ID MSS11_YEAST Reviewed; 758 AA. AC Q03825; D6VZY6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 145. DE RecName: Full=Transcription activator MSS11; DE AltName: Full=Multicopy suppressor of STA genes protein 11; GN Name=MSS11; OrderedLocusNames=YMR164C; ORFNames=YM8520.13C; 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], AND FUNCTION. RX PubMed=9342405; DOI=10.1007/s002940050275; RA Webber A.L., Lambrechts M.G., Pretorius I.S.; RT "MSS11, a novel yeast gene involved in the regulation of starch RT metabolism."; RL Curr. Genet. 32:260-266(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169872; RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; RL Nature 387:90-93(1997). RN [3] 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 [4] RP FUNCTION. RX PubMed=9832522; DOI=10.1093/genetics/150.4.1443; RA Lorenz M.C., Heitman J.; RT "Regulators of pseudohyphal differentiation in Saccharomyces cerevisiae RT identified through multicopy suppressor analysis in ammonium permease RT mutant strains."; RL Genetics 150:1443-1457(1998). RN [5] RP FUNCTION. RX PubMed=10515942; DOI=10.1128/jb.181.20.6497-6508.1999; RA Gagiano M., van Dyk D., Bauer F.F., Lambrechts M.G., Pretorius I.S.; RT "Divergent regulation of the evolutionarily closely related promoters of RT the Saccharomyces cerevisiae STA2 and MUC1 genes."; RL J. Bacteriol. 181:6497-6508(1999). RN [6] RP FUNCTION. RX PubMed=9987114; DOI=10.1046/j.1365-2958.1999.01151.x; RA Gagiano M., van Dyk D., Bauer F.F., Lambrechts M.G., Pretorius I.S.; RT "Msn1p/Mss10p, Mss11p and Muc1p/Flo11p are part of a signal transduction RT pathway downstream of Mep2p regulating invasive growth and pseudohyphal RT differentiation in Saccharomyces cerevisiae."; RL Mol. Microbiol. 31:103-116(1999). RN [7] RP FUNCTION. RX PubMed=14523573; DOI=10.1007/s00294-003-0447-7; RA Kim T.S., Ahn J.Y., Yoon J.H., Kang H.S.; RT "STA10 repression of STA gene expression is caused by a defective RT activator, flo8, in Saccharomyces cerevisiae."; RL Curr. Genet. 44:261-267(2003). RN [8] RP FUNCTION, AND MUTAGENESIS OF 133-PHE-LEU-134; 137-TRP-TRP-138; RP 140-ILE-PHE-141 AND 144-LEU-PHE-145. RX PubMed=12492858; DOI=10.1046/j.1365-2958.2003.03247.x; RA Gagiano M., Bester M.C., van Dyk D., Franken J., Bauer F.F., RA Pretorius I.S.; RT "Mss11p is a transcription factor regulating pseudohyphal differentiation, RT invasive growth and starch metabolism in Saccharomyces cerevisiae in RT response to nutrient availability."; RL Mol. Microbiol. 47:119-134(2003). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [10] RP FUNCTION, DNA-BINDING, AND INTERACTION WITH FLO8; STE12 AND TEC1. RX PubMed=15485921; DOI=10.1128/mcb.24.21.9542-9556.2004; RA Kim T.S., Kim H.Y., Yoon J.H., Kang H.S.; RT "Recruitment of the Swi/Snf complex by Ste12-Tec1 promotes Flo8-Mss11- RT mediated activation of STA1 expression."; RL Mol. Cell. Biol. 24:9542-9556(2004). RN [11] RP FUNCTION. RX PubMed=15466424; DOI=10.1534/genetics.104.033704; RA van Dyk D., Pretorius I.S., Bauer F.F.; RT "Mss11p is a central element of the regulatory network that controls FLO11 RT expression and invasive growth in Saccharomyces cerevisiae."; RL Genetics 169:91-106(2005). RN [12] RP FUNCTION. RX PubMed=16568252; DOI=10.1007/s00294-006-0068-z; RA Bester M.C., Pretorius I.S., Bauer F.F.; RT "The regulation of Saccharomyces cerevisiae FLO gene expression and Ca2+ RT -dependent flocculation by Flo8p and Mss11p."; RL Curr. Genet. 49:375-383(2006). RN [13] RP FUNCTION. RX PubMed=18001350; DOI=10.1111/j.1365-2958.2007.06014.x; RA Fichtner L., Schulze F., Braus G.H.; RT "Differential Flo8p-dependent regulation of FLO1 and FLO11 for cell-cell RT and cell-substrate adherence of S.cerevisiae S288c."; RL Mol. Microbiol. 