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Flocculation protein FLO11 (Flo11p) (Flocculin-11) (Mucin-like protein 1)

 FLO11_YEAST             Reviewed;        1367 AA.
P08640; D6VVV0; P08068;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
12-SEP-2018, entry version 149.
RecName: Full=Flocculation protein FLO11;
Short=Flo11p;
Short=Flocculin-11;
AltName: Full=Mucin-like protein 1;
Flags: Precursor;
Name=FLO11; Synonyms=MAL5, MUC1, S1, S2; OrderedLocusNames=YIR019C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242 AND 762-1331.
PubMed=3106330; DOI=10.1128/jb.169.5.2142-2149.1987;
Yamashita I., Nakamura M., Fukui S.;
"Gene fusion is a possible mechanism underlying the evolution of
STA1.";
J. Bacteriol. 169:2142-2149(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
STRAIN=SPX101-1C;
PubMed=3141213; DOI=10.1016/0014-5793(88)80912-8;
Pardo J.M., Ianez E., Zalacain M., Claros M.G., Jimenez A.;
"Similar short elements in the 5' regions of the STA2 and SGA genes
from Saccharomyces cerevisiae.";
FEBS Lett. 239:179-184(1988).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8955395; DOI=10.1128/jb.178.24.7144-7151.1996;
Lo W.S., Dranginis A.M.;
"FLO11, a yeast gene related to the STA genes, encodes a novel cell
surface flocculin.";
J. Bacteriol. 178:7144-7151(1996).
[6]
FUNCTION.
PubMed=8710886; DOI=10.1073/pnas.93.16.8419;
Lambrechts M.G., Bauer F.F., Marmur J., Pretorius I.S.;
"Muc1, a mucin-like protein that is regulated by Mss10, is critical
for pseudohyphal differentiation in yeast.";
Proc. Natl. Acad. Sci. U.S.A. 93:8419-8424(1996).
[7]
SUBCELLULAR LOCATION.
PubMed=10383953;
Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.;
"Amino acid residues in the omega-minus region participate in cellular
localization of yeast glycosylphosphatidylinositol-attached
proteins.";
J. Bacteriol. 181:3886-3889(1999).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11027318; DOI=10.1073/pnas.220420397;
Guo B., Styles C.A., Feng Q., Fink G.R.;
"A Saccharomyces gene family involved in invasive growth, cell-cell
adhesion, and mating.";
Proc. Natl. Acad. Sci. U.S.A. 97:12158-12163(2000).
[9]
FUNCTION.
STRAIN=Sigma 1278B;
PubMed=11157168; DOI=10.1126/science.291.5505.878;
Reynolds T.B., Fink G.R.;
"Bakers' yeast, a model for fungal biofilm formation.";
Science 291:878-881(2001).
[10]
FUNCTION.
PubMed=16043420; DOI=10.1016/j.femsyr.2005.05.004;
Bayly J.C., Douglas L.M., Pretorius I.S., Bauer F.F., Dranginis A.M.;
"Characteristics of Flo11-dependent flocculation in Saccharomyces
cerevisiae.";
FEMS Yeast Res. 5:1151-1156(2005).
[11]
REPEATS.
PubMed=16086015; DOI=10.1038/ng1618;
Verstrepen K.J., Jansen A., Lewitter F., Fink G.R.;
"Intragenic tandem repeats generate functional variability.";
Nat. Genet. 37:986-990(2005).
[12]
FUNCTION, AND GLYCOSYLATION.
PubMed=17921350; DOI=10.1128/EC.00284-06;
Douglas L.M., Li L., Yang Y., Dranginis A.M.;
"Expression and characterization of the flocculin Flo11/Muc1, a
Saccharomyces cerevisiae mannoprotein with homotypic properties of
adhesion.";
Eukaryot. Cell 6:2214-2221(2007).
[13]
FUNCTION.
