FLO10_YEAST
ID FLO10_YEAST Reviewed; 1169 AA.
AC P36170; D6VXG3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Flocculation protein FLO10;
DE Short=Flocculin-10;
DE Flags: Precursor;
GN Name=FLO10; OrderedLocusNames=YKR102W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 FUNCTION.
RX PubMed=11027318; DOI=10.1073/pnas.220420397;
RA Guo B., Styles C.A., Feng Q., Fink G.R.;
RT "A Saccharomyces gene family involved in invasive growth, cell-cell
RT adhesion, and mating.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12158-12163(2000).
RN [5]
RP FUNCTION.
RX PubMed=15016375; DOI=10.1016/s0092-8674(04)00118-7;
RA Halme A., Bumgarner S., Styles C.A., Fink G.R.;
RT "Genetic and epigenetic regulation of the FLO gene family generates cell-
RT surface variation in yeast.";
RL Cell 116:405-415(2004).
RN [6]
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. Activity is
CC inhibited by mannose, glucose, maltose and sucrose. Also involved in
CC cell-substrate adhesion, haploid invasive growth and diploid
CC pseudohyphae formation. {ECO:0000269|PubMed:11027318,
CC ECO:0000269|PubMed:15016375}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
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). {ECO:0000250}.
CC -!- PTM: Extensively O-glycosylated. {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; Z28327; CAA82182.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09253.1; -; Genomic_DNA.
DR PIR; S38181; S38181.
DR RefSeq; NP_013028.1; NM_001179892.1.
DR AlphaFoldDB; P36170; -.
DR SMR; P36170; -.
DR BioGRID; 34233; 61.
DR STRING; 4932.YKR102W; -.
DR PaxDb; P36170; -.
DR EnsemblFungi; YKR102W_mRNA; YKR102W; YKR102W.
DR GeneID; 853977; -.
DR KEGG; sce:YKR102W; -.
DR SGD; S000001810; FLO10.
DR VEuPathDB; FungiDB:YKR102W; -.
DR eggNOG; ENOG502QPQC; Eukaryota.
DR GeneTree; ENSGT00940000176342; -.
DR HOGENOM; CLU_006076_0_0_1; -.
DR InParanoid; P36170; -.
DR OMA; CTETEST; -.
DR BioCyc; YEAST:G3O-32064-MON; -.
DR PRO; PR:P36170; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36170; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
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:0044182; P:filamentous growth of a population of unicellular organisms; IMP:SGD.
DR GO; GO:0000128; P:flocculation; IMP:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR InterPro; IPR025928; Flocculin_t3_rpt.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR Pfam; PF13928; Flocculin_t3; 2.
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..1146
FT /note="Flocculation protein FLO10"
FT /id="PRO_0000014336"
FT PROPEP 1147..1169
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000372449"
FT DOMAIN 111..271
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT REPEAT 303..326
FT /note="1-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 330..356
FT /note="1-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 357..383
FT /note="1-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 384..419
FT /note="2-1"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 420..446
FT /note="1-4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 447..482
FT /note="2-2"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 483..509
FT /note="1-5"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 510..545
FT /note="2-3"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 546..572
FT /note="1-6"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REPEAT 573..608
FT /note="2-4"
FT /evidence="ECO:0000269|PubMed:16086015"
FT REGION 303..572
FT /note="6 X 27 AA approximate repeats, Ser/Thr-rich"
FT REGION 384..608
FT /note="4 X 36 AA approximate repeats, Ser/Thr-rich"
FT REGION 798..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1146
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 686
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1092
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1099
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1169 AA; 122165 MW; 940C6DFB3569C669 CRC64;
MPVAARYIFL TGLFLLSVAN VALGTTEACL PAGEKKNGMT INFYQYSLKD SSTYSNPSYM
AYGYADAEKL GSVSGQTKLS IDYSIPCNGA SDTCACSDDD ATEYSASQVV PVKRGVKLCS
DNTTLSSKTE KRENDDCDQG AAYWSSDLFG FYTTPTNVTV EMTGYFLPPK TGTYTFGFAT
VDDSAILSVG GNVAFECCKQ EQPPITSTDF TINGIKPWNA DAPTDIKGST YMYAGYYYPI
KIVYSNAVSW GTLPVSVVLP DGTEVNDDFE GYVFSFDDNA TQAHCSVPNP AEHARTCVSS
ATSSWSSSEV CTECTETEST SYVTPYVTSS SWSSSEVCTE CTETESTSTS TPYVTSSSSS
SSEVCTECTE TESTSYVTPY VSSSTAAANY TSSFSSSSEV CTECTETEST STSTPYVTSS
SWSSSEVCTE CTETESTSYV TPYVSSSTAA ANYTSSFSSS SEVCTECTET ESTSTSTPYV
TSSSSSSSEV CTECTETEST SYVTPYVSSS TAAANYTSSF SSSSEVCTEC TETESTSTST
PYVTSSSWSS SEVCTECTET ESTSYVTPYV SSSTAAANYT SSFSSSSEVC TECTETESTS
TSTPYATSST GTATSFTAST SNTMTSLVQT DTTVSFSLSS TVSEHTNAPT SSVESNASTF
ISSNKGSVKS YVTSSIHSIT PMYPSNQTVT SSSVVSTPIT SESSESSASV TILPSTITSE
FKPSTMKTKV VSISSSPTNL ITSYDTTSKD STVGSSTSSV SLISSISLPS SYSASSEQIF
HSSIVSSNGQ ALTSFSSTKV SSSESSESHR TSPTTSSESG IKSSGVEIES TSTSSFSFHE
TSTASTSVQI SSQFVTPSSP ISTVAPRSTG LNSQTESTNS SKETMSSENS ASVMPSSSAT
SPKTGKVTSD ETSSGFSRDR TTVYRMTSET PSTNEQTTLI TVSSCESNSC SNTVSSAVVS
TATTTINGIT TEYTTWCPLS ATELTTVSKL ESEEKTTLIT VTSCESGVCS ETASPAIVST
ATATVNDVVT VYSTWSPQAT NKLAVSSDIE NSASKASFVS EAAETKSISR NNNFVPTSGT
TSIETHTTTT SNASENSDNV SASEAVSSKS VTNPVLISVS QQPRGTPASS MIGSSTASLE
MSSYLGIANH LLTNSGISIF IASLLLAIV
