FKS1_YEAST
ID FKS1_YEAST Reviewed; 1876 AA.
AC P38631; D6VYY0; Q53YZ4; Q6TKS9; Q6TKT0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=1,3-beta-glucan synthase component FKS1;
DE EC=2.4.1.34;
DE AltName: Full=1,3-beta-D-glucan-UDP glucosyltransferase;
DE AltName: Full=Calcineurin dependent protein 1;
DE AltName: Full=Calcofluor white hypersensitivity protein 53;
DE AltName: Full=Echinocandin target gene protein 1;
DE AltName: Full=FK506 sensitivity protein 1;
DE AltName: Full=Glucan synthase of cerevisiae protein 1;
DE AltName: Full=Papulacandin B resistance protein 1;
GN Name=FKS1; Synonyms=CND1, CWH53, ETG1, GLS1, GSC1, PBR1;
GN OrderedLocusNames=YLR342W; ORFNames=L8300.6;
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 [GENOMIC DNA], TOPOLOGY, AND DISRUPTION PHENOTYPE.
RC STRAIN=RC118D;
RX PubMed=7530227; DOI=10.1016/0378-1119(94)90633-5;
RA Eng W.-K., Faucette L., McLaughlin M.M., Cafferkey R., Koltin Y.,
RA Morris R.A., Young P.R., Johnson R.K., Livi G.P.;
RT "The yeast FKS1 gene encodes a novel membrane protein, mutations in which
RT confer FK506 and cyclosporin A hypersensitivity and calcineurin-dependent
RT growth.";
RL Gene 151:61-71(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, TOPOLOGY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=S288c / GRF88;
RX PubMed=7528927; DOI=10.1073/pnas.91.26.12907;
RA Douglas C.M., Foor F., Marrinan J.A., Morin N., Nielsen J.B., Dahl A.M.,
RA Mazur P., Baginsky W., Li W., El-Sherbeini M., Clemas J.A., Mandala S.M.,
RA Frommer B.R., Kurtz M.B.;
RT "The Saccharomyces cerevisiae FKS1 (ETG1) gene encodes an integral membrane
RT protein which is a subunit of 1,3-beta-D-glucan synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:12907-12911(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC STRAIN=ATCC 200589 / A451;
RX PubMed=7649185; DOI=10.1111/j.1432-1033.1995.tb20770.x;
RA Inoue S.B., Takewaki N., Takasuka T., Mio T., Adachi M., Fujii Y.,
RA Miyamoto C., Arisawa M., Furuichi Y., Watanabe T.;
RT "Characterization and gene cloning of 1,3-beta-D-glucan synthase from
RT Saccharomyces cerevisiae.";
RL Eur. J. Biochem. 231:845-854(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND GENE NAME.
RC STRAIN=S288c / GRF88;
RX PubMed=7828729; DOI=10.1016/0014-5793(94)01418-z;
RA Ram A.F.J., Brekelmans S.S.C., Oehlen L.J.W.M., Klis F.M.;
RT "Identification of two cell cycle regulated genes affecting the beta 1,3-
RT glucan content of cell walls in Saccharomyces cerevisiae.";
RL FEBS Lett. 358:165-170(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, ENZYME ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=S288c / GRF88;
RX PubMed=7592316; DOI=10.1128/jb.177.20.5732-5739.1995;
RA Castro C., Ribas J.C., Valdivieso M.H., Varona R., del Rey F., Duran A.;
RT "Papulacandin B resistance in budding and fission yeasts: isolation and
RT characterization of a gene involved in (1,3)beta-D-glucan synthesis in
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 177:5732-5739(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GENE NAME, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7542741; DOI=10.1128/mcb.15.8.4103;
RA Garrett-Engele P., Moilanen B., Cyert M.S.;
RT "Calcineurin, the Ca2+/calmodulin-dependent protein phosphatase, is
RT essential in yeast mutants with cell integrity defects and in mutants that
RT lack a functional vacuolar H(+)-ATPase.";
RL Mol. Cell. Biol. 15:4103-4114(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TOPOLOGY, MUTAGENESIS OF ASN-470 AND
RP LEU-642, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 96519 / YPH250;
RX PubMed=14693557; DOI=10.1128/aac.48.1.319-322.2004;
RA Ohyama T., Miyakoshi S., Isono F.;
RT "FKS1 mutations responsible for selective resistance of Saccharomyces
RT cerevisiae to the novel 1,3-beta-glucan synthase inhibitor arborcandin C.";
RL Antimicrob. Agents Chemother. 48:319-322(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [9]
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 [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=7510323; DOI=10.1099/00221287-139-12-2973;
RA Parent S.A., Nielsen J.B., Morin N., Chrebet G., Ramadan N., Dahl A.M.,
RA Hsu M.J., Bostian K.A., Foor F.;
RT "Calcineurin-dependent growth of an FK506- and CsA-hypersensitive mutant of
RT Saccharomyces cerevisiae.";
RL J. Gen. Microbiol. 139:2973-2984(1993).
