SLG1_YEAST
ID SLG1_YEAST Reviewed; 378 AA.
AC P54867; D6W274;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein SLG1;
DE AltName: Full=Cell wall integrity and stress response component 1;
DE AltName: Full=Synthetic lethal with GAP protein 1;
DE Flags: Precursor;
GN Name=SLG1; Synonyms=WSC1; OrderedLocusNames=YOR008C; ORFNames=UNF378;
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].
RA de Bettignies G., Bergez-Aullo P., Barthe C., Louvet O., Peypouquet M.-F.,
RA Morel C., Doignon F., Crouzet M.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP IDENTIFICATION.
RX PubMed=9613583; DOI=10.1007/s004380050717;
RA Jacoby J.J., Nilius S.M., Heinisch J.J.;
RT "A screen for upstream components of the yeast protein kinase C signal
RT transduction pathway identifies the product of the SLG1 gene.";
RL Mol. Gen. Genet. 258:148-155(1998).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND PHOSPHORYLATION.
RX PubMed=10430578; DOI=10.1093/genetics/152.4.1487;
RA Lodder A.L., Lee T.K., Ballester R.;
RT "Characterization of the Wsc1 protein, a putative receptor in the stress
RT response of Saccharomyces cerevisiae.";
RL Genetics 152:1487-1499(1999).
RN [7]
RP FUNCTION.
RX PubMed=10660075; DOI=10.1007/pl00008657;
RA Ivanovska I., Rose M.D.;
RT "SLG1 plays a role during G1 in the decision to enter or exit the cell
RT cycle.";
RL Mol. Gen. Genet. 262:1147-1156(2000).
RN [8]
RP FUNCTION.
RX PubMed=11113201; DOI=10.1128/mcb.21.1.271-280.2001;
RA Philip B., Levin D.E.;
RT "Wsc1 and Mid2 are cell surface sensors for cell wall integrity signaling
RT that act through Rom2, a guanine nucleotide exchange factor for Rho1.";
RL Mol. Cell. Biol. 21:271-280(2001).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-319; SER-320; SER-322 AND SER-323.
RX PubMed=15470108; DOI=10.1099/mic.0.27264-0;
RA Vay H.A., Philip B., Levin D.E.;
RT "Mutational analysis of the cytoplasmic domain of the Wsc1 cell wall stress
RT sensor.";
RL Microbiology 150:3281-3288(2004).
RN [12]
RP FUNCTION.
RX PubMed=15484288; DOI=10.1002/yea.1155;
RA Gualtieri T., Ragni E., Mizzi L., Fascio U., Popolo L.;
RT "The cell wall sensor Wsc1p is involved in reorganization of actin
RT cytoskeleton in response to hypo-osmotic shock in Saccharomyces
RT cerevisiae.";
RL Yeast 21:1107-1120(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [14]
RP NULL MUTANT, DELETION MUTANTS, AND MUTAGENESIS OF TYR-303.
RX PubMed=17088254; DOI=10.1074/jbc.m604497200;
RA Serrano R., Martin H., Casamayor A., Arino J.;
RT "Signaling alkaline pH stress in the yeast Saccharomyces cerevisiae through
RT the Wsc1 cell surface sensor and the Slt2 MAPK pathway.";
RL J. Biol. Chem. 281:39785-39795(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Plays a role during G1 to regulate entering or exiting the
CC cell cycle. Involved in stress responses. Has a role in cell wall
CC integrity signaling. Activates ROM1 or ROM2 catalyzed guanine
CC nucleotide exchange toward RHO1. Important regulator of the actin
CC cytoskeleton rearrangements in conditions of cell wall expansion and
CC membrane stretching. Specifically required for the actin reorganization
CC induced by hypo-osmotic shock. Multicopy suppressor of 1,3-beta-glucan
CC synthase (GS). Activates GS upstream of RHO1. Acts positively on the
CC PKC1-MAPK pathway. Activates transiently SLT2 during alkaline stress,
CC which leads to an increase in the expression of several specific genes.
CC {ECO:0000269|PubMed:10430578, ECO:0000269|PubMed:10660075,
CC ECO:0000269|PubMed:11113201, ECO:0000269|PubMed:12399379,
CC ECO:0000269|PubMed:15484288}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10430578};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:10430578}.
CC -!- PTM: Glycosylated. Phosphorylated. Phosphorylation serves a negative
CC regulatory role. {ECO:0000269|PubMed:10430578,
CC ECO:0000269|PubMed:15470108}.
