ID FLO11_YEAST Reviewed; 1367 AA. AC P08640; D6VVV0; P08068; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 2. DT 27-MAR-2024, entry version 178. DE RecName: Full=Flocculation protein FLO11; DE Short=Flo11p; DE Short=Flocculin-11; DE AltName: Full=Mucin-like protein 1; DE Flags: Precursor; GN Name=FLO11 {ECO:0000303|PubMed:16043420, ECO:0000312|SGD:S000001458}; GN Synonyms=MAL5, MUC1 {ECO:0000303|PubMed:8710886}, S1, S2; GN OrderedLocusNames=YIR019C {ECO:0000312|SGD:S000001458}; 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=9169870; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(1997). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242 AND 762-1331. RX PubMed=3106330; DOI=10.1128/jb.169.5.2142-2149.1987; RA Yamashita I., Nakamura M., Fukui S.; RT "Gene fusion is a possible mechanism underlying the evolution of STA1."; RL J. Bacteriol. 169:2142-2149(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31. RC STRAIN=SPX101-1C; RX PubMed=3141213; DOI=10.1016/0014-5793(88)80912-8; RA Pardo J.M., Ianez E., Zalacain M., Claros M.G., Jimenez A.; RT "Similar short elements in the 5' regions of the STA2 and SGA genes from RT Saccharomyces cerevisiae."; RL FEBS Lett. 239:179-184(1988). RN [5] RP FUNCTION. RX PubMed=8955395; DOI=10.1128/jb.178.24.7144-7151.1996; RA Lo W.S., Dranginis A.M.; RT "FLO11, a yeast gene related to the STA genes, encodes a novel cell surface RT flocculin."; RL J. Bacteriol. 178:7144-7151(1996). RN [6] RP FUNCTION. RX PubMed=8710886; DOI=10.1073/pnas.93.16.8419; RA Lambrechts M.G., Bauer F.F., Marmur J., Pretorius I.S.; RT "Muc1, a mucin-like protein that is regulated by Mss10, is critical for RT pseudohyphal differentiation in yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 93:8419-8424(1996). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=10383953; DOI=10.1128/jb.181.13.3886-3889.1999; RA Hamada K., Terashima H., Arisawa M., Yabuki N., Kitada K.; RT "Amino acid residues in the omega-minus region participate in cellular RT localization of yeast glycosylphosphatidylinositol-attached proteins."; RL J. Bacteriol. 181:3886-3889(1999). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. 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 [9] RP FUNCTION. RC STRAIN=Sigma 1278B; RX PubMed=11157168; DOI=10.1126/science.291.5505.878; RA Reynolds T.B., Fink G.R.; RT "Bakers' yeast, a model for fungal biofilm formation."; RL Science 291:878-881(2001). RN [10] RP FUNCTION. RX PubMed=16043420; DOI=10.1016/j.femsyr.2005.05.004; RA Bayly J.C., Douglas L.M., Pretorius I.S., Bauer F.F., Dranginis A.M.; RT "Characteristics of Flo11-dependent flocculation in Saccharomyces RT cerevisiae."; RL FEMS Yeast Res. 5:1151-1156(2005). RN [11] 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). RN [12] RP FUNCTION, AND GLYCOSYLATION. RX PubMed=17921350; DOI=10.1128/ec.00284-06; RA Douglas L.M., Li L., Yang Y., Dranginis A.M.; RT "Expression and characterization of the flocculin Flo11/Muc1, a RT Saccharomyces cerevisiae mannoprotein with homotypic properties of RT adhesion."; RL Eukaryot. Cell 6:2214-2221(2007). RN [13] RP FUNCTION. RC STRAIN=Sigma 1278B; RX PubMed=18001350; DOI=10.1111/j.1365-2958.2007.06014.x; RA Fichtner L., Schulze F., Braus G.H.; RT "Differential Flo8p-dependent regulation of FLO1 and FLO11 for cell-cell RT and cell-substrate adherence of S.cerevisiae S288c."; RL Mol. Microbiol. 66:1276-1289(2007). RN [14] RP FUNCTION, SUBCELLULAR LOCATION, SHEDDING, AND MUTAGENESIS OF RP 1340-ILE--PHE-1367. RX PubMed=20619652; DOI=10.1016/j.cub.2010.06.033; RA Karunanithi S., Vadaie N., Chavel C.A., Birkaya B., Joshi J., Grell L., RA Cullen P.J.; RT "Shedding of the mucin-like flocculin Flo11p reveals a new aspect of fungal RT adhesion regulation."; RL Curr. Biol. 20:1389-1395(2010). RN [15] RP FUNCTION, DOMAIN, AND GLYCOSYLATION. RX PubMed=22129043; DOI=10.1111/j.1567-1364.2011.00766.x; RA Goossens K.V., Willaert R.G.; RT "The N-terminal domain of the Flo11 protein from Saccharomyces cerevisiae RT is an adhesin without mannose-binding activity."; RL FEMS Yeast Res. 12:78-87(2012). RN [16] RP FUNCTION. RX PubMed=27547826; DOI=10.1128/msphere.00129-16; RA Barua S., Li L., Lipke P.N., Dranginis A.M.; RT "Molecular Basis for Strain Variation in the Saccharomyces cerevisiae RT Adhesin Flo11p."; RL MSphere 1:e00129-e00129(2016). RN [17] RP FUNCTION, DOMAIN, AND MUTAGENESIS OF TYR-111; TYR-113; TYR-118; TYR-133; RP TRP-144 AND TYR-196. 