RN [11]
RP INDUCTION.
RX PubMed=7565718; DOI=10.1128/mcb.15.10.5671;
RA Mazur P., Morin N., Baginsky W., el-Sherbeini M., Clemas J.A.,
RA Nielsen J.B., Foor F.;
RT "Differential expression and function of two homologous subunits of yeast
RT 1,3-beta-D-glucan synthase.";
RL Mol. Cell. Biol. 15:5671-5681(1995).
RN [12]
RP ENZYME ACTIVITY, AND INTERACTION WITH RHO1.
RX PubMed=8662910; DOI=10.1074/jbc.271.24.14604;
RA Mazur P., Baginsky W.;
RT "In vitro activity of 1,3-beta-D-glucan synthase requires the GTP-binding
RT protein Rho1.";
RL J. Biol. Chem. 271:14604-14609(1996).
RN [13]
RP INTERACTION WITH RHO1, AND SUBCELLULAR LOCATION.
RX PubMed=8602515; DOI=10.1126/science.272.5259.279;
RA Qadota H., Python C.P., Inoue S.B., Arisawa M., Anraku Y., Zheng Y.,
RA Watanabe T., Levin D.E., Ohya Y.;
RT "Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-
RT glucan synthase.";
RL Science 272:279-281(1996).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11856368; DOI=10.1046/j.1356-9597.2001.00495.x;
RA Utsugi T., Minemura M., Hirata A., Abe M., Watanabe D., Ohya Y.;
RT "Movement of yeast 1,3-beta-glucan synthase is essential for uniform cell
RT wall synthesis.";
RL Genes Cells 7:1-9(2002).
RN [15]
RP ENZYME ACTIVITY, AND MUTAGENESIS OF LYS-877; ALA-899 AND GLN-977.
RX PubMed=12399379; DOI=10.1093/genetics/162.2.663;
RA Sekiya-Kawasaki M., Abe M., Saka A., Watanabe D., Kono K.,
RA Minemura-Asakawa M., Ishihara S., Watanabe T., Ohya Y.;
RT "Dissection of upstream regulatory components of the Rho1p effector, 1,3-
RT beta-glucan synthase, in Saccharomyces cerevisiae.";
RL Genetics 162:663-676(2002).
RN [16]
RP ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-146; VAL-302;
RP TYR-329; TYR-335; THR-605; ILE-713; ILE-722; MET-761; ALA-823; THR-828;
RP ILE-853; LEU-855; LEU-872; LYS-877; ALA-899; GLU-907; ASP-920; ALA-932;
RP GLU-934; GLN-977; ASN-982; PHE-1020; ILE-1047; GLU-1111; PHE-1258 AND
RP ASN-1520.
RX PubMed=12185837; DOI=10.1002/yea.866;
RA Dijkgraaf G.J.P., Abe M., Ohya Y., Bussey H.;
RT "Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-
RT glucan in Saccharomyces cerevisiae.";
RL Yeast 19:671-690(2002).
RN [17]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-910, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [18]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [19]
RP CASPOFUNGIN HYPERSENSITIVITY.
RX PubMed=15166135; DOI=10.1534/genetics.167.1.35;
RA Lesage G., Sdicu A.-M., Menard P., Shapiro J., Hussein S., Bussey H.;
RT "Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a
RT synthetic interaction network and altered sensitivity to caspofungin.";
RL Genetics 167:35-49(2004).
RN [20]
RP DISRUPTION PHENOTYPE.
