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 27-MAR-2024, entry version 187. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 290. DR ComplexPortal; CPX-1140; HICS complex. DR DIP; DIP-2472N; -. DR IntAct; P40073; 78. DR MINT; P40073; -. DR STRING; 4932.YER118C; -. DR GlyCosmos; P40073; 1 site, No reported glycans. DR GlyGen; P40073; 1 site. DR iPTMnet; P40073; -. DR PaxDb; 4932-YER118C; -. DR PeptideAtlas; P40073; -. DR EnsemblFungi; YER118C_mRNA; YER118C; YER118C. DR GeneID; 856854; -. DR KEGG; sce:YER118C; -. DR AGR; SGD:S000000920; -. DR SGD; S000000920; SHO1. DR VEuPathDB; FungiDB:YER118C; -. DR eggNOG; ENOG502QW7A; Eukaryota. DR HOGENOM; CLU_043316_0_0_1; -. DR InParanoid; P40073; -. DR OMA; KNGKWWQ; -. DR OrthoDB; 1365981at2759; -. DR BioCyc; YEAST:G3O-30282-MONOMER; -. DR BioGRID-ORCS; 856854; 1 hit in 10 CRISPR screens. 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:0043332; C:mating projection tip; IDA:SGD. DR GO; GO:0016020; C:membrane; NAS: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; NAS:ComplexPortal. DR GO; GO:0007231; P:osmosensory signaling pathway; IGI:SGD. DR GO; GO:0030833; P:regulation of actin filament polymerization; IBA:GO_Central. DR GO; GO:0001402; P:signal transduction involved in filamentous growth; IMP:SGD. DR CDD; cd11855; SH3_Sho1p; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR035522; Sho1_SH3. DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1. DR PANTHER; PTHR15735:SF20; PROTEIN NERVOUS WRECK; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 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 FT high-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 //