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P08640

- FLO11_YEAST

UniProt

P08640 - FLO11_YEAST

Protein

Flocculation protein FLO11

Gene

FLO11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Cell wall protein that participates in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca2+-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. Also involved in cell-substrate adhesion, haploid invasive growth, diploid pseudohyphae formation and biofilm (flor) development. The precise mechanism by which this protein mediates adhesion is unclear but may involve homotypic binding. Adhesive activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose.9 Publications

    GO - Biological processi

    1. biofilm formation Source: SGD
    2. filamentous growth Source: SGD
    3. flocculation Source: SGD
    4. invasive growth in response to glucose limitation Source: SGD
    5. pseudohyphal growth Source: SGD
    6. single organismal cell-cell adhesion Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31439-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flocculation protein FLO11
    Short name:
    Flo11p
    Short name:
    Flocculin-11
    Alternative name(s):
    Mucin-like protein 1
    Gene namesi
    Name:FLO11
    Synonyms:MAL5, MUC1, S1, S2
    Ordered Locus Names:YIR019C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IX

    Organism-specific databases

    CYGDiYIR019c.
    SGDiS000001458. FLO11.

    Subcellular locationi

    Secretedcell wall. Membrane; Lipid-anchorGPI-anchor
    Note: The protein is attached to the cell wall via a GPI-anchor and is also shed liberally into extracellular fluid; increased shedding is associated with biofilm mat expansion but decreased invasive growth.

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. cellular bud neck Source: SGD
    3. cell wall Source: UniProtKB-SubCell
    4. extracellular region Source: SGD
    5. plasma membrane Source: SGD

    Keywords - Cellular componenti

    Cell wall, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1340 – 136728Missing: Increased shedding, associated with loss of GPI-anchor site. 1 PublicationAdd
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 13461325Flocculation protein FLO11PRO_0000019586Add
    BLAST
    Propeptidei1347 – 136721Removed in mature formSequence AnalysisPRO_0000019587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi817 – 8171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi874 – 8741N-linked (GlcNAc...)Sequence Analysis
    Lipidationi1346 – 13461GPI-anchor amidated glycineSequence Analysis

    Post-translational modificationi

    Extensively O-mannosylated.
    The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer By similarity.By similarity
    A soluble form is probably produced by proteolytic cleavage at the cell surface (shedding).

    Keywords - PTMi

    Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PeptideAtlasiP08640.

    Expressioni

    Gene expression databases

    GenevestigatoriP08640.

    Interactioni

    Protein-protein interaction databases

    BioGridi35011. 78 interactions.
    IntActiP08640. 2 interactions.
    MINTiMINT-2782681.

