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Protein

Flocculation protein FLO11

Gene

FLO11

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • cell adhesion involved in single-species biofilm formation Source: SGD
  • coflocculation Source: SGD
  • filamentous growth Source: SGD
  • flocculation Source: SGD
  • invasive growth in response to glucose limitation Source: SGD
  • pseudohyphal growth Source: SGD
  • single organismal cell-cell adhesion Source: SGD
  • single-species biofilm formation on inanimate substrate Source: SGD
  • single-species surface biofilm formation Source: SGD
Complete GO annotation...

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
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIR019C.
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

  • anchored component of membrane Source: UniProtKB-KW
  • cellular bud neck Source: SGD
  • cell wall Source: UniProtKB-SubCell
  • extracellular region Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

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

Interactioni

Protein-protein interaction databases

BioGridi35011. 78 interactions.
DIPiDIP-7821N.
IntActiP08640. 2 interactions.
MINTiMINT-2782681.

Structurei

Secondary structure

1
1367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Beta strandi41 – 433Combined sources
Helixi50 – 545Combined sources
Turni55 – 573Combined sources
Beta strandi61 – 7212Combined sources
Beta strandi75 – 8612Combined sources
Helixi90 – 923Combined sources
Beta strandi93 – 1008Combined sources
Beta strandi102 – 1043Combined sources
Beta strandi108 – 1125Combined sources
Turni113 – 1164Combined sources
Beta strandi125 – 1339Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi149 – 1557Combined sources
Helixi157 – 1659Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi186 – 1927Combined sources
Beta strandi195 – 1984Combined sources
Helixi199 – 2013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UYRX-ray0.89A22-211[»]
4UYSX-ray1.05A30-211[»]
4UYTX-ray1.03A30-211[»]
ProteinModelPortaliP08640.
SMRiP08640. Positions 33-206.
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

GeneTreeiENSGT00730000112629.
InParanoidiP08640.
KOiK19851.
OMAiDPQEQTS.
OrthoDBiEOG092C5RNX.

Family and domain databases

InterProiIPR018789. Uncharacterised_Flo11-rel_N.
[Graphical view]
PfamiPF10182. Flo11. 1 hit.
[Graphical view]
SMARTiSM01213. 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

« Hide

        10         20         30         40         50
MQRPFLLAYL VLSLLFNSAL GFPTALVPRG SSEGTSCNSI VNGCPNLDFN
60 70 80 90 100
WHMDQQNIMQ YTLDVTSVSW VQDNTYQITI HVKGKENIDL KYLWSLKIIG
110 120 130 140 150
VTGPKGTVQL YGYNENTYLI DNPTDFTATF EVYATQDVNS CQVWMPNFQI
160 170 180 190 200
QFEYLQGSAA QYASSWQWGT TSFDLSTGCN NYDNQGHSQT DFPGFYWNID
210 220 230 240 250
CDNNCGGTKS STTTSSTSES STTTSSTSES STTTSSTSES STTTSSTSES
260 270 280 290 300
STSSSTTAPA TPTTTSCTKE KPTPPTTTSC TKEKPTPPHH DTTPCTKKKT
310 320 330 340 350
TTSKTCTKKT TTPVPTPSSS TTESSSAPVP TPSSSTTESS SAPVTSSTTE
360 370 380 390 400
SSSAPVPTPS SSTTESSSAP VTSSTTESSS APVTSSTTES SSAPVPTPSS
410 420 430 440 450
STTESSSAPV TSSTTESSSA PVTSSTTESS SAPVTSSTTE SSSAPVTSST
460 470 480 490 500
TESSSAPVPT PSSSTTESSS APVTSSTTES SSAPVPTPSS STTESSSAPV
510 520 530 540 550
TSSTTESSSA PVPTPSSSTT ESSSAPAPTP SSSTTESSSA PVTSSTTESS
560 570 580 590 600
SAPVPTPSSS TTESSSTPVT SSTTESSSAP VPTPSSSTTE SSSAPVPTPS
610 620 630 640 650
SSTTESSSAP APTPSSSTTE SSSAPVTSST TESSSAPVPT PSSSTTESSS
660 670 680 690 700
APVPTPSSST TESSSAPVPT PSSSTTESSS APVTSSTTES SSAPVTSSTT
710 720 730 740 750
ESSSAPVPTP SSSTTESSSA PVPTPSSSTT ESSSAPVPTP SSSTTESSSA
760 770 780 790 800
PVTSSTTESS SAPVPTPSSS TTESSSAPVP TPSSSTTESS SAPVPTPSSS
810 820 830 840 850
TTESSVAPVP TPSSSSNITS SAPSSTPFSS STESSSVPVP TPSSSTTESS
860 870 880 890 900
SAPVSSSTTE SSVAPVPTPS SSSNITSSAP SSIPFSSTTE SFSTGTTVTP
910 920 930 940 950
SSSKYPGSQT ETSVSSTTET TIVPTKTTTS VTTPSTTTIT TTVCSTGTNS
960 970 980 990 1000
AGETTSGCSP KTVTTTVPTT TTTSVTTSST TTITTTVCST GTNSAGETTS
1010 1020 1030 1040 1050
GCSPKTITTT VPCSTSPSET ASESTTTSPT TPVTTVVSTT VVTTEYSTST
1060 1070 1080 1090 1100
KPGGEITTTF VTKNIPTTYL TTIAPTPSVT TVTNFTPTTI TTTVCSTGTN
1110 1120 1130 1140 1150
SAGETTSGCS PKTVTTTVPC STGTGEYTTE ATTLVTTAVT TTVVTTESST
1160 1170 1180 1190 1200
GTNSAGKTTT GYTTKSVPTT YVTTLAPSAP VTPATNAVPT TITTTECSAA
1210 1220 1230 1240 1250
TNAAGETTSV CSAKTIVSSA SAGENTAPSA TTPVTTAIPT TVITTESSVG
1260 1270 1280 1290 1300
TNSAGETTTG YTTKSIPTTY ITTLIPGSNG AKNYETVATA TNPISIKTTS
1310 1320 1330 1340 1350
QLATTASASS VAPVVTSPSL TGPLQSASGS AVATYSVPSI SSTYQGAANI
1360
KVLGNFMWLL LALPVVF
Length:1,367
Mass (Da):136,111
Last modified:February 1, 1995 - v2
Checksum:i91C00E2DBD61AA9D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4UYRX-ray0.89A22-211[»]
4UYSX-ray1.05A30-211[»]
4UYTX-ray1.03A30-211[»]
ProteinModelPortaliP08640.
SMRiP08640. Positions 33-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35011. 78 interactions.
DIPiDIP-7821N.
IntActiP08640. 2 interactions.
MINTiMINT-2782681.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YIR019C.
SGDiS000001458. FLO11.

Phylogenomic databases

GeneTreeiENSGT00730000112629.
InParanoidiP08640.
KOiK19851.
OMAiDPQEQTS.
OrthoDBiEOG092C5RNX.

Enzyme and pathway databases

BioCyciYEAST:G3O-31439-MONOMER.

Miscellaneous databases

PROiP08640.

Family and domain databases

InterProiIPR018789. Uncharacterised_Flo11-rel_N.
[Graphical view]
PfamiPF10182. Flo11. 1 hit.
[Graphical view]
SMARTiSM01213. Flo11. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: September 7, 2016
This is version 131 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

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.