FLO9_YEAST
ID FLO9_YEAST Reviewed; 1322 AA.
AC P39712; D6VPF6;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Flocculation protein FLO9;
DE Short=Flocculin-9;
DE Flags: Precursor;
GN Name=FLO9; OrderedLocusNames=YAL063C;
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=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 [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 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 [4]
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).
RN [5]
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).
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.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000305|PubMed:15470092}. Membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}. Note=Covalently-linked GPI-modified cell wall
CC protein (GPI-CWP).
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). The Ser/Thr-rich repeats are also important for
CC proper cell wall targeting of the protein. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the flocculin family. {ECO:0000305}.
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DR EMBL; U12980; AAC04971.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06926.1; -; Genomic_DNA.
DR PIR; S51959; S51959.
DR RefSeq; NP_009338.1; NM_001178205.1.
DR AlphaFoldDB; P39712; -.
DR SMR; P39712; -.
DR BioGRID; 31767; 32.
DR IntAct; P39712; 1.
DR STRING; 4932.YAL063C; -.
DR PaxDb; P39712; -.
DR EnsemblFungi; YAL063C_mRNA; YAL063C; YAL063C.
DR GeneID; 851236; -.
DR KEGG; sce:YAL063C; -.
DR SGD; S000000059; FLO9.
DR VEuPathDB; FungiDB:YAL063C; -.
DR eggNOG; ENOG502QPQC; Eukaryota.
DR GeneTree; ENSGT00940000176342; -.
DR HOGENOM; CLU_006076_0_0_1; -.
DR InParanoid; P39712; -.
DR OMA; ADAFTYQ; -.
DR BioCyc; YEAST:G3O-28864-MON; -.
DR PRO; PR:P39712; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P39712; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; ISS:SGD.
DR GO; GO:0005537; F:mannose binding; ISS: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; 13.
DR Pfam; PF13928; Flocculin_t3; 3.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM00758; PA14; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..1299
FT /note="Flocculation protein FLO9"
FT /id="PRO_0000021277"
FT PROPEP 1300..1322
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372454"
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 892..906
FT /note="2-1"
FT REPEAT 907..921
FT /note="2-2"
FT REPEAT 922..936
FT /note="2-3"
FT REPEAT 1013..1063
FT /note="3-1"
FT REPEAT 1085..1135
FT /note="3-2"
FT REPEAT 1136..1186
FT /note="3-3"
FT REGION 197..240
FT /note="Sugar recognition"
FT /evidence="ECO:0000250"
FT REGION 278..862
FT /note="13 X 45 AA approximate tandem repeats, Thr-rich"
FT REGION 770..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..936
FT /note="3 X 15 AA approximate repeats, Ser-rich"
FT REGION 950..1018
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1013..1186
FT /note="3 X 51 AA approximate repeats, Thr-rich"
FT REGION 1186..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1256..1284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1299
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 257
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 270
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 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 888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1322 AA; 138073 MW; AADFD1FF13267CEA CRC64;
MSLAHYCLLL AIVTLLGLTN VVSATTAACL PANSRKNGMN VNFYQYSLRD SSTYSNAAYM
AYGYASKTKL GSVGGQTDIS IDYNIPCVSS SGTFPCPQED LYGNWGCKGI GACSNNPIIA
YWSTDLFGFY TTPTNVTLEM TGYFLPPQTG SYTFKFATVD DSAILSVGGS IAFECCAQEQ
PPITSTNFTI NGIKPWNGSP PDNITGTVYM YAGFYYPMKI VYSNAVAWGT LPISVTLPDG
TTVSDDFEGY VYTFDNNLSQ PNCTIPDPSN YTVSTTITTT 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
TTATTAMTTT QPWNDTFTST STEMTTVTGT NGLPTDETII VIRTPTTATT AITTTEPWNS
TFTSTSTEMT TVTGTNGLPT DETIIVIRTP TTATTAITTT QPWNDTFTST STEMTTVTGT
NGLPTDETII VIRTPTTATT AMTTTQPWND TFTSTSTEIT TVTGTNGLPT DETIIVIRTP
TTATTAMTTT QPWNDTFTST STEMTTVTGT NGVPTDETVI VIRTPTSEGL ISTTTEPWTG
TFTSTSTEMT TVTGTNGQPT DETVIVIRTP TSEGLVTTTT EPWTGTFTST STEMTTITGT
NGQPTDETVI IVKTPTTAIS SSLSSSSGQI TSFITSARPI ITPFYPSNGT SVISSSVISS
SDTSSLVISS SVTSSLVTSS PVISSSFISS PVISSTTTSA SILSESSKSS VIPTSSSTSG
SSESETGSAS SASSSSSISS ESPKSTYSSS SLPPVTSATT SQEITSSLPP VTTTKTSEQT
TLVTVTSCES HVCTESISSA IVSTATVTVS GATTEYTTWC PISTTEITKQ TTETTKQTKG
TTEQTTETTK QTTVVTISSC ESDVCSKTAS PAIVSTSTAT INGVTTEYTT WCPISTTESK
QQTTLVTVTS CGSGVCSETT SPAIVSTATA TVNDVVTVYS TWRPQTTNEQ SVSSKMNSAT
SETTTNTGAA ETTTSTGAAE TKTVVTSSIS RFNHAETQTA SATDVIGHSS SVVSVSETGN
TKSLTSSGLS TMSQQPRSTP ASSMVGSSTA SLEISTYAGS ANSLLAGSGL SVFIASLLLA
II
