NDT80_YEAST
ID NDT80_YEAST Reviewed; 627 AA.
AC P38830; D3DL74; Q66R83;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 4.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Meiosis-specific transcription factor NDT80;
GN Name=NDT80; Synonyms=DAS1; OrderedLocusNames=YHR124W;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=S288c / GRF88;
RX PubMed=8524222; DOI=10.1128/mcb.15.12.6572;
RA Xu L., Ajimura M., Padmore R., Klein C., Kleckner N.;
RT "NDT80, a meiosis-specific gene required for exit from pachytene in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 15:6572-6581(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=9660952; DOI=10.1016/s1097-2765(00)80068-4;
RA Chu S., Herskowitz I.;
RT "Gametogenesis in yeast is regulated by a transcriptional cascade dependent
RT on Ndt80.";
RL Mol. Cell 1:685-696(1998).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=9742092; DOI=10.1128/mcb.18.10.5750;
RA Hepworth S.R., Friesen H., Segall J.;
RT "NDT80 and the meiotic recombination checkpoint regulate expression of
RT middle sporulation-specific genes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 18:5750-5761(1998).
RN [7]
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=11035815; DOI=10.1073/pnas.220464597;
RA Tung K.-S., Hong E.-J.E., Roeder G.S.;
RT "The pachytene checkpoint prevents accumulation and phosphorylation of the
RT meiosis-specific transcription factor Ndt80.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12187-12192(2000).
RN [8]
RP INDUCTION.
RX PubMed=12192041; DOI=10.1128/mcb.22.18.6417-6429.2002;
RA Pak J., Segall J.;
RT "Regulation of the premiddle and middle phases of expression of the NDT80
RT gene during sporulation of Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 22:6417-6429(2002).
RN [9]
RP PHOSPHORYLATION BY IME2.
RX PubMed=12242283; DOI=10.1128/mcb.22.20.7024-7040.2002;
RA Sopko R., Raithatha S., Stuart D.T.;
RT "Phosphorylation and maximal activity of Saccharomyces cerevisiae meiosis-
RT specific transcription factor Ndt80 is dependent on Ime2.";
RL Mol. Cell. Biol. 22:7024-7040(2002).
RN [10]
RP PHOSPHORYLATION BY IME2, AND INDUCTION.
RX PubMed=12783856; DOI=10.1101/gad.1101503;
RA Benjamin K.R., Zhang C., Shokat K.M., Herskowitz I.;
RT "Control of landmark events in meiosis by the CDK Cdc28 and the meiosis-
RT specific kinase Ime2.";
RL Genes Dev. 17:1524-1539(2003).
RN [11]
RP FUNCTION.
RX PubMed=12832469; DOI=10.1128/mcb.23.14.4814-4825.2003;
RA Pierce M., Benjamin K.R., Montano S.P., Georgiadis M.M., Winter E.,
RA Vershon A.K.;
RT "Sum1 and Ndt80 proteins compete for binding to middle sporulation element
RT sequences that control meiotic gene expression.";
RL Mol. Cell. Biol. 23:4814-4825(2003).
RN [12]
RP PHOSPHORYLATION, AND INDUCTION.
RX PubMed=14605875; DOI=10.1007/s00438-003-0922-3;
RA Shubassi G., Luca N., Pak J., Segall J.;
RT "Activity of phosphoforms and truncated versions of Ndt80, a checkpoint-
RT regulated sporulation-specific transcription factor of Saccharomyces
RT cerevisiae.";
RL Mol. Genet. Genomics 270:324-336(2003).
RN [13]
RP DNA-BINDING, AND MUTAGENESIS OF LYS-50; LYS-54; 57-PRO--SER-59; ARG-97;
RP ARG-111; TYR-113; 176-LYS-ARG-177; ARG-208; ARG-254 AND ARG-326.
RX PubMed=15161958; DOI=10.1093/nar/gkh625;
RA Fingerman I.M., Sutphen K., Montano S.P., Georgiadis M.M., Vershon A.K.;
RT "Characterization of critical interactions between Ndt80 and MSE DNA
RT defining a novel family of Ig-fold transcription factors.";
RL Nucleic Acids Res. 32:2947-2956(2004).
RN [14]
RP PHOSPHORYLATION BY IME2, AND DNA-BINDING.