    Structurei

    3D structure databases

    ProteinModelPortaliP08640.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati210 – 219101-11 Publication
    Repeati220 – 229101-21 Publication
    Repeati230 – 239101-31 Publication
    Repeati240 – 249101-41 Publication
    Repeati262 – 274132-11 PublicationAdd
    BLAST
    Repeati275 – 287132-21 PublicationAdd
    BLAST
    Repeati313 – 327153-11 PublicationAdd
    BLAST
    Repeati328 – 342153-21 PublicationAdd
    BLAST
    Repeati343 – 354124-11 PublicationAdd
    BLAST
    Repeati355 – 369153-31 PublicationAdd
    BLAST
    Repeati370 – 381124-21 PublicationAdd
    BLAST
    Repeati382 – 393124-31 PublicationAdd
    BLAST
    Repeati394 – 408153-41 PublicationAdd
    BLAST
    Repeati409 – 420124-41 PublicationAdd
    BLAST
    Repeati421 – 432124-51 PublicationAdd
    BLAST
    Repeati433 – 444124-61 PublicationAdd
    BLAST
    Repeati445 – 456124-71 PublicationAdd
    BLAST
    Repeati457 – 471153-51 PublicationAdd
    BLAST
    Repeati472 – 483124-81 PublicationAdd
    BLAST
    Repeati484 – 498153-61 PublicationAdd
    BLAST
    Repeati499 – 510124-91 PublicationAdd
    BLAST
    Repeati511 – 525153-71 PublicationAdd
    BLAST
    Repeati526 – 540153-81 PublicationAdd
    BLAST
    Repeati541 – 552124-101 PublicationAdd
    BLAST
    Repeati568 – 579124-111 PublicationAdd
    BLAST
    Repeati580 – 594153-91 PublicationAdd
    BLAST
    Repeati595 – 609153-101 PublicationAdd
    BLAST
    Repeati610 – 625163-111 PublicationAdd
    BLAST
    Repeati625 – 636124-121 PublicationAdd
    BLAST
    Repeati637 – 651153-121 PublicationAdd
    BLAST
    Repeati652 – 666153-131 PublicationAdd
    BLAST
    Repeati667 – 681153-141 PublicationAdd
    BLAST
    Repeati682 – 693124-131 PublicationAdd
    BLAST
    Repeati694 – 705124-141 PublicationAdd
    BLAST
    Repeati706 – 720153-151 PublicationAdd
    BLAST
    Repeati721 – 735153-161 PublicationAdd
    BLAST
    Repeati736 – 750153-171 PublicationAdd
    BLAST
    Repeati751 – 762124-151 PublicationAdd
    BLAST
    Repeati763 – 777153-181 PublicationAdd
    BLAST
    Repeati778 – 792153-191 PublicationAdd
    BLAST
    Repeati808 – 822153-211 PublicationAdd
    BLAST
    Repeati838 – 852153-201 PublicationAdd
    BLAST
    Repeati865 – 879153-221 PublicationAdd
    BLAST
    Repeati937 – 968325-11 PublicationAdd
    BLAST
    Repeati981 – 1012325-21 PublicationAdd
    BLAST
    Repeati1088 – 1119325-31 PublicationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni22 – 209188Involved in homotypic bindingCuratedAdd
    BLAST
    Regioni210 – 249404 X 10 AA repeats, Ser/Thr-richAdd
    BLAST
    Regioni262 – 287262 X 13 AA repeats, Thr-richAdd
    BLAST
    Regioni313 – 85254022 X 15 AA approximate repeats, Ser-richAdd
    BLAST
    Regioni343 – 76242015 X 12 AA repeats, Ser/Thr-richAdd
    BLAST
    Regioni937 – 11191833 X 32 AA tandem repeats, Thr-richAdd
    BLAST

    Domaini

    The number of the intragenic tandem repeats varies between different S.cerevisiae strains. There is a linear correlation between protein size and the extend of adhesion: the more repeats, the stronger the adhesion properties and the greater the fraction of flocculating cells By similarity.By similarity
    In vitro, the N-terminal region (residues 22-209) binds homotypically but does not interact with mannose.1 Publication

    Sequence similaritiesi

    Belongs to the flocculin family. Highly divergent.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00730000112629.
    KOiK01178.
    OMAiADQFTYV.
    OrthoDBiEOG7S7SS8.

    Family and domain databases

    InterProiIPR018789. Uncharacterised_Flo11-rel_N.
    [Graphical view]
    PfamiPF10182. Flo11. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08640-1 [UniParc]FASTAAdd to Basket