STRAIN=Sigma 1278B;
PubMed=18001350; DOI=10.1111/j.1365-2958.2007.06014.x;
Fichtner L., Schulze F., Braus G.H.;
"Differential Flo8p-dependent regulation of FLO1 and FLO11 for cell-
cell and cell-substrate adherence of S.cerevisiae S288c.";
Mol. Microbiol. 66:1276-1289(2007).
[14]
FUNCTION, SUBCELLULAR LOCATION, SHEDDING, AND MUTAGENESIS OF
1340-ILE--PHE-1367.
PubMed=20619652; DOI=10.1016/j.cub.2010.06.033;
Karunanithi S., Vadaie N., Chavel C.A., Birkaya B., Joshi J.,
Grell L., Cullen P.J.;
"Shedding of the mucin-like flocculin Flo11p reveals a new aspect of
fungal adhesion regulation.";
Curr. Biol. 20:1389-1395(2010).
[15]
FUNCTION, DOMAIN, AND GLYCOSYLATION.
PubMed=22129043; DOI=10.1111/j.1567-1364.2011.00766.x;
Goossens K.V., Willaert R.G.;
"The N-terminal domain of the Flo11 protein from Saccharomyces
cerevisiae is an adhesin without mannose-binding activity.";
FEMS Yeast Res. 12:78-87(2012).
-!- FUNCTION: Cell wall protein that participates in adhesive cell-
cell interactions during yeast flocculation, a reversible, asexual
and Ca(2+)-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.
{ECO:0000269|PubMed:11027318, ECO:0000269|PubMed:11157168,
ECO:0000269|PubMed:16043420, ECO:0000269|PubMed:17921350,
ECO:0000269|PubMed:18001350, ECO:0000269|PubMed:20619652,
ECO:0000269|PubMed:22129043, ECO:0000269|PubMed:8710886,
ECO:0000269|PubMed:8955395}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-2585, EBI-2585;
-!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Lipid-anchor,
GPI-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.
-!- DOMAIN: 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). {ECO:0000250}.
-!- DOMAIN: In vitro, the N-terminal region (residues 22-209) binds
homotypically but does not interact with mannose.
{ECO:0000269|PubMed:22129043}.
-!- PTM: Extensively O-mannosylated.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: A soluble form is probably produced by proteolytic cleavage
at the cell surface (shedding).
-!- SIMILARITY: Belongs to the flocculin family. Highly divergent.
{ECO:0000305}.
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EMBL; Z38061; CAA86176.1; -; Genomic_DNA.
EMBL; M16164; AAA35014.1; -; Genomic_DNA.
EMBL; M16165; AAA35015.1; -; Genomic_DNA.
EMBL; X13857; CAA32069.1; -; Genomic_DNA.
EMBL; BK006942; DAA08566.1; -; Genomic_DNA.
PIR; S48478; S48478.
RefSeq; NP_012284.3; NM_001179541.3.
PDB; 4UYR; X-ray; 0.89 A; A=22-211.
PDB; 4UYS; X-ray; 1.05 A; A=30-211.
PDB; 4UYT; X-ray; 1.03 A; A=30-211.
PDBsum; 4UYR; -.
PDBsum; 4UYS; -.
PDBsum; 4UYT; -.
ProteinModelPortal; P08640; -.
SMR; P08640; -.
BioGrid; 35011; 115.
DIP; DIP-7821N; -.
IntAct; P08640; 2.
MINT; P08640; -.
STRING; 4932.YIR019C; -.
PaxDb; P08640; -.
PRIDE; P08640; -.
EnsemblFungi; YIR019C; YIR019C; YIR019C.
GeneID; 854836; -.
KEGG; sce:YIR019C; -.
EuPathDB; FungiDB:YIR019C; -.
SGD; S000001458; FLO11.
GeneTree; ENSGT00730000112629; -.
InParanoid; P08640; -.
KO; K19851; -.
OMA; KCNGPIS; -.
OrthoDB; EOG092C5RNX; -.
BioCyc; YEAST:G3O-31439-MONOMER; -.
