YNGRQIYFGP ADKAVGYFQR MGWVKPNRMT SAEFLTSVTV DFENRTLDIK
PGYEDKVPKS SSEFEEYWLN SEDYQELLRT YDDYQSRHPV NETRDRLDVA KKQRLQQGQR
ENSQYVVNYW TQVYYCMIRG FQRVKGDSTY TKVYLSSFLI KALIIGSMFH KIDDKSQSTT
AGAYSRGGML FYVLLFASVT SLAEIGNSFS SRPVIVKHKS YSMYHLSAES LQEIITEFPT
KFVAIVILCL ITYWIPFMKY EAGAFFQYIL YLLTVQQCTS FIFKFVATMS KSGVDAHAVG
GLWVLMLCVY AGFVLPIGEM HHWIRWLHFI NPLTYAFESL VSTEFHHREM LCSALVPSGP
GYEGISIANQ VCDAAGAVKG NLYVSGDSYI LHQYHFAYKH AWRNWGVNIV WTFGYIVFNV
ILSEYLKPVE GGGDLLLYKR GHMPELGTEN ADARTASREE MMEALNGPNV DLEKVIAEKD
VFTWNHLDYT IPYDGATRKL LSDVFGYVKP GKMTALMGES GAGKTTLLNV LAQRINMGVI
TGDMLVNAKP LPASFNRSCG YVAQADNHMA ELSVRESLRF AAELRQQSSV PLEEKYEYVE
KIITLLGMQN YAEALVGKTG RGLNVEQRKK LSIGVELVAK PSLLLFLDEP TSGLDSQSAW
SIVQFMRALA DSGQSILCTI HQPSATLFEQ FDRLLLLKKG GKMVYFGDIG PNSETLLKYF
ERQSGMKCGV SENPAEYILN CIGAGATASV NSDWHDLWLA SPECAAARAE VEELHRTLPG
RAVNDDPELA TRFAASYMTQ IKCVLRRTAL QFWRSPVYIR AKFFECVACA LFVGLSYVGV
NHSVGGAIEA FSSIFMLLLI ALAMINQLHV FAYDSRELYE VREAASNTFH WSVLLLCHAA
VENFWSTLCQ FMCFICYYWP AQFSGRASHA GFFFFFYVLI FPLYFVTYGL WILYMSPDVP
SASMINSNLF AAMLLFCGIL QPREKMPAFW RRLMYNVSPF TYVVQALVTP LVHNKKVVCN
PHEYNIMDPP SGKTCGEFLS TYMDNNTGYL VNPTATENCQ YCPYTVQDQV VAKYNVKWDH
RWRNFGFMWA YICFNIAAML ICYYVVRVKV WSLKSVLNFK KWFNGPRKER HEKDTNIFQT
VPGDENKITK K
