SHO1_YEAST
ID SHO1_YEAST Reviewed; 367 AA.
AC P40073; D3DM24;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=High osmolarity signaling protein SHO1;
DE AltName: Full=Osmosensor SHO1;
DE AltName: Full=Suppressor of SUA8-1 mutation;
DE AltName: Full=Synthetic high osmolarity-sensitive protein 1;
GN Name=SHO1; Synonyms=SSU81; OrderedLocusNames=YER118C;
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 Berroteran R.W., Hampsey M.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7624781; DOI=10.1126/science.7624781;
RA Maeda T., Takekawa M., Saito H.;
RT "Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-
RT containing osmosensor.";
RL Science 269:554-558(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 FUNCTION, AND INTERACTION WITH PBS2.
RX PubMed=9180081; DOI=10.1126/science.276.5319.1702;
RA Posas F., Saito H.;
RT "Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold
RT role of Pbs2p MAPKK.";
RL Science 276:1702-1705(1997).
RN [6]
RP FUNCTION.
RX PubMed=9744864; DOI=10.1101/gad.12.18.2874;
RA O'Rourke S.M., Herskowitz I.;
RT "The Hog1 MAPK prevents cross talk between the HOG and pheromone response
RT MAPK pathways in Saccharomyces cerevisiae.";
RL Genes Dev. 12:2874-2886(1998).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PBS2.
RX PubMed=10970855; DOI=10.1093/emboj/19.17.4623;
RA Raitt D.C., Posas F., Saito H.;
RT "Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent
RT activation of the Hog1 MAPK pathway.";
RL EMBO J. 19:4623-4631(2000).
RN [8]
RP FUNCTION.
RX PubMed=11084293; DOI=10.1016/s0891-5849(00)00432-9;
RA Singh K.K.;
RT "The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates
RT response to oxidative stress and in an oxidant-specific fashion.";
RL Free Radic. Biol. Med. 29:1043-1050(2000).
RN [9]
RP FUNCTION.
RX PubMed=10762242; DOI=10.1128/jb.182.9.2428-2437.2000;
RA Garcia-Rodriguez L.J., Duran A., Roncero C.;
RT "Calcofluor antifungal action depends on chitin and a functional high-
RT osmolarity glycerol response (HOG) pathway: evidence for a physiological
RT role of the Saccharomyces cerevisiae HOG pathway under noninducing
RT conditions.";
RL J. Bacteriol. 182:2428-2437(2000).
RN [10]
RP FUNCTION.
RX PubMed=10931333; DOI=10.1046/j.1365-2958.2000.02002.x;
RA Van Wuytswinkel O., Reiser V., Siderius M., Kelders M.C., Ammerer G.,
RA Ruis H., Mager W.H.;
RT "Response of Saccharomyces cerevisiae to severe osmotic stress: evidence
RT for a novel activation mechanism of the HOG MAP kinase pathway.";
RL Mol. Microbiol. 37:382-397(2000).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10980703; DOI=10.1038/35023568;
RA Reiser V., Salah S.M., Ammerer G.;
RT "Polarized localization of yeast Pbs2 depends on osmostress, the membrane
RT protein Sho1 and Cdc42.";
RL Nat. Cell Biol. 2:620-627(2000).
RN [12]
RP FUNCTION.
RX PubMed=11922108; DOI=10.1266/ggs.76.393;
RA Toh-e A., Oguchi T.;
RT "Defects in glycosylphosphatidylinositol (GPI) anchor synthesis activate
RT Hog1 kinase and confer copper-resistance in Saccharomyces cerevisisae.";
RL Genes Genet. Syst. 76:393-410(2001).
RN [13]
RP FUNCTION.
RX PubMed=12455951; DOI=10.1128/ec.1.2.163-173.2002;
RA Winkler A., Arkind C., Mattison C.P., Burkholder A., Knoche K., Ota I.M.;
RT "Heat stress activates the yeast high-osmolarity glycerol mitogen-activated
RT protein kinase pathway, and protein tyrosine phosphatases are essential
RT under heat stress.";
RL Eukaryot. Cell 1:163-173(2002).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=12374868; DOI=10.1073/pnas.172517799;
RA Bagnat M., Simons K.;
RT "Cell surface polarization during yeast mating.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14183-14188(2002).
RN [15]
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 [16]
RP DOMAIN, AND INTERACTION WITH PBS2.
RX PubMed=14668868; DOI=10.1038/nature02178;
RA Zarrinpar A., Park S.H., Lim W.A.;
RT "Optimization of specificity in a cellular protein interaction network by
RT negative selection.";
RL Nature 426:676-680(2003).
