FLO1_YEAST
ID FLO1_YEAST Reviewed; 1537 AA.
AC P32768; A7U4Y7; D6VPN7; Q58HH7; Q58HH8; Q58HH9; Q58HI0;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Flocculation protein FLO1;
DE Short=Flocculin-1;
DE Flags: Precursor;
GN Name=FLO1; Synonyms=FLO2, FLO4, FLO8; OrderedLocusNames=YAR050W;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8511970; DOI=10.1002/yea.320090413;
RA Teunissen A.W.R.H., Holub E., van der Hucht J., van den Berg J.A.,
RA Steensma H.Y.;
RT "Sequence of the open reading frame of the FLO1 gene from Saccharomyces
RT cerevisiae.";
RL Yeast 9:423-427(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND REPEATS.
RC STRAIN=STX347-1D;
RX PubMed=7483845; DOI=10.1002/yea.320110903;
RA Bidard F., Bony M., Blondin B., Dequin S., Barre P.;
RT "The Saccharomyces cerevisiae FLO1 flocculation gene encodes for a cell
RT surface protein.";
RL Yeast 11:809-822(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8203162; DOI=10.1002/yea.320100208;
RA Watari J., Takata Y., Ogawa M., Sahara H., Koshino S., Onnela M.-L.,
RA Airaksinen U., Jaatinen R., Penttilae M., Keraenen S.;
RT "Molecular cloning and analysis of the yeast flocculation gene FLO1.";
RL Yeast 10:211-225(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REPEATS.
RC STRAIN=S288c / KV1, S288c / KV291, S288c / KV295, and S288c / KV333;
RX PubMed=16086015; DOI=10.1038/ng1618;
RA Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
RT "Intragenic tandem repeats generate functional variability.";
RL Nat. Genet. 37:986-990(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Sigma 1278B;
RX PubMed=18001350; DOI=10.1111/j.1365-2958.2007.06014.x;
RA Fichtner L., Schulze F., Braus G.H.;
RT "Differential Flo8p-dependent regulation of FLO1 and FLO11 for cell-cell
RT and cell-substrate adherence of S.cerevisiae S288c.";
RL Mol. Microbiol. 66:1276-1289(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [7]
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 [8]
RP GENE MAPPING.
RX PubMed=7668043; DOI=10.1002/yea.320110805;
RA Teunissen A.W.R.H., van den Berg J.A., Steensma H.Y.;
RT "Localization of the dominant flocculation genes FLO5 and FLO8 of
RT Saccharomyces cerevisiae.";
RL Yeast 11:735-745(1995).
RN [9]
RP REVIEW.
RX PubMed=7502576; DOI=10.1002/yea.320111102;
RA Teunissen A.W.R.H., Steensma H.Y.;
RT "Review: the dominant flocculation genes of Saccharomyces cerevisiae
RT constitute a new subtelomeric gene family.";
RL Yeast 11:1001-1013(1995).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=8980634; DOI=10.1016/s0304-4165(96)00067-0;
RA van der Vaart J.M., van Schagen F.S., Mooren A.T.A., Chapman J.W.,
RA Klis F.M., Verrips C.T.;
RT "The retention mechanism of cell wall proteins in Saccharomyces cerevisiae.
RT Wall-bound Cwp2p is beta-1,6-glucosylated.";
RL Biochim. Biophys. Acta 1291:206-214(1996).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=9244284; DOI=10.1128/jb.179.15.4929-4936.1997;
RA Bony M., Thines-Sempoux D., Barre P., Blondin B.;
RT "Localization and cell surface anchoring of the Saccharomyces cerevisiae
RT flocculation protein Flo1p.";
RL J. Bacteriol. 179:4929-4936(1997).
RN [12]
RP FUNCTION.
RX PubMed=9851992; DOI=10.1128/jb.180.24.6503-6510.1998;
RA Kobayashi O., Hayashi N., Kuroki R., Sone H.;
RT "Region of FLO1 proteins responsible for sugar recognition.";
RL J. Bacteriol. 180:6503-6510(1998).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9483793;
RX DOI=10.1002/(sici)1097-0061(19980115)14:1<25::aid-yea197>3.0.co;2-c;
RA Bony M., Barre P., Blondin B.;
RT "Distribution of the flocculation protein, flop, at the cell surface during
RT yeast growth: the availability of flop determines the flocculation level.";
RL Yeast 14:25-35(1998).
RN [14]
RP FUNCTION.
