FLO11_CLAL4
ID FLO11_CLAL4 Reviewed; 2164 AA.
AC C4XZ24;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Flocculation protein FLO11 {ECO:0000250|UniProtKB:P08640};
DE Short=Flo11p {ECO:0000250|UniProtKB:P08640};
DE Short=Flocculin-11 {ECO:0000250|UniProtKB:P08640};
DE AltName: Full=ClFLO11 {ECO:0000303|PubMed:32286952};
DE Flags: Precursor;
GN Name=FLO11 {ECO:0000303|PubMed:32286952};
GN ORFNames=CLUG_01197 {ECO:0000312|EMBL:EEQ37076.1};
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902 {ECO:0000312|Proteomes:UP000007703};
RN [1] {ECO:0000312|Proteomes:UP000007703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
RN [2] {ECO:0000305}
RP FUNCTION, AND DOMAIN.
RX PubMed=32286952; DOI=10.7554/elife.55587;
RA Brueckner S., Schubert R., Kraushaar T., Hartmann R., Hoffmann D.,
RA Jelli E., Drescher K., Mueller D.J., Oliver Essen L., Moesch H.U.;
RT "Kin discrimination in social yeast is mediated by cell surface receptors
RT of the Flo11 adhesin family.";
RL Elife 9:e55587-e55587(2020).
CC -!- FUNCTION: Homophilic binding protein that enables kin discrimination in
CC heterogeneous yeast populations by mediating homotypic cell-cell
CC interactions during flocculation, a reversible and asexual process in
CC which cells adhere to form aggregates (flocs).
CC {ECO:0000269|PubMed:32286952}.
CC -!- DOMAIN: The Flo11 domain contains aromatic residues that form two
CC hydrophobic bands on the surface of the protein that confer homophilic
CC binding (PubMed:32286952). The hydrophobic bands are lined by stretches
CC of acidic residues that may sensitise the protein to environmental pH
CC (By similarity). {ECO:0000250|UniProtKB:P08640,
CC ECO:0000269|PubMed:32286952}.
CC -!- SIMILARITY: Belongs to the flocculin family. Highly divergent.
CC {ECO:0000305}.
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DR EMBL; CH408076; EEQ37076.1; -; Genomic_DNA.
DR RefSeq; XP_002620040.1; XM_002619994.1.
DR AlphaFoldDB; C4XZ24; -.
DR SMR; C4XZ24; -.
DR EnsemblFungi; EEQ37076; EEQ37076; CLUG_01197.
DR GeneID; 8500672; -.
DR KEGG; clu:CLUG_01197; -.
DR VEuPathDB; FungiDB:CLUG_01197; -.
DR HOGENOM; CLU_231613_0_0_1; -.
DR InParanoid; C4XZ24; -.
DR OMA; IPTTYGA; -.
DR Proteomes; UP000007703; Unassembled WGS sequence.
DR GO; GO:0097656; P:cell-cell self recognition; IDA:UniProtKB.
DR GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:UniProtKB.
DR InterPro; IPR018789; Flo11.
DR InterPro; IPR025928; Flocculin_t3_rpt.
DR Pfam; PF10182; Flo11; 3.
DR Pfam; PF13928; Flocculin_t3; 4.
DR SMART; SM01213; Flo11; 3.
DR PROSITE; PS51824; FLO11; 3.
