MOT3_YEAST
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 03-AUG-2022, entry version 175.
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; 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}.
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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; 311.
DR IntAct; P54785; 26.
DR MINT; P54785; -.
DR STRING; 4932.YMR070W; -.
DR iPTMnet; P54785; -.
DR MaxQB; P54785; -.
DR PaxDb; P54785; -.
DR PRIDE; P54785; -.
DR EnsemblFungi; YMR070W_mRNA; YMR070W; YMR070W.
DR GeneID; 855092; -.
DR KEGG; sce:YMR070W; -.
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 BioCyc; YEAST:G3O-32772-MON; -.
DR PRO; PR:P54785; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P54785; protein.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF57667; SSF57667; 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
