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Protein SLG1 (Cell wall integrity and stress response component 1) (Synthetic lethal with GAP protein 1)

 SLG1_YEAST              Reviewed;         378 AA.
P54867; D6W274;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 142.
RecName: Full=Protein SLG1;
AltName: Full=Cell wall integrity and stress response component 1;
AltName: Full=Synthetic lethal with GAP protein 1;
Flags: Precursor;
Name=SLG1; Synonyms=WSC1; OrderedLocusNames=YOR008C; ORFNames=UNF378;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
de Bettignies G., Bergez-Aullo P., Barthe C., Louvet O.,
Peypouquet M.-F., Morel C., Doignon F., Crouzet M.;
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8896276;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1091::AID-YEA22>3.3.CO;2-9;
Sterky F., Holmberg A., Pettersson B., Uhlen M.;
"The sequence of a 30 kb fragment on the left arm of chromosome XV
from Saccharomyces cerevisiae reveals 15 open reading frames, five of
which correspond to previously identified genes.";
Yeast 12:1091-1095(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
IDENTIFICATION.
PubMed=9613583; DOI=10.1007/s004380050717;
Jacoby J.J., Nilius S.M., Heinisch J.J.;
"A screen for upstream components of the yeast protein kinase C signal
transduction pathway identifies the product of the SLG1 gene.";
Mol. Gen. Genet. 258:148-155(1998).
[6]
FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, AND PHOSPHORYLATION.
PubMed=10430578;
Lodder A.L., Lee T.K., Ballester R.;
"Characterization of the Wsc1 protein, a putative receptor in the
stress response of Saccharomyces cerevisiae.";
Genetics 152:1487-1499(1999).
[7]
FUNCTION.
PubMed=10660075; DOI=10.1007/PL00008657;
Ivanovska I., Rose M.D.;
"SLG1 plays a role during G1 in the decision to enter or exit the cell
cycle.";
Mol. Gen. Genet. 262:1147-1156(2000).
[8]
FUNCTION.
PubMed=11113201; DOI=10.1128/MCB.21.1.271-280.2001;
Philip B., Levin D.E.;
"Wsc1 and Mid2 are cell surface sensors for cell wall integrity
signaling that act through Rom2, a guanine nucleotide exchange factor
for Rho1.";
Mol. Cell. Biol. 21:271-280(2001).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12399379;
Sekiya-Kawasaki M., Abe M., Saka A., Watanabe D., Kono K.,
Minemura-Asakawa M., Ishihara S., Watanabe T., Ohya Y.;
"Dissection of upstream regulatory components of the Rho1p effector,
1,3-beta-glucan synthase, in Saccharomyces cerevisiae.";
Genetics 162:663-676(2002).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
PHOSPHORYLATION, AND MUTAGENESIS OF SER-319; SER-320; SER-322 AND
SER-323.
PubMed=15470108; DOI=10.1099/mic.0.27264-0;
Vay H.A., Philip B., Levin D.E.;
"Mutational analysis of the cytoplasmic domain of the Wsc1 cell wall
stress sensor.";
Microbiology 150:3281-3288(2004).
[12]
FUNCTION.
PubMed=15484288; DOI=10.1002/yea.1155;
Gualtieri T., Ragni E., Mizzi L., Fascio U., Popolo L.;
"The cell wall sensor Wsc1p is involved in reorganization of actin
cytoskeleton in response to hypo-osmotic shock in Saccharomyces
cerevisiae.";
Yeast 21:1107-1120(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[14]
NULL MUTANT, DELETION MUTANTS, AND MUTAGENESIS OF TYR-303.
PubMed=17088254; DOI=10.1074/jbc.M604497200;
Serrano R., Martin H., Casamayor A., Arino J.;
"Signaling alkaline pH stress in the yeast Saccharomyces cerevisiae
through the Wsc1 cell surface sensor and the Slt2 MAPK pathway.";
J. Biol. Chem. 281:39785-39795(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Plays a role during G1 to regulate entering or exiting
the cell cycle. Involved in stress responses. Has a role in cell
wall integrity signaling. Activates ROM1 or ROM2 catalyzed guanine
nucleotide exchange toward RHO1. Important regulator of the actin
cytoskeleton rearrangements in conditions of cell wall expansion
and membrane stretching. Specifically required for the actin
reorganization induced by hypo-osmotic shock. Multicopy suppressor
of 1,3-beta-glucan synthase (GS). Activates GS upstream of RHO1.