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    MQRPFLLAYL VLSLLFNSAL GFPTALVPRG SSEGTSCNSI VNGCPNLDFN     50
    WHMDQQNIMQ YTLDVTSVSW VQDNTYQITI HVKGKENIDL KYLWSLKIIG 100
    VTGPKGTVQL YGYNENTYLI DNPTDFTATF EVYATQDVNS CQVWMPNFQI 150
    QFEYLQGSAA QYASSWQWGT TSFDLSTGCN NYDNQGHSQT DFPGFYWNID 200
    CDNNCGGTKS STTTSSTSES STTTSSTSES STTTSSTSES STTTSSTSES 250
    STSSSTTAPA TPTTTSCTKE KPTPPTTTSC TKEKPTPPHH DTTPCTKKKT 300
    TTSKTCTKKT TTPVPTPSSS TTESSSAPVP TPSSSTTESS SAPVTSSTTE 350
    SSSAPVPTPS SSTTESSSAP VTSSTTESSS APVTSSTTES SSAPVPTPSS 400
    STTESSSAPV TSSTTESSSA PVTSSTTESS SAPVTSSTTE SSSAPVTSST 450
    TESSSAPVPT PSSSTTESSS APVTSSTTES SSAPVPTPSS STTESSSAPV 500
    TSSTTESSSA PVPTPSSSTT ESSSAPAPTP SSSTTESSSA PVTSSTTESS 550
    SAPVPTPSSS TTESSSTPVT SSTTESSSAP VPTPSSSTTE SSSAPVPTPS 600
    SSTTESSSAP APTPSSSTTE SSSAPVTSST TESSSAPVPT PSSSTTESSS 650
    APVPTPSSST TESSSAPVPT PSSSTTESSS APVTSSTTES SSAPVTSSTT 700
    ESSSAPVPTP SSSTTESSSA PVPTPSSSTT ESSSAPVPTP SSSTTESSSA 750
    PVTSSTTESS SAPVPTPSSS TTESSSAPVP TPSSSTTESS SAPVPTPSSS 800
    TTESSVAPVP TPSSSSNITS SAPSSTPFSS STESSSVPVP TPSSSTTESS 850
    SAPVSSSTTE SSVAPVPTPS SSSNITSSAP SSIPFSSTTE SFSTGTTVTP 900
    SSSKYPGSQT ETSVSSTTET TIVPTKTTTS VTTPSTTTIT TTVCSTGTNS 950
    AGETTSGCSP KTVTTTVPTT TTTSVTTSST TTITTTVCST GTNSAGETTS 1000
    GCSPKTITTT VPCSTSPSET ASESTTTSPT TPVTTVVSTT VVTTEYSTST 1050
    KPGGEITTTF VTKNIPTTYL TTIAPTPSVT TVTNFTPTTI TTTVCSTGTN 1100
    SAGETTSGCS PKTVTTTVPC STGTGEYTTE ATTLVTTAVT TTVVTTESST 1150
    GTNSAGKTTT GYTTKSVPTT YVTTLAPSAP VTPATNAVPT TITTTECSAA 1200
    TNAAGETTSV CSAKTIVSSA SAGENTAPSA TTPVTTAIPT TVITTESSVG 1250
    TNSAGETTTG YTTKSIPTTY ITTLIPGSNG AKNYETVATA TNPISIKTTS 1300
    QLATTASASS VAPVVTSPSL TGPLQSASGS AVATYSVPSI SSTYQGAANI 1350
    KVLGNFMWLL LALPVVF 1367
    Length:1,367
    Mass (Da):136,111
    Last modified:February 1, 1995 - v2
    Checksum:i91C00E2DBD61AA9D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38061 Genomic DNA. Translation: CAA86176.1.
    M16164 Genomic DNA. Translation: AAA35014.1.
    M16165 Genomic DNA. Translation: AAA35015.1.
    X13857 Genomic DNA. Translation: CAA32069.1.
    BK006942 Genomic DNA. Translation: DAA08566.1.
    PIRiS48478.
    RefSeqiNP_012284.3. NM_001179541.3.

    Genome annotation databases

    EnsemblFungiiYIR019C; YIR019C; YIR019C.
    GeneIDi854836.
    KEGGisce:YIR019C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z38061 Genomic DNA. Translation: CAA86176.1 .
    M16164 Genomic DNA. Translation: AAA35014.1 .
    M16165 Genomic DNA. Translation: AAA35015.1 .
    X13857 Genomic DNA. Translation: CAA32069.1 .
    BK006942 Genomic DNA. Translation: DAA08566.1 .
    PIRi S48478.
    RefSeqi NP_012284.3. NM_001179541.3.

    3D structure databases

    ProteinModelPortali P08640.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35011. 78 interactions.
    IntActi P08640. 2 interactions.
    MINTi MINT-2782681.