RX PubMed=11027318; DOI=10.1073/pnas.220420397;
RA Guo B., Styles C.A., Feng Q., Fink G.R.;
RT "A Saccharomyces gene family involved in invasive growth, cell-cell
RT adhesion, and mating.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12158-12163(2000).
RN [15]
RP BIOTECHNOLOGY.
RX DOI=10.1094/ASBCJ-59-0069;
RA Verstrepen K.J., Michiels C., Derdelinckx G., Delvaux F.R., Winderickx J.,
RA Thevelein J.M., Bauer F.F., Pretorius I.S.;
RT "Late fermentation expression of FLO1 in Saccharomyces cerevisiae.";
RL J. Am. Soc. Brew. Chem. 59:69-76(2001).
RN [16]
RP BIOTECHNOLOGY.
RX PubMed=12698276; DOI=10.1007/s00253-002-1200-8;
RA Verstrepen K.J., Derdelinckx G., Verachtert H., Delvaux F.R.;
RT "Yeast flocculation: what brewers should know.";
RL Appl. Microbiol. Biotechnol. 61:197-205(2003).
RN [17]
RP SUBCELLULAR LOCATION, AND REPEATS.
RX PubMed=15470092; DOI=10.1099/mic.0.27420-0;
RA Frieman M.B., Cormack B.P.;
RT "Multiple sequence signals determine the distribution of
RT glycosylphosphatidylinositol proteins between the plasma membrane and cell
RT wall in Saccharomyces cerevisiae.";
RL Microbiology 150:3105-3114(2004).
CC -!- FUNCTION: Cell wall protein that participates directly in adhesive
CC cell-cell interactions during yeast flocculation, a reversible, asexual
CC and Ca(2+)-dependent process in which cells adhere to form aggregates
CC (flocs) consisting of thousands of cells. The lectin-like protein
CC sticks out of the cell wall of flocculent cells and selectively binds
CC mannose residues in the cell walls of adjacent cells. Activity is
CC inhibited by mannose, but not by glucose, maltose, sucrose or
CC galactose. Also involved in cell-substrate adhesion.
CC {ECO:0000269|PubMed:11027318, ECO:0000269|PubMed:18001350,
CC ECO:0000269|PubMed:9483793, ECO:0000269|PubMed:9851992}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC Secreted, cell wall. Note=Identified as GPI-anchored plasma membrane
CC protein (GPI-PMP) as well as covalently-linked GPI-modified cell wall
CC protein (GPI-CWP) in the outer cell wall layer.
CC -!- DOMAIN: The number of the intragenic tandem repeats varies between
CC different S.cerevisiae strains. There is a linear correlation between
CC protein size and the extend of adhesion: the more repeats, the stronger
CC the adhesion properties and the greater the fraction of flocculating
CC cells. The Ser/Thr-rich repeats are also important for proper cell wall
CC targeting of the protein.
CC -!- PTM: Extensively N- and O-glycosylated. {ECO:0000305}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC -!- BIOTECHNOLOGY: For many industrial applications in which the yeast
CC S.cerevisiae is used, e.g. beer, wine and alcohol production,
CC appropriate flocculation behavior is one of the most important
CC characteristics of a good production strain. The ability of yeast cells
CC to flocculate is of considerable importance, as it provides an
CC effective, environment-friendly, simple and cost-free way to separate
CC yeast cells from the fermentation product at the end of fermentation.
CC {ECO:0000269|PubMed:12698276, ECO:0000269|Ref.15}.
CC -!- SIMILARITY: Belongs to the flocculin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X78160; CAA55024.1; -; Genomic_DNA.
DR EMBL; AY949845; AAX47294.1; -; Genomic_DNA.
DR EMBL; AY949846; AAX47295.1; -; Genomic_DNA.
DR EMBL; AY949847; AAX47296.1; -; Genomic_DNA.
DR EMBL; AY949848; AAX47297.1; -; Genomic_DNA.
DR EMBL; EF670005; ABS87371.1; -; Genomic_DNA.
DR EMBL; L28920; AAC09499.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006935; DAA07007.1; -; Genomic_DNA.
DR PIR; S53465; S53465.
DR RefSeq; NP_009424.1; NM_001178230.1.
DR PDB; 4LHL; X-ray; 1.43 A; A=23-271.
DR PDB; 4LHN; X-ray; 2.12 A; A=23-271.
DR PDBsum; 4LHL; -.
DR PDBsum; 4LHN; -.
