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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)DescriptionActionsGraphical viewLength
Mutagenesisi1340 – 1367Missing : Increased shedding, associated with loss of GPI-anchor site. 1 PublicationAdd BLAST28

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001958622 – 1346Flocculation protein FLO11Add BLAST1325
PropeptideiPRO_00000195871347 – 1367Removed in mature formSequence analysisAdd BLAST21

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi817N-linked (GlcNAc...)Sequence analysis1
Glycosylationi874N-linked (GlcNAc...)Sequence analysis1
Lipidationi1346GPI-anchor amidated glycineSequence analysis1

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

PRIDEiP08640.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

11367
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi31 – 33Combined sources3
Beta strandi41 – 43Combined sources3
Helixi50 – 54Combined sources5
Turni55 – 57Combined sources3
Beta strandi61 – 72Combined sources12
Beta strandi75 – 86Combined sources12
Helixi90 – 92Combined sources3
Beta strandi93 – 100Combined sources8
Beta strandi102 – 104Combined sources3
Beta strandi108 – 112Combined sources5
Turni113 – 116Combined sources4
Beta strandi125 – 133Combined sources9
Beta strandi136 – 139Combined sources4
Beta strandi142 – 144Combined sources3
Beta strandi149 – 155Combined sources7
Helixi157 – 165Combined sources9
Beta strandi171 – 177Combined sources7
Beta strandi186 – 192Combined sources7
Beta strandi195 – 198Combined sources4
Helixi199 – 201Combined sources3

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati210 – 2191-11 Publication10
Repeati220 – 2291-21 Publication10
Repeati230 – 2391-31 Publication10
Repeati240 – 2491-41 Publication10
Repeati262 – 2742-11 PublicationAdd BLAST13
Repeati275 – 2872-21 PublicationAdd BLAST13
Repeati313 – 3273-11 PublicationAdd BLAST15
Repeati328 – 3423-21 PublicationAdd BLAST15
Repeati343 – 3544-11 PublicationAdd BLAST12
Repeati355 – 3693-31 PublicationAdd BLAST15
Repeati370 – 3814-21 PublicationAdd BLAST12
Repeati382 – 3934-31 PublicationAdd BLAST12
Repeati394 – 4083-41 PublicationAdd BLAST15
Repeati409 – 4204-41 PublicationAdd BLAST12
Repeati421 – 4324-51 PublicationAdd BLAST12
Repeati433 – 4444-61 PublicationAdd BLAST12
Repeati445 – 4564-71 PublicationAdd BLAST12
Repeati457 – 4713-51 PublicationAdd BLAST15
Repeati472 – 4834-81 PublicationAdd BLAST12
Repeati484 – 4983-61 PublicationAdd BLAST15
Repeati499 – 5104-91 PublicationAdd BLAST12
Repeati511 – 5253-71 PublicationAdd BLAST15
Repeati526 – 5403-81 PublicationAdd BLAST15
Repeati541 – 5524-101 PublicationAdd BLAST12
Repeati568 – 5794-111 PublicationAdd BLAST12
Repeati580 – 5943-91 PublicationAdd BLAST15
Repeati595 – 6093-101 PublicationAdd BLAST15
Repeati610 – 6253-111 PublicationAdd BLAST16
Repeati625 – 6364-121 PublicationAdd BLAST12
Repeati637 – 6513-121 PublicationAdd BLAST15
Repeati652 – 6663-131 PublicationAdd BLAST15
Repeati667 – 6813-141 PublicationAdd BLAST15
Repeati682 – 6934-131 PublicationAdd BLAST12
Repeati694 – 7054-141 PublicationAdd BLAST12
Repeati706 – 7203-151 PublicationAdd BLAST15
Repeati721 – 7353-161 PublicationAdd BLAST15
Repeati736 – 7503-171 PublicationAdd BLAST15
Repeati751 – 7624-151 PublicationAdd BLAST12
Repeati763 – 7773-181 PublicationAdd BLAST15
Repeati778 – 7923-191 PublicationAdd BLAST15
Repeati808 – 8223-211 PublicationAdd BLAST15
Repeati838 – 8523-201 PublicationAdd BLAST15
Repeati865 – 8793-221 PublicationAdd BLAST15
Repeati937 – 9685-11 PublicationAdd BLAST32
Repeati981 – 10125-21 PublicationAdd BLAST32
Repeati1088 – 11195-31 PublicationAdd BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 209Involved in homotypic bindingCuratedAdd BLAST188
Regioni210 – 2494 X 10 AA repeats, Ser/Thr-richAdd BLAST40
Regioni262 – 2872 X 13 AA repeats, Thr-richAdd BLAST26
Regioni313 – 85222 X 15 AA approximate repeats, Ser-richAdd BLAST540
Regioni343 – 76215 X 12 AA repeats, Ser/Thr-richAdd BLAST420
Regioni937 – 11193 X 32 AA tandem repeats, Thr-richAdd BLAST183

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UYRX-ray0.89A22-211[»]
4UYSX-ray1.05A30-211[»]
4UYTX-ray1.03A30-211[»]
ProteinModelPortaliP08640.
SMRiP08640.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PRIDEiP08640.

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: November 2, 2016
This is version 133 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.