FLO11_KOMPG
ID FLO11_KOMPG Reviewed; 839 AA.
AC C4R2D7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=KpFLO11 {ECO:0000303|PubMed:32286952};
DE Flags: Precursor;
GN Name=FLO11 {ECO:0000303|PubMed:32286952};
GN OrderedLocusNames=PAS_chr2-2_0482 {ECO:0000312|EMBL:CAY69661.1};
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223 {ECO:0000312|Proteomes:UP000000314};
RN [1] {ECO:0000312|Proteomes:UP000000314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864 {ECO:0000312|Proteomes:UP000000314};
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
RN [2] {ECO:0007744|PDB:5FV5, ECO:0007744|PDB:5FV6}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 23-198, FUNCTION, DOMAIN, AND
RP DISULFIDE BONDS.
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; FN392320; CAY69661.1; -; Genomic_DNA.
DR RefSeq; XP_002491941.1; XM_002491896.1.
DR PDB; 5FV5; X-ray; 1.40 A; A=23-198.
DR PDB; 5FV6; X-ray; 2.00 A; A/B=23-198.
DR PDBsum; 5FV5; -.
DR PDBsum; 5FV6; -.
DR AlphaFoldDB; C4R2D7; -.
DR SMR; C4R2D7; -.
DR STRING; 644223.C4R2D7; -.
DR EnsemblFungi; CAY69661; CAY69661; PAS_chr2-2_0482.
DR GeneID; 8198658; -.
DR KEGG; ppa:PAS_chr2-2_0482; -.
DR eggNOG; ENOG502S1H2; Eukaryota.
DR HOGENOM; CLU_338918_0_0_1; -.
DR InParanoid; C4R2D7; -.
DR OMA; KSSADDC; -.
DR Proteomes; UP000000314; Chromosome 2.
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 Pfam; PF10182; Flo11; 2.
DR SMART; SM01213; Flo11; 2.
DR PROSITE; PS51824; FLO11; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Disulfide bond; Glycoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..839
FT /note="Flocculation protein FLO11"
FT /evidence="ECO:0000255"
FT /id="PRO_5002941026"
FT DOMAIN 24..194
FT /note="Flo11 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01168"
FT DOMAIN 332..502
FT /note="Flo11 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01168"
FT REGION 187..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..320
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..589
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 28..188
FT /evidence="ECO:0000269|PubMed:32286952,
FT ECO:0007744|PDB:5FV5, ECO:0007744|PDB:5FV6"
FT DISULFID 37..167
FT /evidence="ECO:0000269|PubMed:32286952,
FT ECO:0007744|PDB:5FV5, ECO:0007744|PDB:5FV6"
FT DISULFID 129..192
FT /evidence="ECO:0000269|PubMed:32286952,
FT ECO:0007744|PDB:5FV5, ECO:0007744|PDB:5FV6"
FT DISULFID 143..152
FT /evidence="ECO:0000269|PubMed:32286952,
FT ECO:0007744|PDB:5FV5, ECO:0007744|PDB:5FV6"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:5FV5"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:5FV5"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5FV5"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 113..124
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:5FV5"
FT TURN 150..154
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5FV6"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:5FV5"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:5FV5"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5FV5"
SQ SEQUENCE 839 AA; 91099 MW; C15E76E77A74341B CRC64;
MVSLRSIFTS SILAAGLTRA HGSSGKTCPT SEVSPACYAN QWETTFPPSD IKITGATWVQ
DNIYDVTLSY EAESLELENL TELKIIGLNS PTGGTKLVWS LNSKVYDIDN PAKWTTTLRV
YTKSSADDCY VEMYPFQIQV DWCEAGASTD GCSAWKWPKS YDYDIGCDNM QDGVSRKHHP
VYKWPKKCSS DCGVEPTTSD EPEEPTTSEE PVEPTSSDEE PTTSEEPTTS EEPEEPTTSD
EPEEPTTSEE PEEPTTSEEP EEPTTSEEPT TSEEPEEPTS SDEEPTTSDE PEEPTTSDEP
EEPTTSEEPT TSEEPEEPTT SSEEPTPSEE PEGPTCPTSE VSPACYADQW ETTFPPSDIK
ITGATWVEDN IYDVTLSYEA ESLELENLTE LKIIGLNSPT GGTKVVWSLN SGIYDIDNPA
KWTTTLRVYT KSSADDCYVE MYPFQIQVDW CEAGASTDGC SAWKWPKSYD YDIGCDNMQD
GVSRKHHPVY KWPKKCSSNC GVEPTTSDEP EEPTTSEEPE EPTTSEEPEE PTSSDEEPTT
SEEPEEPTTS DEPEEPTTSE EPEEPTTSEE PEEPTTSEEP EEPTTSDEEP GTTEEPLVPT
TKTETDVSTT LLTVTDCGTK TCTKSLVITG VTKETVTTHG KTTVITTYCP LPTETVTPTP
VTVTSTIYAD ESVTKTTVYT TGAVEKTVTV GGSSTVVVVH TPLTTAVVQS QSTDEIKTVV
TARPSTTTIV RDVCYNSVCS VATIVTGVTE KTITFSTGSI TVVPTYVPLV ESEEHQRTAS
TSETRATSVV VPTVVGQSSS ASATSSIFPS VTIHEGVANT VKNSMISGAV ALLFNALFL
