ID MOT3_YEAST Reviewed; 490 AA. AC P54785; D6VZP4; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 182. DE RecName: Full=Transcriptional activator/repressor MOT3; DE AltName: Full=Hypoxic gene repressor protein 7; DE AltName: Full=Modulator of transcription protein 3; GN Name=MOT3; Synonyms=ROX7; OrderedLocusNames=YMR070W; GN ORFNames=YM9916.09; 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], FUNCTION, AND DNA-BINDING. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9528759; DOI=10.1128/mcb.18.4.1879; RA Madison J.M., Dudley A.M., Winston F.; RT "Identification and analysis of Mot3, a zinc finger protein that binds to RT the retrotransposon Ty long terminal repeat (delta) in Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 18:1879-1890(1998). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP FUNCTION IN TRANSCRIPTIONAL ACTIVATION, DNA-BINDING, AND SUBCELLULAR RP LOCATION. RX PubMed=9611199; DOI=10.1093/genetics/149.2.879; RA Grishin A.V., Rothenberg M., Downs M.A., Blumer K.J.; RT "Mot3, a Zn finger transcription factor that modulates gene expression and RT attenuates mating pheromone signaling in Saccharomyces cerevisiae."; RL Genetics 149:879-892(1998). RN [6] RP FUNCTION. RX PubMed=10982825; DOI=10.1128/mcb.20.19.7088-7098.2000; RA Kastaniotis A.J., Mennella T.A., Konrad C., Rodriguez Torres A.M., RA Zitomer R.S.; RT "Roles of transcription factor Mot3 and chromatin in repression of the RT hypoxic gene ANB1 in yeast."; RL Mol. Cell. Biol. 20:7088-7098(2000). RN [7] RP FUNCTION IN TRANSCRIPTIONAL REPRESSION. RX PubMed=12145211; DOI=10.1093/emboj/cdf415; RA Hongay C., Jia N., Bard M., Winston F.; RT "Mot3 is a transcriptional repressor of ergosterol biosynthetic genes and RT is required for normal vacuolar function in Saccharomyces cerevisiae."; RL EMBO J. 21:4114-4124(2002). RN [8] 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 [9] RP FUNCTION IN REPRESSION OF HYPOXIC GENES, AND INDUCTION. RX PubMed=14530431; DOI=10.1093/nar/gkg792; RA Sertil O., Kapoor R., Cohen B.D., Abramova N., Lowry C.V.; RT "Synergistic repression of anaerobic genes by Mot3 and Rox1 in RT Saccharomyces cerevisiae."; RL Nucleic Acids Res. 31:5831-5837(2003). RN [10] RP FUNCTION. RX PubMed=15821125; DOI=10.1128/ec.4.4.649-660.2005; RA Klinkenberg L.G., Mennella T.A., Luetkenhaus K., Zitomer R.S.; RT "Combinatorial repression of the hypoxic genes of Saccharomyces cerevisiae RT by DNA binding proteins Rox1 and Mot3."; RL Eukaryot. Cell 4:649-660(2005). RN [11] RP PRION FORMATION. RX PubMed=19345193; DOI=10.1016/j.cell.2009.02.044; RA Alberti S., Halfmann R., King O., Kapila A., Lindquist S.; RT "A systematic survey identifies prions and illuminates sequence features of RT prionogenic proteins."; RL Cell 137:146-158(2009). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 affects the expression of a large CC set of genes. Recognizes and binds to the consensus sequence 5'- CC [CAT]AGG[TC]A-3' in the promoter region. Plays a major role in the CC repression of a specific subset of hypoxic genes (e.g. ANB1, DAN1 and CC HEM13) under aerobic conditions. Acts synergistically with the CC transcription factor ROX1 to recruit the general repression complex CC SSN6-TUP1 to the promoter of hypoxic genes. Represses transcription of CC ergosterol biosynthetic genes. Negatively regulates pheromone-induced CC gene expression. Can act as a transcriptional activator (e.g. of genes CC like CYC1, SUC2 and the Ty long terminal repeat delta promoter). CC {ECO:0000269|PubMed:10982825, ECO:0000269|PubMed:12145211, CC ECO:0000269|PubMed:14530431, ECO:0000269|PubMed:15821125, CC ECO:0000269|PubMed:9528759, ECO:0000269|PubMed:9611199}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9611199}. CC -!- INDUCTION: Induced under aerobic conditions and repressed under CC anaerobic conditions. {ECO:0000269|PubMed:14530431}. CC -!