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). RN [18] RP X-RAY CRYSTALLOGRAPHY (0.89 ANGSTROMS) OF 22-211, FUNCTION, DOMAIN, RP MUTAGENESIS OF 31-SER--THR-213; TYR-111; TYR-113 AND TYR-118, AND DISULFIDE RP BONDS. RX PubMed=25960408; DOI=10.1016/j.str.2015.03.021; RA Kraushaar T., Brueckner S., Veelders M., Rhinow D., Schreiner F., Birke R., RA Pagenstecher A., Moesch H.U., Essen L.O.; RT "Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III- RT like Adhesin Domain Girdled by Aromatic Bands."; RL Structure 23:1005-1017(2015). 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) (PubMed:32286952, CC PubMed:25960408, PubMed:27547826, PubMed:17921350, PubMed:22129043). CC Plays a role in cell-substrate adhesion, haploid invasive growth, CC diploid pseudohyphae formation and biofilm (flor) development CC (PubMed:18001350, PubMed:11027318, PubMed:11157168, PubMed:16043420, CC PubMed:17921350, PubMed:20619652, PubMed:8710886, PubMed:8955395). CC Adhesive activity is inhibited by mannose, but not by glucose, maltose, CC sucrose or galactose (PubMed:16043420, PubMed:22129043). CC {ECO:0000269|PubMed:11027318, ECO:0000269|PubMed:11157168, CC ECO:0000269|PubMed:16043420, ECO:0000269|PubMed:17921350, CC ECO:0000269|PubMed:18001350, ECO:0000269|PubMed:20619652, CC ECO:0000269|PubMed:22129043, ECO:0000269|PubMed:25960408, CC ECO:0000269|PubMed:27547826, ECO:0000269|PubMed:32286952, CC ECO:0000269|PubMed:8710886, ECO:0000269|PubMed:8955395}. CC -!- INTERACTION: CC P08640; P08640: FLO11; NbExp=3; IntAct=EBI-2585, EBI-2585; CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10383953, CC ECO:0000269|PubMed:11027318, ECO:0000269|PubMed:20619652}. Membrane; CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:20619652}. Note=The CC protein is attached to the cell wall via a GPI-anchor and is also shed CC liberally into extracellular fluid; increased shedding is associated CC with biofilm mat expansion but decreased invasive growth. CC {ECO:0000269|PubMed:20619652}. 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 -!- 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, PubMed:25960408, PubMed:22129043). The CC hydrophobic bands are lined by stretches of acidic residues that may CC sensitise the protein to environmental pH (PubMed:25960408). The domain CC is required for biofilm formation (PubMed:25960408). The domain does CC not interact with mannose or calcium ions (PubMed:22129043, CC PubMed:25960408). {ECO:0000269|PubMed:22129043, CC ECO:0000269|PubMed:25960408, ECO:0000269|PubMed:32286952}. CC -!- PTM: Extensively O-mannosylated. {ECO:0000269|PubMed:17921350, CC ECO:0000269|PubMed:22129043}. 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 -!- PTM: A soluble form is probably produced by proteolytic cleavage at the CC cell surface (shedding). CC -!- MISCELLANEOUS: In the reference strain S288C, the transcriptional CC activator FLO8 contains an internal in-frame stop codon, leading to CC impaired FLO11 expression in this strain. CC {ECO:0000303|PubMed:18001350}. CC -!- SIMILARITY: Belongs to the flocculin family. Highly divergent. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z38061; CAA86176.1; -; Genomic_DNA. DR EMBL; M16164; AAA35014.1; -; Genomic_DNA. DR EMBL; M16165; AAA35015.1; -; Genomic_DNA. DR EMBL; X13857; CAA32069.1; -; Genomic_DNA. DR EMBL; BK006942; DAA08566.1; -; Genomic_DNA. DR PIR; S48478; S48478. DR RefSeq; NP_012284.3; NM_001179541.3. DR PDB; 4UYR; X-ray; 0.89 A; A=22-211. DR PDB; 4UYS; X-ray; 1.05 A; A=30-211. DR PDB; 4UYT; X-ray; 1.03 A; A=30-211. DR PDBsum; 4UYR; -. DR PDBsum; 4UYS; -. DR PDBsum; 4UYT; -. DR AlphaFoldDB; P08640; -. DR SMR; P08640; -. DR BioGRID; 35011; 116. DR DIP; DIP-7821N; -. DR IntAct; P08640; 2. DR MINT; P08640; -. DR STRING; 4932.YIR019C; -. DR GlyCosmos; P08640; 2 sites, No reported glycans. DR GlyGen; P08640; 2 sites. DR PaxDb; 4932-YIR019C; -. DR PeptideAtlas; P08640; -. DR EnsemblFungi; YIR019C_mRNA; YIR019C; YIR019C. DR GeneID; 854836; -. DR KEGG; sce:YIR019C; -. DR AGR; SGD:S000001458; -. DR SGD; S000001458; FLO11. DR VEuPathDB; FungiDB:YIR019C; -. DR eggNOG; ENOG502S1H2; Eukaryota. DR GeneTree; ENSGT00940000176775; -. DR HOGENOM; CLU_245303_0_0_1; -. DR InParanoid; P08640; -. DR OMA; ESMDSHD; -. DR OrthoDB; 2039984at2759; -. DR BioCyc; YEAST:G3O-31439-MONOMER; -. DR BioGRID-ORCS; 854836; 2 hits in 10 CRISPR screens. DR PRO; PR:P08640; -. DR Proteomes; UP000002311; Chromosome IX. DR RNAct; P08640; Protein. DR GO; GO:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0005576; C:extracellular region; IDA:SGD. DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD. DR GO; GO:0005886; C:plasma membrane; IDA:SGD. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0043709; P:cell adhesion involved in single-species biofilm formation; IMP:SGD. DR GO; GO:0098609; P:cell-cell adhesion; IMP:SGD. DR GO; GO:0097656; P:cell-cell self recognition; IDA:UniProtKB. DR GO; GO:0030447; P:filamentous growth; IDA:SGD. DR GO; GO:0000128; P:flocculation; IMP:SGD. DR GO; GO:0034109; P:homotypic cell-cell adhesion; IDA:UniProtKB. DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD. DR GO; GO:0007124; P:pseudohyphal growth; IMP:SGD. DR GO; GO:0090606; P:single-species surface biofilm formation; IMP:SGD. DR InterPro; IPR018789; Flo11. DR Pfam; PF10182; Flo11; 1. DR SMART; SM01213; Flo11; 1. DR PROSITE; PS51824; FLO11; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Cell wall; Disulfide bond; Glycoprotein; KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Repeat; Secreted; KW Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..1346 FT /note="Flocculation protein FLO11" FT /id="PRO_0000019586" FT PROPEP 1347..1367 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000019587" FT DOMAIN 31..207 FT /note="Flo11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01168" FT REPEAT 210..219 FT /note="1-1" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 220..229 FT /note="1-2" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 230..239 FT /note="1-3" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 240..249 FT /note="1-4" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 262..274 FT /note="2-1" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 275..287 FT /note="2-2" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 313..327 FT /note="3-1" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 328..342 FT /note="3-2" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 343..354 FT /note="4-1" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 355..369 FT /note="3-3" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 370..381 FT /note="4-2" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 382..393 FT /note="4-3" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 394..408 FT /note="3-4" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 409..420 FT /note="4-4" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 421..432 FT /note="4-5" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 433..444 FT /note="4-6" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 445..456 FT /note="4-7" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 457..471 FT /note="3-5" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 472..483 FT /note="4-8" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 484..498 FT /note="3-6" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 499..510 FT /note="4-9" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 511..525 FT /note="3-7" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 526..540 FT /note="3-8" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 541..552 FT /note="4-10" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 568..579 FT /note="4-11" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 580..594 FT /note="3-9" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 595..609 FT /note="3-10" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 610..624 FT /note="3-11" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 625..636 FT /note="4-12" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 637..651 FT /note="3-12" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 652..666 FT /note="3-13" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 667..681 FT /note="3-14" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 682..693 FT /note="4-13" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 694..705 FT /note="4-14" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 