FLO11_YEAST
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 03-AUG-2022, entry version 170.
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}.
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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 PaxDb; P08640; -.
DR PRIDE; P08640; -.
DR EnsemblFungi; YIR019C_mRNA; YIR019C; YIR019C.
DR GeneID; 854836; -.
DR KEGG; sce:YIR019C; -.
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; HSGSNYN; -.
DR BioCyc; YEAST:G3O-31439-MON; -.
DR PRO; PR:P08640; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P08640; protein.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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: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:0044011; P:single-species biofilm formation on inanimate substrate; 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