RX PubMed=14680970; DOI=10.1016/j.pep.2003.08.025;
RA Sopko R., Stuart D.T.;
RT "Purification and characterization of the DNA binding domain of
RT Saccharomyces cerevisiae meiosis-specific transcription factor Ndt80.";
RL Protein Expr. Purif. 33:134-144(2004).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-340 IN COMPLEX WITH DNA.
RX PubMed=12411490; DOI=10.1093/emboj/cdf572;
RA Lamoureux J.S., Stuart D.T., Tsang R., Wu C., Glover J.N.M.;
RT "Structure of the sporulation-specific transcription factor Ndt80 bound to
RT DNA.";
RL EMBO J. 21:5721-5732(2002).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 59-330, MUTAGENESIS OF LYS-110;
RP ARG-111; TYR-113; HIS-173; LYS-176; ARG-177; ARG-202; ARG-208; ARG-254 AND
RP ARG-326, AND SUBUNIT.
RX PubMed=12384578; DOI=10.1073/pnas.222312199;
RA Montano S.P., Cote M.L., Fingerman I.M., Pierce M., Vershon A.K.,
RA Georgiadis M.M.;
RT "Crystal structure of the DNA-binding domain from Ndt80, a transcriptional
RT activator required for meiosis in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14041-14046(2002).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-340 IN COMPLEXES WITH TARGET
RP DNA.
RX PubMed=16531239; DOI=10.1016/j.str.2005.11.017;
RA Lamoureux J.S., Glover J.N.M.;
RT "Principles of protein-DNA recognition revealed in the structural analysis
RT of Ndt80-MSE DNA complexes.";
RL Structure 14:555-565(2006).
CC -!- FUNCTION: Transcription factor required for successful completion of
CC meiosis and spore formation. Gets activated after completion of meiotic
CC recombination at the end of prophase I. Recognizes and binds to the
CC middle sporulation element (MSE) 5'-C[AG]CAAA[AT]-3' in the promoter
CC region of stage-specific genes that are required for progression
CC through meiosis and sporulation. Competes for binding to MSE with the
CC transcriptional repressor SUM1, which represses middle sporulation-
CC specific genes during mitosis and early sporulation.
CC {ECO:0000269|PubMed:12832469, ECO:0000269|PubMed:8524222,
CC ECO:0000269|PubMed:9660952, ECO:0000269|PubMed:9742092}.
CC -!- SUBUNIT: Binds to DNA as a monomer. {ECO:0000269|PubMed:12384578,
CC ECO:0000269|PubMed:12411490}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11035815}.
CC -!- INDUCTION: Induced during prophase I of meiosis. Requires protein
CC kinase IME2 for initial expression and continued transcription during
CC meiotic divisions. Can autoactivate its own synthesis.
CC {ECO:0000269|PubMed:12192041, ECO:0000269|PubMed:12783856,
CC ECO:0000269|PubMed:14605875, ECO:0000269|PubMed:9742092}.
CC -!- PTM: Phosphorylated by pachytene checkpoint kinase IME2, but also
CC phosphorylated in an IME2-independent manner. Phosphorylation probably
CC eliminates SUM1-mediated repression and is also required for full
CC transcriptional activation activity. Phosphorylation of the DNA-binding
CC domain by IME2 does not alter DNA binding affinity.
CC {ECO:0000269|PubMed:11035815, ECO:0000269|PubMed:12242283,
CC ECO:0000269|PubMed:12783856, ECO:0000269|PubMed:14605875,
CC ECO:0000269|PubMed:14680970}.
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DR EMBL; U35122; AAA92299.1; -; Genomic_DNA.
DR EMBL; U10398; AAB68408.1; -; Genomic_DNA.
DR EMBL; AY723825; AAU09742.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06818.1; -; Genomic_DNA.
DR PIR; S48968; S48968.
DR RefSeq; NP_011992.1; NM_001179254.1.
DR PDB; 1M6U; X-ray; 2.30 A; A/B=59-330.
DR PDB; 1M7U; X-ray; 2.80 A; A/B=59-330.
DR PDB; 1MN4; X-ray; 2.20 A; A=59-340.
DR PDB; 1MNN; X-ray; 1.40 A; A=1-340.