RX PubMed=17142567; DOI=10.1128/ec.00203-06;
RA Grabinska K.A., Magnelli P., Robbins P.W.;
RT "Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III
RT activity and chitin chain length.";
RL Eukaryot. Cell 6:328-336(2007).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-269 AND THR-272, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [23]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-259; LYS-275; LYS-386;
RP LYS-910; LYS-915; LYS-1539 AND LYS-1547, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Alternate catalytic subunit of the 1,3-beta-glucan synthase
CC (GS). Synthesizes 1,3-beta-glucan, a major structural component of the
CC yeast cell wall. Involved in cell wall synthesis, maintenance and cell
CC wall remodeling. {ECO:0000269|PubMed:11856368}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000269|PubMed:12185837, ECO:0000269|PubMed:12399379,
CC ECO:0000269|PubMed:7528927, ECO:0000269|PubMed:7592316,
CC ECO:0000269|PubMed:8662910};
CC -!- SUBUNIT: Component of the 1,3-beta-glucan synthase (GS), composed of
CC two alternate catalytic subunits FKS1 or GSC2, and a regulatory subunit
CC RHO1. Interacts with RHO1, which is a GTP-binding protein.
CC {ECO:0000269|PubMed:8602515, ECO:0000269|PubMed:8662910}.
CC -!- INTERACTION:
CC P38631; P06780: RHO1; NbExp=3; IntAct=EBI-7708, EBI-15121;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11856368,
CC ECO:0000269|PubMed:12185837, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:8602515}. Cell membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}. Note=Localizes to the sites of
CC polarized growth. Colocalizes with cortical actin patches and moves on
CC the cell surface at the sites of cell wall remodeling. Actin patch
CC motility is required for the movement. Early at the cell cycle,
CC localizes at the presumed bud site of the mother cell and at the tip of
CC the small bud. As the bud enlarges, appears as discernible spots in the
CC medium-sized bud and these spots colocalize with actin patches. Late in
CC the cell cycle, disappears in large budded cells, while the actin
CC patches disperse over the cell. During cytokinesis, is concentrated in
CC the neck, overlapping with the location of cortical actin patches.
CC -!- INDUCTION: During vegetative growth. Expressed periodically during the
CC cell cycle. {ECO:0000269|PubMed:7565718}.
CC -!- DISRUPTION PHENOTYPE: Cells are hypersensitive to immunosuppressant
CC drugs FK506 and cyclosporin A (CsA) due to the inhibition of
CC calcineurin phosphatase activity by the receptor-drug complexes and is
CC dependent on calcineurin for vegetative growth. It confers a slow
CC growth phenotype which is partially suppressed by exogenously added
CC Ca(2+) and exacerbated by EGTA. Simultaneous disruption of CNA1 and
CC CNA2 or CNB1 is lethal in FKS1-1. Disruption of FPR1 or CPR1 results in
CC the loss of hypersensitivity. Overexpression of CNA1 or CNA2, in
CC conjunction with CNB1, results in a significant decrease in
CC hypersensitivity to FK506 and CsA. FKS1-8 mutant is sensitive to FK506
CC and cyclosporin A, has increased tendency to lyse and exhibits slow
CC growth that is improved by the addition of osmotic stabilizing agents.
CC It is more sensitive to the drugs when grown on galactose compared to
CC dextrose. ETG1-1 mutant is resistant to the cell wall active
CC echinocandins, which are inhibitors of 1,3-beta-D-glucan synthase.
CC ETG1-4 mutant is hypersensitive to the chitin synthase inhibitor
CC nikkomycin Z. Deletion of FKS1 leads to hypersensitivity to
CC echinocandin-like antifungal lipopeptide caspofungin, a 1,3-beta-glucan
CC synthase inhibitor. Deletion mutant also displays a 30% reduction in
CC 1,3-beta-glucan and 15% reduction in alkali-insoluble 1,6-beta-glucan
CC compared to wild-type. Increases cellular chitin level
CC (PubMed:17142567). Increases chitin chain length (PubMed:17142567).
CC {ECO:0000269|PubMed:14693557, ECO:0000269|PubMed:17142567,
CC ECO:0000269|PubMed:7510323, ECO:0000269|PubMed:7528927,
CC ECO:0000269|PubMed:7530227, ECO:0000269|PubMed:7542741,
CC ECO:0000269|PubMed:7592316}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000305}.
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DR EMBL; U08459; AAC13763.1; -; Genomic_DNA.
DR EMBL; U12893; AAC48981.1; -; Genomic_DNA.
DR EMBL; D42126; BAA07706.1; -; Genomic_DNA.
DR EMBL; X80817; CAA56783.1; -; Genomic_DNA.
DR EMBL; Z46262; CAA86404.1; -; Genomic_DNA.
DR EMBL; L35923; AAA79760.1; -; Genomic_DNA.