PRO; PR:P08640; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0005576; C:extracellular region; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:SGD.
GO; GO:0098609; P:cell-cell adhesion; IMP:SGD.
GO; GO:0036281; P:coflocculation; IMP:SGD.
GO; GO:0030447; P:filamentous growth; IDA:SGD.
GO; GO:0000128; P:flocculation; IMP:SGD.
GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
GO; GO:0007124; P:pseudohyphal growth; IMP:SGD.
GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:SGD.
GO; GO:0090606; P:single-species surface biofilm formation; IMP:SGD.
InterPro; IPR018789; Flo11.
Pfam; PF10182; Flo11; 1.
SMART; SM01213; Flo11; 1.
PROSITE; PS51824; FLO11; 1.
1: Evidence at protein level;
3D-structure; Cell wall; Complete proteome; Glycoprotein; GPI-anchor;
Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 1346 Flocculation protein FLO11.
/FTId=PRO_0000019586.
PROPEP 1347 1367 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000019587.
DOMAIN 31 207 Flo11. {ECO:0000255|PROSITE-
ProRule:PRU01168}.
REPEAT 210 219 1-1. {ECO:0000269|PubMed:16086015}.
REPEAT 220 229 1-2. {ECO:0000269|PubMed:16086015}.
REPEAT 230 239 1-3. {ECO:0000269|PubMed:16086015}.
REPEAT 240 249 1-4. {ECO:0000269|PubMed:16086015}.
REPEAT 262 274 2-1. {ECO:0000269|PubMed:16086015}.
REPEAT 275 287 2-2. {ECO:0000269|PubMed:16086015}.
REPEAT 313 327 3-1. {ECO:0000269|PubMed:16086015}.
REPEAT 328 342 3-2. {ECO:0000269|PubMed:16086015}.
REPEAT 343 354 4-1. {ECO:0000269|PubMed:16086015}.
REPEAT 355 369 3-3. {ECO:0000269|PubMed:16086015}.
REPEAT 370 381 4-2. {ECO:0000269|PubMed:16086015}.
REPEAT 382 393 4-3. {ECO:0000269|PubMed:16086015}.
REPEAT 394 408 3-4. {ECO:0000269|PubMed:16086015}.
REPEAT 409 420 4-4. {ECO:0000269|PubMed:16086015}.
REPEAT 421 432 4-5. {ECO:0000269|PubMed:16086015}.
REPEAT 433 444 4-6. {ECO:0000269|PubMed:16086015}.
REPEAT 445 456 4-7. {ECO:0000269|PubMed:16086015}.
REPEAT 457 471 3-5. {ECO:0000269|PubMed:16086015}.
REPEAT 472 483 4-8. {ECO:0000269|PubMed:16086015}.
REPEAT 484 498 3-6. {ECO:0000269|PubMed:16086015}.
REPEAT 499 510 4-9. {ECO:0000269|PubMed:16086015}.
REPEAT 511 525 3-7. {ECO:0000269|PubMed:16086015}.
REPEAT 526 540 3-8. {ECO:0000269|PubMed:16086015}.
REPEAT 541 552 4-10. {ECO:0000269|PubMed:16086015}.
REPEAT 568 579 4-11. {ECO:0000269|PubMed:16086015}.
REPEAT 580 594 3-9. {ECO:0000269|PubMed:16086015}.
REPEAT 595 609 3-10. {ECO:0000269|PubMed:16086015}.
REPEAT 610 625 3-11. {ECO:0000269|PubMed:16086015}.
REPEAT 625 636 4-12. {ECO:0000269|PubMed:16086015}.
REPEAT 637 651 3-12. {ECO:0000269|PubMed:16086015}.
REPEAT 652 666 3-13. {ECO:0000269|PubMed:16086015}.
REPEAT 667 681 3-14. {ECO:0000269|PubMed:16086015}.
REPEAT 682 693 4-13. {ECO:0000269|PubMed:16086015}.