RN [17]
RP FUNCTION.
RX PubMed=12511654; DOI=10.1126/science.1076979;
RA Park S.H., Zarrinpar A., Lim W.A.;
RT "Rewiring MAP kinase pathways using alternative scaffold assembly
RT mechanisms.";
RL Science 299:1061-1064(2003).
RN [18]
RP FUNCTION, AND INTERACTION WITH MSB2.
RX PubMed=15256499; DOI=10.1101/gad.1178604;
RA Cullen P.J., Sabbagh W. Jr., Graham E., Irick M.M., van Olden E.K.,
RA Neal C., Delrow J., Bardwell L., Sprague G.F. Jr.;
RT "A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous
RT growth pathway in yeast.";
RL Genes Dev. 18:1695-1708(2004).
RN [19]
RP FUNCTION, AND INTERACTION WITH FUS1.
RX PubMed=15020407; DOI=10.1534/genetics.166.1.67;
RA Nelson B., Parsons A.B., Evangelista M., Schaefer K., Kennedy K.,
RA Ritchie S., Petryshen T.L., Boone C.;
RT "Fus1p interacts with components of the Hog1p mitogen-activated protein
RT kinase and Cdc42p morphogenesis signaling pathways to control cell fusion
RT during yeast mating.";
RL Genetics 166:67-77(2004).
RN [20]
RP FUNCTION.
RX PubMed=14595107; DOI=10.1091/mbc.e03-07-0521;
RA O'Rourke S.M., Herskowitz I.;
RT "Unique and redundant roles for HOG MAPK pathway components as revealed by
RT whole-genome expression analysis.";
RL Mol. Biol. Cell 15:532-542(2004).
RN [21]
RP FUNCTION, INTERACTION WITH PBS2, DOMAIN, AND MUTAGENESIS OF TYR-309;
RP ASP-317 AND TYR-355.
RX PubMed=15200958; DOI=10.1016/j.molcel.2004.05.024;
RA Marles J.A., Dahesh S., Haynes J., Andrews B.J., Davidson A.R.;
RT "Protein-protein interaction affinity plays a crucial role in controlling
RT the Sho1p-mediated signal transduction pathway in yeast.";
RL Mol. Cell 14:813-823(2004).
RN [22]
RP FUNCTION, AND INTERACTION WITH STE11.
RX PubMed=15200959; DOI=10.1016/j.molcel.2004.06.011;
RA Zarrinpar A., Bhattacharyya R.P., Nittler M.P., Lim W.A.;
RT "Sho1 and Pbs2 act as coscaffolds linking components in the yeast high
RT osmolarity MAP kinase pathway.";
RL Mol. Cell 14:825-832(2004).
RN [23]
RP IDENTIFICATION BY 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 [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STE11 AND STE50.
RX PubMed=16778768; DOI=10.1038/sj.emboj.7601192;
RA Tatebayashi K., Yamamoto K., Tanaka K., Tomida T., Maruoka T., Kasukawa E.,
RA Saito H.;
RT "Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory
RT HOG MAPK pathway.";
RL EMBO J. 25:3033-3044(2006).
RN [25]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [26]
RP PHOSPHORYLATION AT SER-166, MUTAGENESIS OF SER-166, AND SUBUNIT.
RX PubMed=17363249; DOI=10.1016/j.cub.2007.02.044;
RA Hao N., Behar M., Parnell S.C., Torres M.P., Borchers C.H., Elston T.C.,
RA Dohlman H.G.;
RT "A systems-biology analysis of feedback inhibition in the Sho1 osmotic-
RT stress-response pathway.";
RL Curr. Biol. 17:659-667(2007).
RN [27]
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 [28]
RP FUNCTION.
RX PubMed=18480263; DOI=10.1073/pnas.0710770105;
RA Hersen P., McClean M.N., Mahadevan L., Ramanathan S.;
RT "Signal processing by the HOG MAP kinase pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7165-7170(2008).
RN [29]
RP FUNCTION.
RX PubMed=19439450; DOI=10.1091/mbc.e08-07-0760;
RA Pitoniak A., Birkaya B., Dionne H.M., Vadaie N., Cullen P.J.;
RT "The signaling mucins Msb2 and Hkr1 differentially regulate the
RT filamentation mitogen-activated protein kinase pathway and contribute to a
RT multimodal response.";
RL Mol. Biol. Cell 20:3101-3114(2009).
RN [30]
RP FUNCTION.