DR EMBL; AY395693; AAR86935.1; -; Genomic_DNA.
DR EMBL; AY395694; AAR86936.1; -; Genomic_DNA.
DR EMBL; AY395695; AAR86937.1; -; Genomic_DNA.
DR EMBL; U19028; AAB67256.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09646.1; -; Genomic_DNA.
DR PIR; S50235; S50235.
DR RefSeq; NP_013446.1; NM_001182231.1.
DR AlphaFoldDB; P38631; -.
DR BioGRID; 31604; 537.
DR ComplexPortal; CPX-1812; 1,3-beta-D-glucan synthase complex, FKS1-RHO1 variant.
DR DIP; DIP-5749N; -.
DR IntAct; P38631; 68.
DR MINT; P38631; -.
DR STRING; 4932.YLR342W; -.
DR CAZy; GT48; Glycosyltransferase Family 48.
DR TCDB; 9.B.119.1.1; the glycan synthase, fks1 (fks1) family.
DR iPTMnet; P38631; -.
DR MaxQB; P38631; -.
DR PaxDb; P38631; -.
DR PRIDE; P38631; -.
DR EnsemblFungi; YLR342W_mRNA; YLR342W; YLR342W.
DR GeneID; 851055; -.
DR KEGG; sce:YLR342W; -.
DR SGD; S000004334; FKS1.
DR VEuPathDB; FungiDB:YLR342W; -.
DR eggNOG; KOG0916; Eukaryota.
DR GeneTree; ENSGT00940000176776; -.
DR HOGENOM; CLU_000844_0_1_1; -.
DR InParanoid; P38631; -.
DR OMA; IFVVAYM; -.
DR BioCyc; YEAST:YLR342W-MON; -.
DR PRO; PR:P38631; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P38631; protein.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IDA:SGD.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IDA:SGD.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IDA:SGD.
DR GO; GO:0030476; P:ascospore wall assembly; IC:ComplexPortal.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IC:ComplexPortal.
DR GO; GO:0051278; P:fungal-type cell wall polysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0008361; P:regulation of cell size; IMP:SGD.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
DR SMART; SM01205; FKS1_dom1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Glycosyltransferase; Isopeptide bond; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT CHAIN 1..1876
FT /note="1,3-beta-glucan synthase component FKS1"
FT /id="PRO_0000121725"
FT TOPO_DOM 1..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..563
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..678
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 700..1358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1359..1379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1380..1444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1445..1465
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1466..1469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1470..1490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1491..1560
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1561..1581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1582..1601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1602..1622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1623..1643
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1644..1664
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1665..1672
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1673..1695
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1696..1802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1803..1823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1824..1876
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 272
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 275
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 386
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 910
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 915
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 1539
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 1547
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 146
FT /note="E->V: In 1132; temperature-sensitive mutant; no
FT gross alteration in beta-glucan content of cells; when
FT associated with N-329; N-335 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 302
FT /note="V->N: In 1082; temperature-sensitive mutant; no
FT gross alteration in beta-glucan content of cells; when
FT associated with DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 329
FT /note="Y->N: In 1132; temperature-sensitive mutant; no
FT gross alteration in beta-glucan content of cells; when
FT associated with V-146; N-335 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 335
FT /note="Y->N: In 1132; temperature-sensitive mutant; no
FT gross alteration in beta-glucan content of cells; when
FT associated with V-146; N-329 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 470
FT /note="N->K: In ACR79-5; selectively resistant to
FT antibiotic arborcandin C."
FT /evidence="ECO:0000269|PubMed:14693557"
FT MUTAGEN 605
FT /note="T->I: In 1093; temperature-sensitive mutant; higher
FT beta-glucan content of cells; when associated with T-761
FT and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 642
FT /note="L->S: In ACR1A3; selectively resistant to antibiotic
FT arborcandin C."