REPEAT 694 705 4-14. {ECO:0000269|PubMed:16086015}.
REPEAT 706 720 3-15. {ECO:0000269|PubMed:16086015}.
REPEAT 721 735 3-16. {ECO:0000269|PubMed:16086015}.
REPEAT 736 750 3-17. {ECO:0000269|PubMed:16086015}.
REPEAT 751 762 4-15. {ECO:0000269|PubMed:16086015}.
REPEAT 763 777 3-18. {ECO:0000269|PubMed:16086015}.
REPEAT 778 792 3-19. {ECO:0000269|PubMed:16086015}.
REPEAT 808 822 3-21. {ECO:0000269|PubMed:16086015}.
REPEAT 838 852 3-20. {ECO:0000269|PubMed:16086015}.
REPEAT 865 879 3-22. {ECO:0000269|PubMed:16086015}.
REPEAT 937 968 5-1. {ECO:0000269|PubMed:16086015}.
REPEAT 981 1012 5-2. {ECO:0000269|PubMed:16086015}.
REPEAT 1088 1119 5-3. {ECO:0000269|PubMed:16086015}.
REGION 22 209 Involved in homotypic binding.
{ECO:0000305}.
REGION 210 249 4 X 10 AA repeats, Ser/Thr-rich.
REGION 262 287 2 X 13 AA repeats, Thr-rich.
REGION 313 852 22 X 15 AA approximate repeats, Ser-rich.
REGION 343 762 15 X 12 AA repeats, Ser/Thr-rich.
REGION 937 1119 3 X 32 AA tandem repeats, Thr-rich.
LIPID 1346 1346 GPI-anchor amidated glycine.
{ECO:0000255}.
CARBOHYD 817 817 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 874 874 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 1340 1367 Missing: Increased shedding, associated
with loss of GPI-anchor site.
{ECO:0000269|PubMed:20619652}.
STRAND 31 33 {ECO:0000244|PDB:4UYR}.
STRAND 41 43 {ECO:0000244|PDB:4UYR}.
HELIX 50 54 {ECO:0000244|PDB:4UYR}.
TURN 55 57 {ECO:0000244|PDB:4UYR}.
STRAND 61 72 {ECO:0000244|PDB:4UYR}.
STRAND 75 86 {ECO:0000244|PDB:4UYR}.
HELIX 90 92 {ECO:0000244|PDB:4UYR}.
STRAND 93 100 {ECO:0000244|PDB:4UYR}.
STRAND 102 104 {ECO:0000244|PDB:4UYR}.
STRAND 108 112 {ECO:0000244|PDB:4UYR}.
TURN 113 116 {ECO:0000244|PDB:4UYR}.
STRAND 125 133 {ECO:0000244|PDB:4UYR}.
STRAND 136 139 {ECO:0000244|PDB:4UYR}.
STRAND 142 144 {ECO:0000244|PDB:4UYR}.
STRAND 149 155 {ECO:0000244|PDB:4UYR}.
HELIX 157 165 {ECO:0000244|PDB:4UYR}.
STRAND 171 177 {ECO:0000244|PDB:4UYR}.
STRAND 186 192 {ECO:0000244|PDB:4UYR}.
STRAND 195 198 {ECO:0000244|PDB:4UYR}.
HELIX 199 201 {ECO:0000244|PDB:4UYR}.