RX PubMed=19318625; DOI=10.1126/scisignal.2000056;
RA Macia J., Regot S., Peeters T., Conde N., Sole R., Posas F.;
RT "Dynamic signaling in the Hog1 MAPK pathway relies on high basal signal
RT transduction.";
RL Sci. Signal. 2:RA13-RA13(2009).
RN [31]
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 [32]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 298-367.
RA Kursula P., Kursula I., Song Y.H., Paraskevopoulos M., Wilmanns M.;
RT "Structural genomics of yeast SH3 domains.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Plasma membrane osmosensor that activates the high osmolarity
CC glycerol (HOG) MAPK signaling pathway in response to high osmolarity.
CC Detects changes in external osmolarity and activates PBS2 through the
CC stimulation of STE11 and targets PBS2 to the plasma membrane. PBS2
CC activation leads to changes in glycerol production that helps to
CC balance the intracellular and external osmotic pressures. Activates
CC also HOG1 in response to heat stress and mediates resistance to
CC oxidative stress. Involved in the regulation of the mating pathway. May
CC be a receptor that feeds into the pseudohyphal growth pathway.
CC {ECO:0000269|PubMed:10762242, ECO:0000269|PubMed:10931333,
CC ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:10980703,
CC ECO:0000269|PubMed:11084293, ECO:0000269|PubMed:11922108,
CC ECO:0000269|PubMed:12455951, ECO:0000269|PubMed:12511654,
CC ECO:0000269|PubMed:14595107, ECO:0000269|PubMed:15020407,
CC ECO:0000269|PubMed:15200958, ECO:0000269|PubMed:15200959,
CC ECO:0000269|PubMed:15256499, ECO:0000269|PubMed:16778768,
CC ECO:0000269|PubMed:18480263, ECO:0000269|PubMed:19318625,
CC ECO:0000269|PubMed:19439450, ECO:0000269|PubMed:7624781,
CC ECO:0000269|PubMed:9180081, ECO:0000269|PubMed:9744864}.
CC -!- SUBUNIT: Forms homooligomers. Interacts (via the SH3 domain) with PBS2.
CC Interacts with FUS1, STE11, STE50 and RNA polymerase II.
CC {ECO:0000269|PubMed:10970855, ECO:0000269|PubMed:14668868,
CC ECO:0000269|PubMed:15020407, ECO:0000269|PubMed:15200958,
CC ECO:0000269|PubMed:15200959, ECO:0000269|PubMed:15256499,
CC ECO:0000269|PubMed:16778768, ECO:0000269|PubMed:17363249,
CC ECO:0000269|PubMed:9180081}.
CC -!- INTERACTION:
CC P40073; P42884: AAD14; NbExp=2; IntAct=EBI-18140, EBI-1994;
CC P40073; P36122: BCH2; NbExp=2; IntAct=EBI-18140, EBI-26374;
CC P40073; Q07533: CYK3; NbExp=4; IntAct=EBI-18140, EBI-31510;
CC P40073; P11710: FUS1; NbExp=7; IntAct=EBI-18140, EBI-7179;
CC P40073; P40036: GIP2; NbExp=2; IntAct=EBI-18140, EBI-7612;
CC P40073; Q05080: HOF1; NbExp=5; IntAct=EBI-18140, EBI-5412;
CC P40073; P53901: INN1; NbExp=4; IntAct=EBI-18140, EBI-28955;
CC P40073; Q12446: LAS17; NbExp=5; IntAct=EBI-18140, EBI-10022;
CC P40073; P53153: LCL3; NbExp=2; IntAct=EBI-18140, EBI-23857;
CC P40073; P21339: MSB1; NbExp=2; IntAct=EBI-18140, EBI-11322;
CC P40073; P08018: PBS2; NbExp=8; IntAct=EBI-18140, EBI-12972;
CC P40073; P39081: PCF11; NbExp=2; IntAct=EBI-18140, EBI-12980;
CC P40073; P39083: RGA1; NbExp=2; IntAct=EBI-18140, EBI-15044;
CC P40073; P23561: STE11; NbExp=3; IntAct=EBI-18140, EBI-18259;
CC P40073; P25344: STE50; NbExp=3; IntAct=EBI-18140, EBI-18305;
CC P40073; Q06412: TUS1; NbExp=3; IntAct=EBI-18140, EBI-37117;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Bud.
CC Bud neck. Cell projection. Note=Localizes at the tip of the mating
CC projection during conjugation.
CC -!- MISCELLANEOUS: Present with 2330 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SHO1 family. {ECO:0000305}.
