ID   FLO5_YEAST              Reviewed;        1075 AA.
AC   P38894; D3DLG0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Flocculation protein FLO5;
DE            Short=Flocculin-5;
DE   Flags: Precursor;
GN   Name=FLO5; OrderedLocusNames=YHR211W;
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=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   [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   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   [4]
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   [5]
RP   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   [6]
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   [7]
RP   REPEATS.
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   [8]
RP   BIOTECHNOLOGY.
RX   PubMed=16487349; DOI=10.1111/j.1567-1364.2006.00038.x;
RA   Cunha A.F., Missawa S.K., Gomes L.H., Reis S.F., Pereira G.A.G.;
RT   "Control by sugar of Saccharomyces cerevisiae flocculation for industrial
RT   ethanol production.";
RL   FEMS Yeast Res. 6:280-287(2006).
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.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9483793}.
CC       Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
CC       Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- PTM: Extensively 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 (By
CC       similarity). {ECO:0000250}.
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|PubMed:16487349}.
CC   -!- SIMILARITY: Belongs to the flocculin family. {ECO:0000305}.
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DR   EMBL; U00029; AAB69731.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06904.1; -; Genomic_DNA.
DR   PIR; S48992; S48992.
DR   RefSeq; NP_012081.1; NM_001179342.1.
DR   PDB; 2XJP; X-ray; 0.95 A; A=23-271.
DR   PDB; 2XJQ; X-ray; 1.35 A; A=23-271.
DR   PDB; 2XJR; X-ray; 1.25 A; A=23-271.
DR   PDB; 2XJS; X-ray; 1.30 A; A=23-271.
DR   PDB; 2XJT; X-ray; 1.20 A; A=23-271.
DR   PDB; 2XJU; X-ray; 1.70 A; A=23-271.
DR   PDB; 2XJV; X-ray; 1.74 A; A=23-271.
DR   PDB; 4AHW; X-ray; 1.50 A; A=23-271.
DR   PDB; 4AHX; X-ray; 1.60 A; A=23-271.
DR   PDB; 4AHY; X-ray; 1.70 A; A=23-271.
DR   PDB; 4AHZ; X-ray; 1.90 A; A=23-271.
DR   PDB; 4AI0; X-ray; 1.80 A; A=23-271.
DR   PDB; 4AI1; X-ray; 1.80 A; A=23-271.
DR   PDB; 4AI2; X-ray; 1.79 A; A=23-271.
DR   PDB; 4AI3; X-ray; 1.90 A; A=23-271.
DR   PDBsum; 2XJP; -.
DR   PDBsum; 2XJQ; -.
DR   PDBsum; 2XJR; -.
DR   PDBsum; 2XJS; -.
DR   PDBsum; 2XJT; -.
DR   PDBsum; 2XJU; -.
DR   PDBsum; 2XJV; -.
DR   PDBsum; 4AHW; -.
DR   PDBsum; 4AHX; -.
DR   PDBsum; 4AHY; -.
DR   PDBsum; 4AHZ; -.
DR   PDBsum; 4AI0; -.
DR   PDBsum; 4AI1; -.
DR   PDBsum; 4AI2; -.
DR   PDBsum; 4AI3; -.
DR   AlphaFoldDB; P38894; -.
DR   SMR; P38894; -.
DR   BioGRID; 36645; 9.
DR   DIP; DIP-4056N; -.
DR   IntAct; P38894; 3.
DR   STRING; 4932.YHR211W; -.
DR   UniLectin; P38894; -.
DR   GlyCosmos; P38894; 6 sites, No reported glycans.
DR   GlyGen; P38894; 6 sites.
DR   PaxDb; 4932-YHR211W; -.
DR   EnsemblFungi; YHR211W_mRNA; YHR211W; YHR211W.
DR   GeneID; 856618; -.
DR   KEGG; sce:YHR211W; -.
DR   AGR; SGD:S000001254; -.
DR   SGD; S000001254; FLO5.
DR   VEuPathDB; FungiDB:YHR211W; -.
DR   eggNOG; ENOG502QPQC; Eukaryota.
DR   GeneTree; ENSGT00940000176342; -.
DR   HOGENOM; CLU_006076_0_0_1; -.
DR   InParanoid; P38894; -.
DR   OMA; TRGWAGN; -.
DR   OrthoDB; 2039698at2759; -.
DR   BioCyc; YEAST:G3O-31236-MONOMER; -.
DR   BioGRID-ORCS; 856618; 0 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P38894; -.
DR   PRO; PR:P38894; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P38894; Protein.
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:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005537; F:mannose binding; IMP:SGD.
DR   GO; GO:0031589; P:cell-substrate adhesion; IMP:SGD.
DR   GO; GO:0000128; P:flocculation; IMP:SGD.
DR   Gene3D; 2.60.120.1560; -; 1.
DR   Gene3D; 6.20.60.20; -; 1.
DR   InterPro; IPR001389; Flocculin.