FT /evidence="ECO:0000269|PubMed:14693557"
FT MUTAGEN 713
FT /note="I->L: In 1163; temperature-sensitive mutant; no
FT gross alteration in beta-glucan content of cells; when
FT associated with V-722 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 722
FT /note="I->V: In 1163; temperature-sensitive mutant; no
FT gross alteration in beta-glucan content of cells; when
FT associated with L-713 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 761
FT /note="M->T: In 1093; temperature-sensitive mutant; higher
FT beta-glucan content of cells; when associated with I-605
FT and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 823
FT /note="A->V: In 1104; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with E-920
FT and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 828
FT /note="T->A: In 1014; temperature-sensitive mutant; no
FT gross alteration in beta-glucan content of cells; partially
FT K1 killer toxin-sensitive; when associated with DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 853
FT /note="I->T: In 1114; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with G-932;
FT D-934; Y-1020; N-1047 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 855
FT /note="L->R: In A6; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with DEL-
FT GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 872
FT /note="L->F: In 1144; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with K-907;
FT S-982 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 877
FT /note="K->N: In 1154; temperature-sensitive mutant which is
FT able to grow at 25 degrees Celsius but fails to grow at
FT temperatures above 35 degrees Celsius; defective in 1,3-
FT beta-glucan synthesis and thus has lower beta-glucan
FT content; hypersensitive to echinocandin B and to a chitin-
FT binding reagent, Calcofluor white; fails to grow in a low
FT glucose medium; when associated with S-899; P-977 and DEL-
FT GSC2."
FT /evidence="ECO:0000269|PubMed:12185837,
FT ECO:0000269|PubMed:12399379"
FT MUTAGEN 899
FT /note="A->S: In 1154; temperature-sensitive mutant which is
FT able to grow at 25 degrees Celsius but fails to grow at
FT temperatures above 35 degrees Celsius; defective in 1,3-
FT beta-glucan synthesis and thus has lower beta-glucan
FT content; hypersensitive to echinocandin B and to a chitin-
FT binding reagent, Calcofluor white; fails to grow in a low
FT glucose medium; when associated with N-877; P-977 and DEL-
FT GSC2."
FT /evidence="ECO:0000269|PubMed:12185837,
FT ECO:0000269|PubMed:12399379"
FT MUTAGEN 907
FT /note="E->K: In 1144; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with F-872;
FT S-982 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 920
FT /note="D->E: In 1104; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with V-823
FT and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 932
FT /note="A->G: In 1114; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with T-853;
FT D-934; Y-1020; N-1047 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 934
FT /note="E->D: In 1114; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with T-853;
FT G-932; Y-1020; N-1047 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 977
FT /note="Q->P: In 1154; temperature-sensitive mutant which is
FT able to grow at 25 degrees Celsius but fails to grow at
FT temperatures above 35 degrees Celsius; defective in 1,3-
FT beta-glucan synthesis and thus has lower beta-glucan
FT content; hypersensitive to echinocandin B and to a chitin-
FT binding reagent, Calcofluor white; fails to grow in a low
FT glucose medium; when associated with N-877; S-899 and DEL-
FT GSC2."
FT /evidence="ECO:0000269|PubMed:12185837,
FT ECO:0000269|PubMed:12399379"
FT MUTAGEN 982
FT /note="N->S: In 1144; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with F-872;
FT K-907 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 1020
FT /note="F->Y: In 1114; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with T-853;
FT G-932; D-934; N-1047 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 1047
FT /note="I->N: In 1114; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with T-853;
FT G-932; D-934; Y-1020 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 1111
FT /note="E->G: In F4; temperature-sensitive mutant; lower
FT beta-glucan content of cells; when associated with DEL-
FT GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 1258
FT /note="F->Y: In 1125; temperature-sensitive mutant; lower
FT beta-glucan content of cells and partially K1 killer toxin-
FT resistant; when associated with D-1520 and DEL-GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT MUTAGEN 1520
FT /note="N->D: In 1125; temperature-sensitive mutant; lower
FT beta-glucan content of cells and partial K1 killer toxin-
FT resistant phenotype; when associated with Y-1258 and DEL-
FT GSC2."