DR AlphaFoldDB; P32768; -.
DR SMR; P32768; -.
DR BioGRID; 31813; 61.
DR STRING; 4932.YAR050W; -.
DR UniLectin; P32768; -.
DR PaxDb; P32768; -.
DR PRIDE; P32768; -.
DR EnsemblFungi; YAR050W_mRNA; YAR050W; YAR050W.
DR GeneID; 851289; -.
DR KEGG; sce:YAR050W; -.
DR SGD; S000000084; FLO1.
DR VEuPathDB; FungiDB:YAR050W; -.
DR eggNOG; ENOG502QPQC; Eukaryota.
DR GeneTree; ENSGT00940000176342; -.
DR HOGENOM; CLU_006076_0_0_1; -.
DR InParanoid; P32768; -.
DR OMA; PSYVTVF; -.
DR BioCyc; YEAST:G3O-28884-MON; -.
DR PRO; PR:P32768; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P32768; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005537; F:mannose binding; IMP:SGD.
DR GO; GO:0000128; P:flocculation; IMP:SGD.
DR InterPro; IPR001389; Flocculin.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR Pfam; PF00624; Flocculin; 18.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM00758; PA14; 1.
DR PROSITE; PS51820; PA14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell wall; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1514
FT /note="Flocculation protein FLO1"
FT /id="PRO_0000021273"
FT PROPEP 1515..1537
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000021274"
FT DOMAIN 74..249
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT REPEAT 278..322
FT /note="1-1"
FT REPEAT 323..367
FT /note="1-2"
FT REPEAT 368..412
FT /note="1-3"
FT REPEAT 413..457
FT /note="1-4"
FT REPEAT 458..502
FT /note="1-5"
FT REPEAT 503..547
FT /note="1-6"
FT REPEAT 548..592
FT /note="1-7"
FT REPEAT 593..637
FT /note="1-8"
FT REPEAT 638..682
FT /note="1-9"
FT REPEAT 683..727
FT /note="1-10"
FT REPEAT 728..772
FT /note="1-11"
FT REPEAT 773..817
FT /note="1-12"
FT REPEAT 818..862
FT /note="1-13"
FT REPEAT 863..907
FT /note="1-14"
FT REPEAT 908..952
FT /note="1-15"
FT REPEAT 953..997
FT /note="1-16"
FT REPEAT 998..1042
FT /note="1-17"
FT REPEAT 1043..1087
FT /note="1-18"
FT REPEAT 1118..1137
FT /note="2-1"
FT REPEAT 1138..1157
FT /note="2-2"
FT REPEAT 1226..1276
FT /note="3-1"
FT REPEAT 1291..1341
FT /note="3-2"
FT REPEAT 1342..1392
FT /note="3-3"
FT REPEAT 1408..1416
FT /note="4-1"
FT REPEAT 1417..1425
FT /note="4-2"
FT REPEAT 1426..1434
FT /note="4-3"
FT REGION 197..240
FT /note="Sugar recognition"
FT REGION 278..1087
FT /note="18 X 45 AA approximate tandem repeats, Thr-rich"
FT REGION 770..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1157
FT /note="2 X 20 AA approximate tandem repeats, Ser/Thr-rich"
FT REGION 1161..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1226..1392
FT /note="3 X 51 AA approximate repeats, Ser/Thr-rich"
FT REGION 1392..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1408..1434
FT /note="3 X 9 AA approximate tandem repeats, Thr-rich"
FT REGION 1468..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1514
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 303..797
FT /note="Missing (in strain: S288c / KV295)"
FT VARIANT 317..946
FT /note="Missing (in strain: S288c / KV333)"
FT VARIANT 317..901
FT /note="Missing (in strain: S288c / KV291)"
FT CONFLICT 330
FT /note="S -> G (in Ref. 4; AAX47297)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="R -> P (in Ref. 4; AAX47297)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="S -> G (in Ref. 4; AAX47297)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="L -> M (in Ref. 4; AAX47297)"
FT /evidence="ECO:0000305"
FT CONFLICT 416..422