PE 3: Inferred from homology;
KW Cell adhesion; Disulfide bond; Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..2164
FT /note="Flocculation protein FLO11"
FT /evidence="ECO:0000255"
FT /id="PRO_5002946239"
FT DOMAIN 23..185
FT /note="Flo11 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01168"
FT DOMAIN 208..382
FT /note="Flo11 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01168"
FT DOMAIN 422..596
FT /note="Flo11 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01168"
FT REGION 196..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2091..2111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 1627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 221..567
FT /evidence="ECO:0000250|UniProtKB:P08640"
SQ SEQUENCE 2164 AA; 219717 MW; 34375F850FED067B CRC64;
MLRGFFTLLI FVAFTAATAV INACPNQKFT FHAQVVNFPQ ATITVTDPSD NGDGTWDVTI
NFNADATMSL KSLSELKILS LSKTYFLYSY NLKVDNINNP GSWSQRVTVT PRSVGDYKTC
MPQFTIQYDW CSAGVTDWSE CQNWKYQGSY DYITGCDNFD QSTGFSQKDA PDYCWDATLP
QSSSAVISSA APSSSAPVVP SAPATPNTPS SPSDPNTINA CPNQKFTFHA QVVNFPQATI
TVTDPSDNGD GTWDVTINFN AVATMSLKSL SELKILSLSK TYFLYSYNLK VDNINNPGSW
SQRVTVTPRS VGNYKTCMPQ FTIQFDWCSA GVTDQSECQN WKYQGSYDYI TGCDNFDQST
GFSQKDAPDY CWDVNVPSSS SAIVSSSAAP SSSSVPAAPS SSSVPVAPQS SSAPAVPSAP
ATPNTPTDPD TINACPNQKF TFHAQVVNFP QATITVTDPS DNGDGTWDVT INFNAVATMS
LKSLSELKIL SLSKTYFLYS YNLKVDNINN PGSWSQRVTV TPRSVGNYKT CMPQFTIQYD
WCSAGVTDWS ECQNWKYQGS YDYITGCDNF DQSTGFSQKD APDYCWNEPK SSSSQSSATY
LTPHNFDVTS GDFSVPASSS VVSSQASSSV VSSQASSSVV SSSSSEVTSE TPNDPQNRPP
PRTVGPEVST VTFSSDSASS AISSRTARLS SSAASSGLSS SEVSSSEVSS TLPSSDASST
EASSVVSSDA SSAITSEFHP HTLAPKFSLV SSYDFPPSSD SISTESSSQE SSVVSSTDGS
SVVSSTEVSS KASSTDGSSA ISSTEESSKV SSTDVSSSTE ESSVVSSTEA SSKVSSTEGS
SVVSSTEVSS KASSKISSRA SSTEGSSKVS STEVSSKVSS AEVSSTEVSS KVSSTEGSSA
VSSTEGSSVV SSDVSSKVSS TEVSSRASSK VSSKVSSTEE SSKVSSTEVS SKVSSTDGSS
VVSSTEVSSK DSSSTTSEFH PHTLAPKFSL ISSYDFPPSS DSISTESSSQ ESSVVSSTDG
SSVVSSTHGS SIVSSTEVSS KVSSTEGSSV VSSTEASSKV SSTEVSSKAS SKTSSRVSST
EGSSVVSSTE VSSTASSSTT SEFHPHTLAP KFSLISSYDF PPSSDSISTE SSSQESSVVS
STEGSSKVSS KVSSTDGSSV VSSTEGSSKV SSTEASSKAS STEGSSKVSS TEASSKASST
EGSSKVSSTE ASSKVSSTKA SSKVSSSKVS STEASVVSST EGSSKVSSTE RSSKVSSTDA
SSVVSSTDGS SVVVSSTETS SVAYPTDSSS VVSSTEASAT TSEFHPHTIA PKFSLITSDE
VSSTDGSSVV SSTEGSSKVS STEGSSKASS TEGSSKVSST EGSSKASSTE GSSVVSSTEG
SSKVSSTEAS SKVSSTKVSS TEASVVSSTE GSSKVSSTEA SVVSSTEASS VVSSTEASSV
ASSTEGSSVV SSTEGSSVVS STEASSVASS TEGSSVVSST EGSSVVSSTE ASSVVSSTEG
SSVVSSTEGS SKVSSTEASS VASSTEGSSV VSSTEASSVV SSTDDSSIVS STETTSTWPH
TIAPKFSLVT SSEPSTEQSS VASSTETSNS FTTTFPVDPR ILIESSTSST IFSSSETPIS
SFARYTNSSI VVSTPQPSEP AFSLPPPGQP VVPAFSSGSS FDASSSTNVD SSSASPSGSF
STDSSSGSLF VSSSDLTSSS TFSSASSTIA SSGSSPSPSV PGYSSTDGSS SGVPSGSIPA
VPFGASSTDG SSYSVPSGSS PAVPSGSSST DGSSYSVPSG SSPAVPSGSS STDGFSSVAS
ESSPADPTGS QYATTSVPSA SVTSDVSTSG FTSEQPTPSA PGTTTLTITS CDKSTCTTSY
KTTGITVRTT TIGSLVTKFT TYCPLTGVSS TPSPSEGVQT PTTGSPDVPS PSTTTITETT
CDETSCTTSY KTTGVTVITT TVGSIVTKYT TYCPLTGTSP SEPLNGVSTG VPHVPAPSTT
TITEVSCDDT TCATAYKTTG LTVVTTTIGS VVTEYTTYCP LSGTHSEVVE TVSTIAPTAS
APSTTTITET SCDESSCTTA YKTTGVTVIT TTINEMVTEY TTYCPLSGQS TATTPVGETS
TTPAGSKETT ISSVYHSGSP VSTESGVVSS PSSSPLITIA STSGGASNVR LSVASLLVLL
PLFI