FT /evidence="ECO:0000269|PubMed:12185837"
FT CONFLICT 19
FT /note="G -> D (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="A -> P (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="I -> V (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="V -> I (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="K -> T (in Ref. 1; AAC13763)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="N -> K (in Ref. 7; AAR86936)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="K -> R (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="L -> S (in Ref. 7; AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1341
FT /note="V -> F (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1457
FT /note="M -> I (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1790
FT /note="T -> S (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1827..1828
FT /note="KH -> DQ (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1834
FT /note="D -> T (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1844
FT /note="I -> V (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
FT CONFLICT 1853
FT /note="S -> F (in Ref. 1; AAC13763, 6; AAA79760 and 7;
FT AAR86935/AAR86936/AAR86937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1876 AA; 214851 MW; AD4B4CB8CB28B5D8 CRC64;
MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA GTEADMYGQQ
PPNESYDQDY TNGEYYGQPP NMAAQDGENF SDFSSYGPPG TPGYDSYGGQ YTASQMSYGE
PNSSGTSTPI YGNYDPNAIA MALPNEPYPA WTADSQSPVS IEQIEDIFID LTNRLGFQRD
SMRNMFDHFM VLLDSRSSRM SPDQALLSLH ADYIGGDTAN YKKWYFAAQL DMDDEIGFRN
MSLGKLSRKA RKAKKKNKKA MEEANPEDTE ETLNKIEGDN SLEAADFRWK AKMNQLSPLE
RVRHIALYLL CWGEANQVRF TAECLCFIYK CALDYLDSPL CQQRQEPMPE GDFLNRVITP
IYHFIRNQVY EIVDGRFVKR ERDHNKIVGY DDLNQLFWYP EGIAKIVLED GTKLIELPLE
ERYLRLGDVV WDDVFFKTYK ETRTWLHLVT NFNRIWVMHI SIFWMYFAYN SPTFYTHNYQ
QLVDNQPLAA YKWASCALGG TVASLIQIVA TLCEWSFVPR KWAGAQHLSR RFWFLCIIFG
INLGPIIFVF AYDKDTVYST AAHVVAAVMF FVAVATIIFF SIMPLGGLFT SYMKKSTRRY
VASQTFTAAF APLHGLDRWM SYLVWVTVFA AKYSESYYFL VLSLRDPIRI LSTTAMRCTG
EYWWGAVLCK VQPKIVLGLV IATDFILFFL DTYLWYIIVN TIFSVGKSFY LGISILTPWR
NIFTRLPKRI YSKILATTDM EIKYKPKVLI SQVWNAIIIS MYREHLLAID HVQKLLYHQV
PSEIEGKRTL RAPTFFVSQD DNNFETEFFP RDSEAERRIS FFAQSLSTPI PEPLPVDNMP
TFTVLTPHYA ERILLSLREI IREDDQFSRV TLLEYLKQLH PVEWECFVKD TKILAEETAA
YEGNENEAEK EDALKSQIDD LPFYCIGFKS AAPEYTLRTR IWASLRSQTL YRTISGFMNY
SRAIKLLYRV ENPEIVQMFG GNAEGLEREL EKMARRKFKF LVSMQRLAKF KPHELENAEF
LLRAYPDLQI AYLDEEPPLT EGEEPRIYSA LIDGHCEILD NGRRRPKFRV QLSGNPILGD
GKSDNQNHAL IFYRGEYIQL IDANQDNYLE ECLKIRSVLA EFEELNVEQV NPYAPGLRYE
EQTTNHPVAI VGAREYIFSE NSGVLGDVAA GKEQTFGTLF ARTLSQIGGK LHYGHPDFIN
ATFMTTRGGV SKAQKGLHLN EDIYAGMNAM LRGGRIKHCE YYQCGKGRDL GFGTILNFTT
KIGAGMGEQM LSREYYYLGT QLPVDRFLTF YYAHPGFHLN NLFIQLSLQM FMLTLVNLSS
LAHESIMCIY DRNKPKTDVL VPIGCYNFQP AVDWVRRYTL SIFIVFWIAF VPIVVQELIE
RGLWKATQRF FCHLLSLSPM FEVFAGQIYS SALLSDLAIG GARYISTGRG FATSRIPFSI
LYSRFAGSAI YMGARSMLML LFGTVAHWQA PLLWFWASLS SLIFAPFVFN PHQFAWEDFF
LDYRDYIRWL SRGNNQYHRN SWIGYVRMSR ARITGFKRKL VGDESEKAAG DASRAHRTNL
IMAEIIPCAI YAAGCFIAFT FINAQTGVKT TDDDRVNSVL RIIICTLAPI AVNLGVLFFC
MGMSCCSGPL FGMCCKKTGS VMAGIAHGVA VIVHIAFFIV MWVLESFNFV RMLIGVVTCI
QCQRLIFHCM TALMLTREFK NDHANTAFWT GKWYGKGMGY MAWTQPSREL TAKVIELSEF
AADFVLGHVI LICQLPLIII PKIDKFHSIM LFWLKPSRQI RPPIYSLKQT RLRKRMVKKY
CSLYFLVLAI FAGCIIGPAV ASAKIHKHIG DSLDGVVHNL FQPINTTNND TGSQMSTYQS
HYYTHTPSLK TWSTIK