FT /note="QPWNDTF -> HHGTTLL (in Ref. 4; AAX47297)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="L -> M (in Ref. 2; CAA55024 and 4; AAX47297)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="N -> K (in Ref. 4; AAX47297)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="N -> D (in Ref. 2; CAA55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 469
FT /note="S -> P (in Ref. 4; AAX47297)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="L -> M (in Ref. 2; CAA55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="I -> M (in Ref. 2; CAA55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="P -> T (in Ref. 2; CAA55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="M -> L (in Ref. 2; CAA55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="I -> M (in Ref. 2; CAA55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="I -> M (in Ref. 2; CAA55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="T -> N (in Ref. 2; CAA55024)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="H -> T (in Ref. 2; CAA55024 and 4; AAX47294/
FT AAX47295/AAX47297)"
FT /evidence="ECO:0000305"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:4LHL"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:4LHL"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:4LHL"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4LHL"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:4LHL"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:4LHL"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:4LHL"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 160..168
FT /evidence="ECO:0007829|PDB:4LHL"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 215..224
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4LHL"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:4LHL"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:4LHL"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:4LHL"
SQ SEQUENCE 1537 AA; 160668 MW; C7D4213C46ED23EF CRC64;
MTMPHRYMFL AVFTLLALTS VASGATEACL PAGQRKSGMN INFYQYSLKD SSTYSNAAYM
AYGYASKTKL GSVGGQTDIS IDYNIPCVSS SGTFPCPQED SYGNWGCKGM GACSNSQGIA
YWSTDLFGFY TTPTNVTLEM TGYFLPPQTG SYTFKFATVD DSAILSVGGA TAFNCCAQQQ
PPITSTNFTI DGIKPWGGSL PPNIEGTVYM YAGYYYPMKV VYSNAVSWGT LPISVTLPDG
TTVSDDFEGY VYSFDDDLSQ SNCTVPDPSN YAVSTTTTTT EPWTGTFTST STEMTTVTGT
NGVPTDETVI VIRTPTTAST IITTTEPWNS TFTSTSTELT TVTGTNGVRT DETIIVIRTP
TTATTAITTT EPWNSTFTST STELTTVTGT NGLPTDETII VIRTPTTATT AMTTTQPWND
TFTSTSTELT TVTGTNGLPT DETIIVIRTP TTATTAMTTT QPWNDTFTST STELTTVTGT
NGLPTDETII VIRTPTTATT AMTTTQPWND TFTSTSTEIT TVTGTNGLPT DETIIVIRTP
TTATTAMTTP QPWNDTFTST STEMTTVTGT NGLPTDETII VIRTPTTATT AITTTEPWNS
TFTSTSTEMT TVTGTNGLPT DETIIVIRTP TTATTAITTT QPWNDTFTST STEMTTVTGT
NGLPTDETII VIRTPTTATT AMTTTQPWND TFTSTSTEIT TVTGTTGLPT DETIIVIRTP
TTATTAMTTT QPWNDTFTST STEMTTVTGT NGVPTDETVI VIRTPTSEGL ISTTTEPWTG
TFTSTSTEMT TVTGTNGQPT DETVIVIRTP TSEGLVTTTT EPWTGTFTST STEMTTITGT
NGVPTDETVI VIRTPTSEGL ISTTTEPWTG TFTSTSTEMT TITGTNGQPT DETVIVIRTP
TSEGLISTTT EPWTGTFTST STEMTHVTGT NGVPTDETVI VIRTPTSEGL ISTTTEPWTG
TFTSTSTEVT TITGTNGQPT DETVIVIRTP TSEGLISTTT EPWTGTFTST STEMTTVTGT
NGQPTDETVI VIRTPTSEGL VTTTTEPWTG TFTSTSTEMS TVTGTNGLPT DETVIVVKTP
TTAISSSLSS SSSGQITSSI TSSRPIITPF YPSNGTSVIS SSVISSSVTS SLFTSSPVIS
SSVISSSTTT STSIFSESSK SSVIPTSSST SGSSESETSS AGSVSSSSFI SSESSKSPTY
SSSSLPLVTS ATTSQETASS LPPATTTKTS EQTTLVTVTS CESHVCTESI SPAIVSTATV
TVSGVTTEYT TWCPISTTET TKQTKGTTEQ TTETTKQTTV VTISSCESDV CSKTASPAIV
STSTATINGV TTEYTTWCPI STTESRQQTT LVTVTSCESG VCSETASPAI VSTATATVND
VVTVYPTWRP QTANEESVSS KMNSATGETT TNTLAAETTT NTVAAETITN TGAAETKTVV
TSSLSRSNHA ETQTASATDV IGHSSSVVSV SETGNTKSLT SSGLSTMSQQ PRSTPASSMV
GYSTASLEIS TYAGSANSLL AGSGLSVFIA SLLLAII