SEQUENCE 1367 AA; 136111 MW; 91C00E2DBD61AA9D CRC64;
MQRPFLLAYL VLSLLFNSAL GFPTALVPRG SSEGTSCNSI VNGCPNLDFN WHMDQQNIMQ
YTLDVTSVSW VQDNTYQITI HVKGKENIDL KYLWSLKIIG VTGPKGTVQL YGYNENTYLI
DNPTDFTATF EVYATQDVNS CQVWMPNFQI QFEYLQGSAA QYASSWQWGT TSFDLSTGCN
NYDNQGHSQT DFPGFYWNID CDNNCGGTKS STTTSSTSES STTTSSTSES STTTSSTSES
STTTSSTSES STSSSTTAPA TPTTTSCTKE KPTPPTTTSC TKEKPTPPHH DTTPCTKKKT
TTSKTCTKKT TTPVPTPSSS TTESSSAPVP TPSSSTTESS SAPVTSSTTE SSSAPVPTPS
SSTTESSSAP VTSSTTESSS APVTSSTTES SSAPVPTPSS STTESSSAPV TSSTTESSSA
PVTSSTTESS SAPVTSSTTE SSSAPVTSST TESSSAPVPT PSSSTTESSS APVTSSTTES
SSAPVPTPSS STTESSSAPV TSSTTESSSA PVPTPSSSTT ESSSAPAPTP SSSTTESSSA
PVTSSTTESS SAPVPTPSSS TTESSSTPVT SSTTESSSAP VPTPSSSTTE SSSAPVPTPS
SSTTESSSAP APTPSSSTTE SSSAPVTSST TESSSAPVPT PSSSTTESSS APVPTPSSST
TESSSAPVPT PSSSTTESSS APVTSSTTES SSAPVTSSTT ESSSAPVPTP SSSTTESSSA
PVPTPSSSTT ESSSAPVPTP SSSTTESSSA PVTSSTTESS SAPVPTPSSS TTESSSAPVP
TPSSSTTESS SAPVPTPSSS TTESSVAPVP TPSSSSNITS SAPSSTPFSS STESSSVPVP
TPSSSTTESS SAPVSSSTTE SSVAPVPTPS SSSNITSSAP SSIPFSSTTE SFSTGTTVTP
SSSKYPGSQT ETSVSSTTET TIVPTKTTTS VTTPSTTTIT TTVCSTGTNS AGETTSGCSP
KTVTTTVPTT TTTSVTTSST TTITTTVCST GTNSAGETTS GCSPKTITTT VPCSTSPSET
ASESTTTSPT TPVTTVVSTT VVTTEYSTST KPGGEITTTF VTKNIPTTYL TTIAPTPSVT
TVTNFTPTTI TTTVCSTGTN SAGETTSGCS PKTVTTTVPC STGTGEYTTE ATTLVTTAVT
TTVVTTESST GTNSAGKTTT GYTTKSVPTT YVTTLAPSAP VTPATNAVPT TITTTECSAA
TNAAGETTSV CSAKTIVSSA SAGENTAPSA TTPVTTAIPT TVITTESSVG TNSAGETTTG
YTTKSIPTTY ITTLIPGSNG AKNYETVATA TNPISIKTTS QLATTASASS VAPVVTSPSL
TGPLQSASGS AVATYSVPSI SSTYQGAANI KVLGNFMWLL LALPVVF


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22152S RPR carbon 5 ml Method: Flocculation Agglutination (Latex) Kits 5 ml x 10
22172 VDRL Method: Flocculation Agglutination (Latex) Kits 1500 t
EIAAB14689 Fc receptor homolog expressed in B cells protein 2,Fc receptor-like and mucin-like protein 2,Fc receptor-like B,Fc receptor-like protein 2,Fc receptor-related protein Y,Fcrl2,Fcrlb,Fcrlm2,FcRY,Fcry,Fr
EIAAB14690 Fc receptor homolog expressed in B cells protein 2,Fc receptor-like and mucin-like protein 2,Fc receptor-like B,Fc receptor-like protein 2,Fc receptor-related protein Y,FCRL2,FCRLB,FCRLM2,FcRY,FCRY,FR
EIAAB29917 Castration-induced prostatic apoptosis-related protein 1,Cipar1,CIPAR-1,Parm1,PARM-1,Prostate androgen-regulated mucin-like protein 1 homolog,Prostatic androgen-repressed message 1 protein,Rat,Rattus
22152 RPR carbon 150t Method: Flocculation Agglutination (Latex) Kits 150 t


 

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