66:1276-1289(2007). RN [14] RP FUNCTION. RX PubMed=18202364; DOI=10.1534/genetics.107.081315; RA Barrales R.R., Jimenez J., Ibeas J.I.; RT "Identification of novel activation mechanisms for FLO11 regulation in RT Saccharomyces cerevisiae."; RL Genetics 178:145-156(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Transcription factor that regulates pseudohyphal CC differentiation, invasive growth, floculation, adhesion and starch CC metabolism in response to nutrient availability. CC {ECO:0000269|PubMed:10515942, ECO:0000269|PubMed:12492858, CC ECO:0000269|PubMed:14523573, ECO:0000269|PubMed:15466424, CC ECO:0000269|PubMed:15485921, ECO:0000269|PubMed:16568252, CC ECO:0000269|PubMed:18001350, ECO:0000269|PubMed:18202364, CC ECO:0000269|PubMed:9342405, ECO:0000269|PubMed:9832522, CC ECO:0000269|PubMed:9987114}. CC -!- SUBUNIT: Interacts with FLO8, STE12 and TEC1. CC {ECO:0000269|PubMed:15485921}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus CC {ECO:0000269|PubMed:14562095}. CC -!- SIMILARITY: Belongs to the MSS11 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; Z49705; CAA89800.1; -; Genomic_DNA. DR EMBL; BK006946; DAA10060.1; -; Genomic_DNA. DR PIR; S54522; S54522. DR RefSeq; NP_013887.1; NM_001182668.1. DR AlphaFoldDB; Q03825; -. DR BioGRID; 35342; 78. DR IntAct; Q03825; 1. DR STRING; 4932.YMR164C; -. DR GlyGen; Q03825; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q03825; -. DR PaxDb; 4932-YMR164C; -. DR PeptideAtlas; Q03825; -. DR EnsemblFungi; YMR164C_mRNA; YMR164C; YMR164C. DR GeneID; 855200; -. DR KEGG; sce:YMR164C; -. DR AGR; SGD:S000004774; -. DR SGD; S000004774; MSS11. DR VEuPathDB; FungiDB:YMR164C; -. DR eggNOG; ENOG502S549; Eukaryota. DR HOGENOM; CLU_368109_0_0_1; -. DR InParanoid; Q03825; -. DR OMA; FLIEWWN; -. DR OrthoDB; 1978411at2759; -. DR BioCyc; YEAST:G3O-32854-MONOMER; -. DR BioGRID-ORCS; 855200; 6 hits in 10 CRISPR screens. DR PRO; PR:Q03825; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; Q03825; Protein. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IC:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD. DR InterPro; IPR006594; LisH. DR PANTHER; PTHR45093; TRANSCRIPTION ACTIVATOR MSS11; 1. DR PANTHER; PTHR45093:SF2; TRANSCRIPTION ACTIVATOR MSS11; 1. DR Pfam; PF08513; LisH; 1. DR SMART; SM00667; LisH; 1. DR PROSITE; PS50896; LISH; 1. PE 1: Evidence at protein level; KW Activator; Cytoplasm; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..758 FT /note="Transcription activator MSS11" FT /id="PRO_0000203315" FT DOMAIN 51..83 FT /note="LisH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 191..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 268..299 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 322..355 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 428..454 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 587..681 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..669 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 133..134 FT /note="FL->GA: Reduces ability to activate transcription FT and to induce invasive growth." FT /evidence="ECO:0000269|PubMed:12492858" FT MUTAGEN 137..138 FT /note="WW->GA: Reduces ability to activate transcription FT and to induce invasive growth." FT /evidence="ECO:0000269|PubMed:12492858" FT MUTAGEN 140..141 FT /note="IF->GA: Reduces ability to activate transcription FT and to induce invasive growth." FT /evidence="ECO:0000269|PubMed:12492858" FT MUTAGEN 144..145 FT /note="LF->GA: Reduces ability to activate transcription FT and to induce invasive growth." FT /evidence="ECO:0000269|PubMed:12492858" SQ SEQUENCE 758 AA; 85050 MW; BA05BFC754D9294B CRC64; MDNTTNINTN ERSSNTDFSS APNIKGLNSH TQLQFDADSR VFVSDVMAKN SKQLLYAHIY NYLIKNNYWN SAAKFLSEAD LPLSRINGSA SGGKTSLNAS LKQGLMDIAS KGDIVSEDGL LPSKMLMDAN DTFLLEWWEI FQSLFNGDLE SGYQQDHNPL RERIIPILPA NSKSNMPSHF SNLPPNVIPP TQNSFPVSEE SFRPNGDGSN FNLNDPTNRN VSERFLSRTS GVYDKQNSAN FAPDTAINSD IAGQQYATIN LHKHFNDLQS PAQPQQSSQQ QIQQPQHQPQ HQPQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQHQQQQQT PYPIVNPQMV PHIPSENSHS TGLMPSVPPT NQQFNAQTQS SMFSDQQRFF QYQLHHQNQG QAPSFQQSQS GRFDDMNAMK MFFQQQALQQ NSLQQNLGNQ NYQSNTRNNT AEETTPTNDN NANGNSLLQE HIRARFNKMK TIPQQMKNQS TVANPVVSDI TSQQQYMHMM MQRMAANQQL QNSAFPPDTN RIAPANNTMP LQPGNMGSPV IENPGMRQTN PSGQNPMINM QPLYQNVSSA MHAFAPQQQF HLPQHYKTNT SVPQNDSTSV FPLPNNNNNN NNNNNNNNNN NSNNSNNNNN NNNNNNNSNN TPTVSQPSSK CTSSSSTTPN ITTTIQPKRK QRVGKTKTKE SRKVAAAQKV MKSKKLEQNG DSAATNFINV TPKDSGGKGT VKVQNSNSQQ QLNGSFSMDT ETFDIFNIGD FSPDLMDS //