DR   InterPro; IPR025928; Flocculin_t3_rpt.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   Pfam; PF00624; Flocculin; 8.
DR   Pfam; PF13928; Flocculin_t3; 3.
DR   Pfam; PF07691; PA14; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..1052
FT                   /note="Flocculation protein FLO5"
FT                   /id="PRO_0000021275"
FT   PROPEP          1053..1075
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021276"
FT   DOMAIN          74..249
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   REPEAT          278..322
FT                   /note="1-1"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          323..367
FT                   /note="1-2"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          368..412
FT                   /note="1-3"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          413..457
FT                   /note="1-4"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          458..502
FT                   /note="1-5"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          503..547
FT                   /note="1-6"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          548..592
FT                   /note="1-7"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          593..637
FT                   /note="1-8"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          667..686
FT                   /note="2-1"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          687..706
FT                   /note="2-2"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          775..825
FT                   /note="3-1"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          847..897
FT                   /note="3-2"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REPEAT          898..948
FT                   /note="3-3"
FT                   /evidence="ECO:0000269|PubMed:16086015"
FT   REGION          197..240
FT                   /note="Sugar recognition"
FT                   /evidence="ECO:0000250"
FT   REGION          278..637
FT                   /note="8 X 45 AA approximate tandem repeats, Thr-rich"
FT   REGION          322..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..394
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..706
FT                   /note="2 X 20 AA approximate tandem repeats, Ser-rich"
FT   REGION          702..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..948
FT                   /note="3 X 51 AA approximate repeats, Ser/Thr-rich"
FT   REGION          948..980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1038
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           1052
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        203
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        663
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        749
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   STRAND          36..45
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   HELIX           57..61
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   HELIX           63..66
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          69..76
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   TURN            125..128
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          135..144
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          147..157
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          160..168
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   TURN            169..171
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          189..192
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          196..198
FT                   /evidence="ECO:0007829|PDB:4AHW"
FT   STRAND          205..210
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          215..224
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          233..236
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          242..246
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   TURN            248..250
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          251..253
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   STRAND          264..266
FT                   /evidence="ECO:0007829|PDB:2XJP"
FT   TURN            268..270
FT                   /evidence="ECO:0007829|PDB:2XJP"
SQ   SEQUENCE   1075 AA;  111982 MW;  D151B370B60C8D9F CRC64;
     MTIAHHCIFL VILAFLALIN VASGATEACL PAGQRKSGMN INFYQYSLKD SSTYSNAAYM
     AYGYASKTKL GSVGGQTDIS IDYNIPCVSS SGTFPCPQED SYGNWGCKGM GACSNSQGIA
     YWSTDLFGFY TTPTNVTLEM TGYFLPPQTG SYTFSFATVD DSAILSVGGS IAFECCAQEQ
     PPITSTNFTI NGIKPWDGSL PDNITGTVYM YAGYYYPLKV VYSNAVSWGT LPISVELPDG
     TTVSDNFEGY VYSFDDDLSQ SNCTIPDPSI HTTSTITTTT EPWTGTFTST STEMTTITDT
     NGQLTDETVI VIRTPTTAST ITTTTEPWTG TFTSTSTEMT TVTGTNGQPT DETVIVIRTP
     TSEGLITTTT EPWTGTFTST STEMTTVTGT NGQPTDETVI VIRTPTSEGL ITTTTEPWTG
     TFTSTSTEVT TITGTNGQPT DETVIVIRTP TSEGLITTTT EPWTGTFTST STEMTTVTGT
     NGQPTDETVI VIRTPTSEGL ISTTTEPWTG TFTSTSTEVT TITGTNGQPT DETVIVIRTP
     TSEGLITTTT EPWTGTFTST STEMTTVTGT NGQPTDETVI VIRTPTSEGL ITRTTEPWTG
     TFTSTSTEVT TITGTNGQPT DETVIVIRTP TTAISSSLSS SSGQITSSIT SSRPIITPFY
     PSNGTSVISS SVISSSVTSS LVTSSSFISS SVISSSTTTS TSIFSESSTS SVIPTSSSTS
     GSSESKTSSA SSSSSSSSIS SESPKSPTNS SSSLPPVTSA TTGQETASSL PPATTTKTSE
     QTTLVTVTSC ESHVCTESIS SAIVSTATVT VSGVTTEYTT WCPISTTETT KQTKGTTEQT
     KGTTEQTTET TKQTTVVTIS SCESDICSKT ASPAIVSTST ATINGVTTEY TTWCPISTTE
     SKQQTTLVTV TSCESGVCSE TTSPAIVSTA TATVNDVVTV YPTWRPQTTN EQSVSSKMNS
     ATSETTTNTG AAETKTAVTS SLSRFNHAET QTASATDVIG HSSSVVSVSE TGNTMSLTSS
     GLSTMSQQPR STPASSMVGS STASLEISTY AGSANSLLAG SGLSVFIASL LLAII
//