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DR EMBL; U15653; AAA61904.1; -; Genomic_DNA.
DR EMBL; L41926; AAC41664.1; -; Genomic_DNA.
DR EMBL; U18916; AAC03216.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07778.1; -; Genomic_DNA.
DR PIR; S50621; S50621.
DR RefSeq; NP_011043.1; NM_001179008.1.
DR PDB; 2VKN; X-ray; 2.05 A; A=298-367.
DR PDBsum; 2VKN; -.
DR AlphaFoldDB; P40073; -.
DR SMR; P40073; -.
DR BioGRID; 36863; 287.
DR ComplexPortal; CPX-1140; HICS complex.
DR DIP; DIP-2472N; -.
DR IntAct; P40073; 78.
DR MINT; P40073; -.
DR STRING; 4932.YER118C; -.
DR iPTMnet; P40073; -.
DR PaxDb; P40073; -.
DR PRIDE; P40073; -.
DR EnsemblFungi; YER118C_mRNA; YER118C; YER118C.
DR GeneID; 856854; -.
DR KEGG; sce:YER118C; -.
DR SGD; S000000920; SHO1.
DR VEuPathDB; FungiDB:YER118C; -.
DR eggNOG; ENOG502QW7A; Eukaryota.
DR HOGENOM; CLU_043316_0_0_1; -.
DR InParanoid; P40073; -.
DR OMA; NGKWWQA; -.
DR BioCyc; YEAST:G3O-30282-MON; -.
DR EvolutionaryTrace; P40073; -.
DR PRO; PR:P40073; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40073; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0044697; C:HICS complex; IPI:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005078; F:MAP-kinase scaffold activity; IMP:SGD.
DR GO; GO:0005034; F:osmosensor activity; IPI:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IGI:SGD.
DR GO; GO:1902410; P:mitotic cytokinetic process; IC:ComplexPortal.
DR GO; GO:0007231; P:osmosensory signaling pathway; IGI:SGD.
DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD.
DR CDD; cd11855; SH3_Sho1p; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR039644; Sho1.
DR InterPro; IPR035522; Sho1_SH3.
DR PANTHER; PTHR15735:SF15; PTHR15735:SF15; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; SH3 domain; Stress response;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..367
FT /note="High osmolarity signaling protein SHO1"
FT /id="PRO_0000072231"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..65
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..93
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..122
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 144..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 300..361
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 252..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17363249"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 166
FT /note="S->E: Diminishes the formation of oligomers, dampens
FT activation of the HOG1 kinase, and impairs growth in high-
FT salt or sorbitol conditions."
FT /evidence="ECO:0000269|PubMed:17363249"
FT MUTAGEN 309
FT /note="Y->A: Decreases the interaction with PBS2 and leads
FT to decreased HOG pathway response and increased aberrant
FT mating pathway activation."
FT /evidence="ECO:0000269|PubMed:15200958"
FT MUTAGEN 317
FT /note="D->I,H: Decreases the interaction with PBS2 and
FT leads to decreased HOG pathway response and increased
FT aberrant mating pathway activation."
FT /evidence="ECO:0000269|PubMed:15200958"
FT MUTAGEN 355
FT /note="Y->A,F,I,M: Decreases the interaction with PBS2 and
FT leads to decreased HOG pathway response and increased
FT aberrant mating pathway activation."
FT /evidence="ECO:0000269|PubMed:15200958"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:2VKN"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:2VKN"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:2VKN"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:2VKN"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:2VKN"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:2VKN"
FT STRAND 356..363
FT /evidence="ECO:0007829|PDB:2VKN"
SQ SEQUENCE 367 AA; 41126 MW; E467A4D50AA3EDB6 CRC64;
MSISSKIRPT PRKPSRMATD HSFKMKKFYA DPFAISSISL AIVSWVIAIG GSISSASTNE
SFPRFTWWGI VYQFLIICSL MLFYCFDLVD HYRIFITTSI AVAFVYNTNS ATNLVYADGP
KKAAASAGVI LLSIINLIWI LYYGGDNASP TNRWIDSFSI KGIRPSPLEN SLHRARRRGN
RNTTPYQNNV YNDAIRDSGY ATQFDGYPQQ QPSHTNYVSS TALAGFENTQ PNTSEAVNLH
LNTLQQRINS ASNAKETNDN SNNQTNTNIG NTFDTDFSNG NTETTMGDTL GLYSDIGDDN
FIYKAKALYP YDADDDDAYE ISFEQNEILQ VSDIEGRWWK ARRANGETGI IPSNYVQLID
GPEEMHR
