FLO5_YEAST
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 03-AUG-2022, entry version 159.
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 PaxDb; P38894; -.
DR EnsemblFungi; YHR211W_mRNA; YHR211W; YHR211W.
DR GeneID; 856618; -.
DR KEGG; sce:YHR211W; -.
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; DISTTTH; -.
DR BioCyc; YEAST:G3O-31236-MON; -.
DR EvolutionaryTrace; P38894; -.
DR PRO; PR:P38894; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38894; 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: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 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 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