CC -!- DISRUPTION PHENOTYPE: Lack of SLG1 leads to a significant defect of
CC 1,3-beta-glucan synthesis and confers sensitivity to caffeine, SDS,
CC Calcofluor and alkaline pH stress. Deletion of residues 21-256 results
CC in non-functional protein, removal of residues 21-110 yields a protein
CC still able to confer some tolerance to alkaline stress, and deletion of
CC residues 116-256 has no effect on the function.
CC {ECO:0000269|PubMed:12399379}.
CC -!- MISCELLANEOUS: Present with 664 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U39481; AAA85862.1; -; Genomic_DNA.
DR EMBL; U43491; AAC49488.1; -; Genomic_DNA.
DR EMBL; Z74916; CAA99196.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10790.1; -; Genomic_DNA.
DR PIR; S61992; S61992.
DR RefSeq; NP_014650.1; NM_001183427.1.
DR AlphaFoldDB; P54867; -.
DR SMR; P54867; -.
DR BioGRID; 34412; 229.
DR DIP; DIP-4196N; -.
DR IntAct; P54867; 2.
DR STRING; 4932.YOR008C; -.
DR iPTMnet; P54867; -.
DR MaxQB; P54867; -.
DR PaxDb; P54867; -.
DR PRIDE; P54867; -.
DR EnsemblFungi; YOR008C_mRNA; YOR008C; YOR008C.
DR GeneID; 854170; -.
DR KEGG; sce:YOR008C; -.
DR SGD; S000005534; SLG1.
DR VEuPathDB; FungiDB:YOR008C; -.
DR eggNOG; KOG4157; Eukaryota.
DR HOGENOM; CLU_024893_1_1_1; -.
DR InParanoid; P54867; -.
DR OMA; TTFHTEG; -.
DR BioCyc; YEAST:G3O-33558-MON; -.
DR PRO; PR:P54867; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P54867; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IGI:SGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
DR GO; GO:0009408; P:response to heat; IMP:SGD.
DR GO; GO:0006970; P:response to osmotic stress; IGI:SGD.
DR GO; GO:0007266; P:Rho protein signal transduction; IMP:SGD.
DR InterPro; IPR002889; WSC_carb-bd.
DR Pfam; PF01822; WSC; 1.
DR SMART; SM00321; WSC; 1.
DR PROSITE; PS51212; WSC; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell membrane; Cell wall biogenesis/degradation; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Stress response;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..378
FT /note="Protein SLG1"
FT /id="PRO_0000041483"
FT TOPO_DOM 22..264
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..110
FT /note="WSC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00558"
FT REGION 115..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 303
FT /note="Y->A: Sensitive to alkali. Fails to restore normal
FT levels of SLT2 phosphorylation upon alkaline stress."
FT /evidence="ECO:0000269|PubMed:17088254"
FT MUTAGEN 319
FT /note="S->A: No phosphorylation; when associated with A-
FT 320."
FT /evidence="ECO:0000269|PubMed:15470108"
FT MUTAGEN 320
FT /note="S->A: No phosphorylation; when associated with A-
FT 319."
FT /evidence="ECO:0000269|PubMed:15470108"
FT MUTAGEN 322
FT /note="S->A: No phosphorylation; when associated with A-
FT 323."
FT /evidence="ECO:0000269|PubMed:15470108"
FT MUTAGEN 323
FT /note="S->A: No phosphorylation; when associated with A-
FT 322."
FT /evidence="ECO:0000269|PubMed:15470108"
SQ SEQUENCE 378 AA; 39270 MW; EEE164F2374CCCE3 CRC64;
MRPNKTSLLL ALLSILSQAN AYEYVNCFSS LPSDFSKADS YNWQSSSHCN SECSAKGASY
FALYNHSECY CGDTNPSGSE STSSSCNTYC FGYSSEMCGG EDAYSVYQLD SDTNSNSISS
SDSSTESTSA SSSTTSSTTS STTSTTSSTT SSTTSSMASS STVQNSPEST QAAASISTSQ
SSSTVTSESS LTSDTLATSS TSSQSQDATS IIYSTTFHTE GGSTIFVTNT ITASAQNSGS
ATGTAGSDST SGSKTHKKKA NVGAIVGGVV GGVVGAVAIA LCILLIVRHI NMKREQDRME
KEYQEAIKPV EYPDKLYASS FSSNHGPSSG SFEEEHTKGQ TDINPFDDSR RISNGTFING
GPGGKNNVLT VVNPDEAD