Acts positively on the PKC1-MAPK pathway. Activates transiently
SLT2 during alkaline stress, which leads to an increase in the
expression of several specific genes.
{ECO:0000269|PubMed:10430578, ECO:0000269|PubMed:10660075,
ECO:0000269|PubMed:11113201, ECO:0000269|PubMed:12399379,
ECO:0000269|PubMed:15484288}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10430578};
Single-pass type I membrane protein {ECO:0000269|PubMed:10430578}.
-!- PTM: Glycosylated. Phosphorylated. Phosphorylation serves a
negative regulatory role. {ECO:0000269|PubMed:10430578,
ECO:0000269|PubMed:15470108}.
-!- DISRUPTION PHENOTYPE: Lack of SLG1 leads to a significant defect
of 1,3-beta-glucan synthesis and confers sensitivity to caffeine,
SDS, Calcofluor and alkaline pH stress. Deletion of residues 21-
256 results in non-functional protein, removal of residues 21-110
yields a protein still able to confer some tolerance to alkaline
stress, and deletion of residues 116-256 has no effect on the
function. {ECO:0000269|PubMed:12399379}.
-!- MISCELLANEOUS: Present with 664 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U39481; AAA85862.1; -; Genomic_DNA.
EMBL; U43491; AAC49488.1; -; Genomic_DNA.
EMBL; Z74916; CAA99196.1; -; Genomic_DNA.
EMBL; BK006948; DAA10790.1; -; Genomic_DNA.
PIR; S61992; S61992.
RefSeq; NP_014650.1; NM_001183427.1.
ProteinModelPortal; P54867; -.
BioGrid; 34412; 201.
DIP; DIP-4196N; -.
IntAct; P54867; 2.
MINT; MINT-496110; -.
STRING; 4932.YOR008C; -.
iPTMnet; P54867; -.
MaxQB; P54867; -.
PRIDE; P54867; -.
EnsemblFungi; YOR008C; YOR008C; YOR008C.
GeneID; 854170; -.
KEGG; sce:YOR008C; -.
EuPathDB; FungiDB:YOR008C; -.
SGD; S000005534; SLG1.
GeneTree; ENSGT00730000112583; -.
HOGENOM; HOG000000780; -.
InParanoid; P54867; -.
KO; K11244; -.
OMA; NPFDDSR; -.
OrthoDB; EOG092C5SG6; -.
BioCyc; YEAST:G3O-33558-MONOMER; -.
PRO; PR:P54867; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0004888; F:transmembrane signaling receptor activity; IGI:SGD.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
GO; GO:0030242; P:autophagy of peroxisome; IMP:SGD.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:SGD.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:SGD.
GO; GO:0009408; P:response to heat; IMP:SGD.
GO; GO:0006970; P:response to osmotic stress; IGI:SGD.
GO; GO:0007266; P:Rho protein signal transduction; IMP:SGD.
Gene3D; 1.20.5.100; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR002889; WSC_carb-bd.
Pfam; PF01822; WSC; 1.
SMART; SM00321; WSC; 1.
PROSITE; PS51212; WSC; 1.
1: Evidence at protein level;
Cell cycle; Cell membrane; Cell wall biogenesis/degradation;
Complete proteome; Glycoprotein; Membrane; Phosphoprotein;
Reference proteome; Signal; Stress response; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 378 Protein SLG1.
/FTId=PRO_0000041483.
TOPO_DOM 22 264 Extracellular. {ECO:0000255}.
TRANSMEM 265 285 Helical. {ECO:0000255}.
TOPO_DOM 286 378 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 110 WSC. {ECO:0000255|PROSITE-
ProRule:PRU00558}.
COMPBIAS 125 255 Thr-rich.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000244|PubMed:15665377,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 303 303 Y->A: Sensitive to alkali. Fails to
restore normal levels of SLT2
phosphorylation upon alkaline stress.
{ECO:0000269|PubMed:17088254}.
MUTAGEN 319 319 S->A: No phosphorylation; when associated
with A-320.
{ECO:0000269|PubMed:15470108}.
MUTAGEN 320 320 S->A: No phosphorylation; when associated
with A-319.
{ECO:0000269|PubMed:15470108}.
MUTAGEN 322 322 S->A: No phosphorylation; when associated
with A-323.
{ECO:0000269|PubMed:15470108}.
MUTAGEN 323 323 S->A: No phosphorylation; when associated
with A-322.
{ECO:0000269|PubMed:15470108}.
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


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