706..720 FT /note="3-15" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 721..735 FT /note="3-16" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 736..750 FT /note="3-17" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 751..762 FT /note="4-15" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 763..777 FT /note="3-18" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 778..792 FT /note="3-19" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 808..822 FT /note="3-21" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 838..852 FT /note="3-20" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 865..879 FT /note="3-22" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 937..968 FT /note="5-1" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 981..1012 FT /note="5-2" FT /evidence="ECO:0000269|PubMed:16086015" FT REPEAT 1088..1119 FT /note="5-3" FT /evidence="ECO:0000269|PubMed:16086015" FT REGION 209..975 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 210..249 FT /note="4 X 10 AA repeats, Ser/Thr-rich" FT REGION 262..287 FT /note="2 X 13 AA repeats, Thr-rich" FT REGION 313..852 FT /note="22 X 15 AA approximate repeats, Ser-rich" FT REGION 343..762 FT /note="15 X 12 AA repeats, Ser/Thr-rich" FT REGION 937..1119 FT /note="3 X 32 AA tandem repeats, Thr-rich" FT REGION 1008..1032 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..283 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 298..975 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 1346 FT /note="GPI-anchor amidated glycine" FT /evidence="ECO:0000255" FT CARBOHYD 817 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 874 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 37..201 FT /evidence="ECO:0000269|PubMed:25960408, FT ECO:0007744|PDB:4UYR, ECO:0007744|PDB:4UYS, FT ECO:0007744|PDB:4UYT" FT DISULFID 44..179 FT /evidence="ECO:0000269|PubMed:25960408, FT ECO:0007744|PDB:4UYR, ECO:0007744|PDB:4UYS, FT ECO:0007744|PDB:4UYT" FT DISULFID 141..205 FT /evidence="ECO:0000269|PubMed:25960408, FT ECO:0007744|PDB:4UYR, ECO:0007744|PDB:4UYS, FT ECO:0007744|PDB:4UYT" FT MUTAGEN 111 FT /note="Y->D: Disrupts homotypic domain interactions; when FT associated with D-113 and D-118." FT /evidence="ECO:0000269|PubMed:25960408, FT ECO:0000269|PubMed:32286952" FT MUTAGEN 113 FT /note="Y->D: Disrupts homotypic domain interactions; when FT associated with D-111 and D-118." FT /evidence="ECO:0000269|PubMed:25960408, FT ECO:0000269|PubMed:32286952" FT MUTAGEN 118 FT /note="Y->D: Disrupts homotypic domain interactions; when FT associated with D-111 and D-113." FT /evidence="ECO:0000269|PubMed:25960408, FT ECO:0000269|PubMed:32286952" FT MUTAGEN 133 FT /note="Y->D: Disrupts homotypic domain interactions; when FT associated with D-144 and D-196." FT /evidence="ECO:0000269|PubMed:32286952" FT MUTAGEN 144 FT /note="W->D: Disrupts homotypic domain interactions; when FT associated with D-133 and D-196." FT /evidence="ECO:0000269|PubMed:32286952" FT MUTAGEN 196 FT /note="Y->D: Disrupts homotypic domain interactions; when FT associated with D-133 and D-144." FT /evidence="ECO:0000269|PubMed:32286952" FT MUTAGEN 1340..1367 FT /note="Missing: Increased shedding, associated with loss of FT GPI-anchor site." FT /evidence="ECO:0000269|PubMed:20619652" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:4UYR" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:4UYR" FT TURN 55..57 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 61..72 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 75..86 FT /evidence="ECO:0007829|PDB:4UYR" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 93..100 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:4UYR" FT TURN 113..116 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 125..133 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 136..139 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 149..155 FT /evidence="ECO:0007829|PDB:4UYR" FT HELIX 157..165 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 171..177 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 186..192 FT /evidence="ECO:0007829|PDB:4UYR" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:4UYR" FT HELIX 199..201 FT /evidence="ECO:0007829|PDB:4UYR" SQ 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 //