    Proteomic databases

    PeptideAtlasi P08640.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YIR019C ; YIR019C ; YIR019C .
    GeneIDi 854836.
    KEGGi sce:YIR019C.

    Organism-specific databases

    CYGDi YIR019c.
    SGDi S000001458. FLO11.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00730000112629.
    KOi K01178.
    OMAi ADQFTYV.
    OrthoDBi EOG7S7SS8.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31439-MONOMER.

    Miscellaneous databases

    NextBioi 977713.
    PROi P08640.

    Gene expression databases

    Genevestigatori P08640.

    Family and domain databases

    InterProi IPR018789. Uncharacterised_Flo11-rel_N.
    [Graphical view ]
    Pfami PF10182. Flo11. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. "Gene fusion is a possible mechanism underlying the evolution of STA1."
      Yamashita I., Nakamura M., Fukui S.
      J. Bacteriol. 169:2142-2149(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242 AND 762-1331.
    4. "Similar short elements in the 5' regions of the STA2 and SGA genes from Saccharomyces cerevisiae."
      Pardo J.M., Ianez E., Zalacain M., Claros M.G., Jimenez A.
      FEBS Lett. 239:179-184(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
      Strain: SPX101-1C.
    5. "FLO11, a yeast gene related to the STA genes, encodes a novel cell surface flocculin."
      Lo W.S., Dranginis A.M.
      J. Bacteriol. 178:7144-7151(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "Muc1, a mucin-like protein that is regulated by Mss10, is critical for pseudohyphal differentiation in yeast."
      Lambrechts M.G., Bauer F.F., Marmur J., Pretorius I.S.
      Proc. Natl. Acad. Sci. U.S.A. 93:8419-8424(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins."
      Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.
      J. Bacteriol. 181:3886-3889(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "A Saccharomyces gene family involved in invasive growth, cell-cell adhesion, and mating."
      Guo B., Styles C.A., Feng Q., Fink G.R.
      Proc. Natl. Acad. Sci. U.S.A. 97:12158-12163(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Bakers' yeast, a model for fungal biofilm formation."
      Reynolds T.B., Fink G.R.
      Science 291:878-881(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Sigma 1278B.
    10. "Characteristics of Flo11-dependent flocculation in Saccharomyces cerevisiae."
      Bayly J.C., Douglas L.M., Pretorius I.S., Bauer F.F., Dranginis A.M.
      FEMS Yeast Res. 5:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Intragenic tandem repeats generate functional variability."
      Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.
      Nat. Genet. 37:986-990(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REPEATS.
    12. "Expression and characterization of the flocculin Flo11/Muc1, a Saccharomyces cerevisiae mannoprotein with homotypic properties of adhesion."
      Douglas L.M., Li L., Yang Y., Dranginis A.M.
      Eukaryot. Cell 6:2214-2221(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GLYCOSYLATION.
    13. "Differential Flo8p-dependent regulation of FLO1 and FLO11 for cell-cell and cell-substrate adherence of S.cerevisiae S288c."
      Fichtner L., Schulze F., Braus G.H.
      Mol. Microbiol. 66:1276-1289(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: Sigma 1278B.
    14. "Shedding of the mucin-like flocculin Flo11p reveals a new aspect of fungal adhesion regulation."
      Karunanithi S., Vadaie N., Chavel C.A., Birkaya B., Joshi J., Grell L., Cullen P.J.
      Curr. Biol. 20:1389-1395(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SHEDDING, MUTAGENESIS OF 1340-ILE--PHE-1367.
    15. "The N-terminal domain of the Flo11 protein from Saccharomyces cerevisiae is an adhesin without mannose-binding activity."
      Goossens K.V., Willaert R.G.
      FEMS Yeast Res. 12:78-87(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN, GLYCOSYLATION.

    Entry informationi

    Entry nameiFLO11_YEAST
    AccessioniPrimary (citable) accession number: P08640
    Secondary accession number(s): D6VVV0, P08068
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IX
      Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

    External Data

    Dasty 3