DR PDB; 2ETW; X-ray; 1.67 A; A=1-340.
DR PDB; 2EUV; X-ray; 1.94 A; A=1-340.
DR PDB; 2EUW; X-ray; 1.68 A; A=1-340.
DR PDB; 2EUX; X-ray; 1.57 A; A=1-340.
DR PDB; 2EUZ; X-ray; 1.56 A; A=1-340.
DR PDB; 2EVF; X-ray; 1.56 A; A=1-340.
DR PDB; 2EVG; X-ray; 1.55 A; A=1-340.
DR PDB; 2EVH; X-ray; 1.99 A; A=1-340.
DR PDB; 2EVI; X-ray; 1.80 A; A=1-340.
DR PDB; 2EVJ; X-ray; 1.89 A; A=1-340.
DR PDBsum; 1M6U; -.
DR PDBsum; 1M7U; -.
DR PDBsum; 1MN4; -.
DR PDBsum; 1MNN; -.
DR PDBsum; 2ETW; -.
DR PDBsum; 2EUV; -.
DR PDBsum; 2EUW; -.
DR PDBsum; 2EUX; -.
DR PDBsum; 2EUZ; -.
DR PDBsum; 2EVF; -.
DR PDBsum; 2EVG; -.
DR PDBsum; 2EVH; -.
DR PDBsum; 2EVI; -.
DR PDBsum; 2EVJ; -.
DR AlphaFoldDB; P38830; -.
DR SMR; P38830; -.
DR BioGRID; 36557; 116.
DR IntAct; P38830; 3.
DR MINT; P38830; -.
DR STRING; 4932.YHR124W; -.
DR PaxDb; P38830; -.
DR PRIDE; P38830; -.
DR EnsemblFungi; YHR124W_mRNA; YHR124W; YHR124W.
DR GeneID; 856524; -.
DR KEGG; sce:YHR124W; -.
DR SGD; S000001166; NDT80.
DR VEuPathDB; FungiDB:YHR124W; -.
DR eggNOG; ENOG502R1FS; Eukaryota.
DR HOGENOM; CLU_015202_0_0_1; -.
DR InParanoid; P38830; -.
DR BioCyc; YEAST:G3O-31165-MON; -.
DR EvolutionaryTrace; P38830; -.
DR PRO; PR:P38830; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38830; protein.
DR GO; GO:0000228; C:nuclear chromosome; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR Gene3D; 2.60.40.1390; -; 1.
DR InterPro; IPR024061; NDT80_DNA-bd_dom.
DR InterPro; IPR037141; NDT80_DNA-bd_dom_sf.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR Pfam; PF05224; NDT80_PhoG; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS51517; NDT80; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; DNA-binding; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..627
FT /note="Meiosis-specific transcription factor NDT80"
FT /id="PRO_0000096772"
FT DNA_BIND 28..335
FT /note="NDT80"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00850"
FT REGION 324..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 58
FT /note="Interaction with DNA"
FT SITE 111
FT /note="Interaction with DNA"
FT SITE 177
FT /note="Interaction with DNA"
FT SITE 208
FT /note="Interaction with DNA"
FT SITE 254
FT /note="Interaction with DNA"
FT SITE 326
FT /note="Interaction with DNA"
FT MUTAGEN 50
FT /note="K->A: Reduces DNA-binding by 70%."
FT /evidence="ECO:0000269|PubMed:15161958"
FT MUTAGEN 54
FT /note="K->A: Reduces DNA-binding by 50%."
FT /evidence="ECO:0000269|PubMed:15161958"
FT MUTAGEN 57
FT /note="P->A: Reduces DNA-binding by 65%."
FT MUTAGEN 58
FT /note="R->A: Reduces DNA-binding by 65%."
FT MUTAGEN 59
FT /note="S->A: Reduces DNA-binding by 86%."
FT MUTAGEN 97
FT /note="R->A: Reduces DNA-binding by 67%."
FT /evidence="ECO:0000269|PubMed:15161958"
FT MUTAGEN 110
FT /note="K->A: No effect on DNA-binding but strongly reduces
FT progress through meiosis and sporulation."
FT /evidence="ECO:0000269|PubMed:12384578"
FT MUTAGEN 111
FT /note="R->A: Reduces DNA-binding by 95% and abolishes
FT sporulation."