- DOMAIN: The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is CC unstructured in its native, soluble form, and which forms a parallel CC in-register beta-sheet in its amyloid form. {ECO:0000250}. CC -!- MISCELLANEOUS: [MOT3+] is the prion form of MOT3. [MOT3+] is the result CC of a conformational change of the cellular MOT3 protein that becomes CC self-propagating and infectious. This conformational change generates a CC form of MOT3 that assembles into amyloid fibrils. [MOT3+]-aggregates CC sequester soluble MOT3, resulting in a loss-of-function phenotype for CC MOT3. [MOT3+] can be cured by GdnHCl and by inactivation of the CC molecular chaperone HSP104, which is required for [MOT3+] propagation. CC It is speculated that prion properties of transcription factors may CC generate an optimized phenotypic heterogeneity that buffers yeast CC populations against diverse environmental insults. CC {ECO:0000305|PubMed:19345193}. CC -!- MISCELLANEOUS: Present with 1690 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; U25279; AAC49982.1; -; Genomic_DNA. DR EMBL; Z48952; CAA88795.1; -; Genomic_DNA. DR EMBL; AY693209; AAT93228.1; -; Genomic_DNA. DR EMBL; BK006946; DAA09968.1; -; Genomic_DNA. DR PIR; S52830; S52830. DR RefSeq; NP_013786.1; NM_001182568.1. DR AlphaFoldDB; P54785; -. DR BioGRID; 35245; 331. DR IntAct; P54785; 26. DR MINT; P54785; -. DR STRING; 4932.YMR070W; -. DR iPTMnet; P54785; -. DR MaxQB; P54785; -. DR PaxDb; 4932-YMR070W; -. DR PeptideAtlas; P54785; -. DR EnsemblFungi; YMR070W_mRNA; YMR070W; YMR070W. DR GeneID; 855092; -. DR KEGG; sce:YMR070W; -. DR AGR; SGD:S000004674; -. DR SGD; S000004674; MOT3. DR VEuPathDB; FungiDB:YMR070W; -. DR eggNOG; KOG1721; Eukaryota. DR HOGENOM; CLU_562847_0_0_1; -. DR InParanoid; P54785; -. DR OMA; NHPNYPP; -. DR OrthoDB; 2038716at2759; -. DR BioCyc; YEAST:G3O-32772-MONOMER; -. DR BioGRID-ORCS; 855092; 7 hits in 13 CRISPR screens. DR PRO; PR:P54785; -. DR Proteomes; UP000002311; Chromosome XIII. DR RNAct; P54785; Protein. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IMP:SGD. DR GO; GO:0010895; P:negative regulation of ergosterol biosynthetic process; IMP:SGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR40626; MIP31509P; 1. DR PANTHER; PTHR40626:SF11; ZINC FINGER PROTEIN YGR067C; 1. DR SMART; SM00355; ZnF_C2H2; 2. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. PE 1: Evidence at protein level; KW Acetylation; Activator; Amyloid; Metal-binding; Nucleus; Prion; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..490 FT /note="Transcriptional activator/repressor MOT3" FT /id="PRO_0000046807" FT ZN_FING 346..368 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 374..397 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT REGION 1..69 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 98..295 FT /note="Prion domain (PrD)" FT REGION 101..162 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 214..267 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 421..458 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 214..231 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 249..267 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 421..439 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 490 AA; 54382 MW; 4D0DA8DE43F171ED CRC64; MNADHHLQQQ QQQRQQHQQQ QHQQQQHQHQ HQQQQHTILQ NVSNTNNIGS DSLASQPFNT TTVSSNKDDV MVNSGARELP MPLHQQQYIY PYYQYTSNNS NNNNVTAGNN MSASPIVHNN SNNSNNSNIS ASDYTVANNS TSNNNNNNNN NNNNNNNIHP NQFTAAANMN SNAAAAAYYS FPTANMPIPQ QDQQYMFNPA SYISHYYSAV NSNNNGNNAA NNGSNNSSHS APAPAPGPPH HHHHHSNTHN NLNNGGAVNT NNAPQHHPTI ITDQFQFQLQ QNPSPNLNLN INPAQPLHLP PGWKINTMPQ PRPTTAPNHP PAPVPSSNPV ASNLVPAPSS DHKYIHQCQF CEKSFKRKSW LKRHLLSHSQ QRHFLCPWCL SRQKRKDNLL QHMKLKHTNY LLDELKKNNI IFNYNNSSSS NNNNDNNNNN NSNSASGSGG AGAAAAAATA PENEDGNGYD TNIKTLINDG VLNKDDVKRV LNNLIVSHNK //