FT /evidence="ECO:0000269|PubMed:12384578,
FT ECO:0000269|PubMed:15161958"
FT MUTAGEN 113
FT /note="Y->A: Reduces DNA-binding by 80% and abolishes
FT sporulation."
FT /evidence="ECO:0000269|PubMed:12384578,
FT ECO:0000269|PubMed:15161958"
FT MUTAGEN 173
FT /note="H->A: Reduces DNA-binding by 80% and strongly
FT reduces progress through meiosis and sporulation."
FT /evidence="ECO:0000269|PubMed:12384578"
FT MUTAGEN 176
FT /note="K->A: Reduces DNA-binding by 50% but does not
FT abolish sporulation."
FT /evidence="ECO:0000269|PubMed:12384578"
FT MUTAGEN 177
FT /note="R->A: Reduces DNA-binding by 96% and abolishes
FT sporulation."
FT /evidence="ECO:0000269|PubMed:12384578"
FT MUTAGEN 202
FT /note="R->A: No effect on DNA-binding but strongly reduces
FT progress through meiosis and sporulation."
FT /evidence="ECO:0000269|PubMed:12384578"
FT MUTAGEN 208
FT /note="R->A: Reduces DNA-binding by 50% and abolishes
FT sporulation."
FT /evidence="ECO:0000269|PubMed:12384578,
FT ECO:0000269|PubMed:15161958"
FT MUTAGEN 254
FT /note="R->A: Reduces DNA-binding by 93% and abolishes
FT sporulation."
FT /evidence="ECO:0000269|PubMed:12384578,
FT ECO:0000269|PubMed:15161958"
FT MUTAGEN 326
FT /note="R->A: Reduces DNA-binding by 50% and abolishes
FT sporulation."
FT /evidence="ECO:0000269|PubMed:12384578,
FT ECO:0000269|PubMed:15161958"
FT CONFLICT 200
FT /note="I -> T (in Ref. 15)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="M -> T (in Ref. 16)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="D -> N (in Ref. 16)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="S -> F (in Ref. 16)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="L -> S (in Ref. 4; AAU09742)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="F -> L (in Ref. 1; AAA92299)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="P -> N (in Ref. 1; AAA92299)"
FT /evidence="ECO:0000305"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:1MNN"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1MNN"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 127..132
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1MNN"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1MN4"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2EVG"
FT STRAND 152..161
FT /evidence="ECO:0007829|PDB:1MNN"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1M7U"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:1MNN"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 241..257
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 273..283
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:1M6U"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1M6U"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 303..317
FT /evidence="ECO:0007829|PDB:1MNN"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1MNN"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1MNN"
SQ SEQUENCE 627 AA; 71479 MW; 947DA0BA08065595 CRC64;
MNEMENTDPV LQDDLVSKYE RELSTEQEED TPVILTQLNE DGTTSNYFDK RKLKIAPRST
LQFKVGPPFE LVRDYCPVVE SHTGRTLDLR IIPRIDRGFD HIDEEWVGYK RNYFTLVSTF
ETANCDLDTF LKSSFDLLVE DSSVESRLRV QYFAIKIKAK NDDDDTEINL VQHTAKRDKG
PQFCPSVCPL VPSPLPKHQI IREASNVRNI TKMKKYDSTF YLHRDHVNYE EYGVDSLLFS
YPEDSIQKVA RYERVQFASS ISVKKPSQQN KHFSLHVILG AVVDPDTFHG ENPGIPYDEL
ALKNGSKGMF VYLQEMKTPP LIIRGRSPSN YASSQRITVR TPSSVNSSQN STKRKMPSMA
QPLNESCLNA RPSKRRSKVA LGAPNSGASI SPIKSRQSTP MEASKENEDP FFRPNKRVET
LEHIQNKLGA LKNQCPDSSL KYPSSSSRGM EGCLEKEDLV YSSSFSVNMK QIELKPARSF
EHENIFKVGS LAFKKINELP HENYDITIEK KSMEQNYLRP EIGSRSECKT SYGNELSLSN
ISFSILPNSA ENFHLETALF PATEEDVPRT FSRILETGSF QNYYQKMDAE NADRVYSKGV
KLIASGTLPS GIFNREELFE EDSFYKY
