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P54785 (MOT3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcriptional activator/repressor MOT3
Alternative name(s):
Hypoxic gene repressor protein 7
Modulator of transcription protein 3
Gene names
Name:MOT3
Synonyms:ROX7
Ordered Locus Names:YMR070W
ORF Names:YM9916.09
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length490 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that affects the expression of a large set of genes. Recognizes and binds to the consensus sequence 5'-[CAT]AGG[TC]A-3' in the promoter region. Plays a major role in the repression of a specific subset of hypoxic genes (e.g. ANB1, DAN1 and HEM13) under aerobic conditions. Acts synergistically with the transcription factor ROX1 to recruit the general repression complex SSN6-TUP1 to the promoter of hypoxic genes. Represses transcription of ergosterol biosynthetic genes. Negatively regulates pheromone-induced gene expression. Can act as a transcriptional activator (e.g. of genes like CYC1, SUC2 and the Ty long terminal repeat delta promoter). Ref.1 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10

Subcellular location

Nucleus Ref.5.

Induction

Induced under aerobic conditions and repressed under anaerobic conditions. Ref.9

Domain

The prion domain (PrD) is a Gln/Asn (Q/N)-rich domain, which is unstructured in its native, soluble form, and which forms a parallel in-register beta-sheet in its amyloid form By similarity.

Miscellaneous

[MOT3+] is the prion form of MOT3. [MOT3+] is the result of a conformational change of the cellular MOT3 protein that becomes self-propagating and infectious. This conformational change generates a form of MOT3 that assembles into amyloid fibrils. [MOT3+] aggregates sequester soluble MOT3, resulting in a loss-of-function phenotype for MOT3. [MOT3+] can be cured by GdnHCl and by inactivation of the molecular chaperone HSP104, which is required for [MOT3+] propagation. It is speculated that prion properties of transcription factors may generate an optimized phenotypic heterogeneity that buffers yeast populations against diverse environmental insults (Ref.11).

Present with 1690 molecules/cell in log phase SD medium.

Sequence similarities

Contains 2 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentAmyloid
Nucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionActivator
Prion
Repressor
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular hyperosmotic response

Inferred from mutant phenotype PubMed 21299653. Source: SGD

negative regulation of ergosterol biosynthetic process

Inferred from mutant phenotype Ref.7PubMed 21299653. Source: SGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.6Ref.7PubMed 21299653. Source: SGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 11292809. Source: SGD

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from direct assay PubMed 22932476. Source: SGD

nucleus

Inferred from direct assay PubMed 22932476Ref.5. Source: SGD

   Molecular_functionRNA polymerase II activating transcription factor binding

Inferred from physical interaction PubMed 16783004. Source: SGD

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay Ref.5. Source: SGD

RNA polymerase II repressing transcription factor binding

Inferred from mutant phenotype PubMed 14665463. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 490490Transcriptional activator/repressor MOT3
PRO_0000046807

Regions

Zinc finger346 – 36823C2H2-type 1
Zinc finger374 – 39724C2H2-type 2
Region98 – 295198Prion domain (PrD)
Compositional bias8 – 3528Poly-Gln
Compositional bias98 – 1047Poly-Asn
Compositional bias143 – 15715Poly-Asn
Compositional bias173 – 1775Poly-Ala
Compositional bias240 – 2456Poly-His
Compositional bias417 – 4204Poly-Ser
Compositional bias421 – 43313Poly-Asn
Compositional bias441 – 45010Poly-Ala

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12

Sequences

Sequence LengthMass (Da)Tools
P54785 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 4D0DA8DE43F171ED

FASTA49054,382
        10         20         30         40         50         60 
MNADHHLQQQ QQQRQQHQQQ QHQQQQHQHQ HQQQQHTILQ NVSNTNNIGS DSLASQPFNT 

        70         80         90        100        110        120 
TTVSSNKDDV MVNSGARELP MPLHQQQYIY PYYQYTSNNS NNNNVTAGNN MSASPIVHNN 

       130        140        150        160        170        180 
SNNSNNSNIS ASDYTVANNS TSNNNNNNNN NNNNNNNIHP NQFTAAANMN SNAAAAAYYS 

       190        200        210        220        230        240 
FPTANMPIPQ QDQQYMFNPA SYISHYYSAV NSNNNGNNAA NNGSNNSSHS APAPAPGPPH 

       250        260        270        280        290        300 
HHHHHSNTHN NLNNGGAVNT NNAPQHHPTI ITDQFQFQLQ QNPSPNLNLN INPAQPLHLP 

       310        320        330        340        350        360 
PGWKINTMPQ PRPTTAPNHP PAPVPSSNPV ASNLVPAPSS DHKYIHQCQF CEKSFKRKSW 

       370        380        390        400        410        420 
LKRHLLSHSQ QRHFLCPWCL SRQKRKDNLL QHMKLKHTNY LLDELKKNNI IFNYNNSSSS 

       430        440        450        460        470        480 
NNNNDNNNNN NSNSASGSGG AGAAAAAATA PENEDGNGYD TNIKTLINDG VLNKDDVKRV 

       490 
LNNLIVSHNK 

« Hide

References

« Hide 'large scale' references
[1]"Identification and analysis of Mot3, a zinc finger protein that binds to the retrotransposon Ty long terminal repeat (delta) in Saccharomyces cerevisiae."
Madison J.M., Dudley A.M., Winston F.
Mol. Cell. Biol. 18:1879-1890(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DNA-BINDING.
Strain: ATCC 204508 / S288c.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"Mot3, a Zn finger transcription factor that modulates gene expression and attenuates mating pheromone signaling in Saccharomyces cerevisiae."
Grishin A.V., Rothenberg M., Downs M.A., Blumer K.J.
Genetics 149:879-892(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL ACTIVATION, DNA-BINDING, SUBCELLULAR LOCATION.
[6]"Roles of transcription factor Mot3 and chromatin in repression of the hypoxic gene ANB1 in yeast."
Kastaniotis A.J., Mennella T.A., Konrad C., Rodriguez Torres A.M., Zitomer R.S.
Mol. Cell. Biol. 20:7088-7098(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Mot3 is a transcriptional repressor of ergosterol biosynthetic genes and is required for normal vacuolar function in Saccharomyces cerevisiae."
Hongay C., Jia N., Bard M., Winston F.
EMBO J. 21:4114-4124(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Synergistic repression of anaerobic genes by Mot3 and Rox1 in Saccharomyces cerevisiae."
Sertil O., Kapoor R., Cohen B.D., Abramova N., Lowry C.V.
Nucleic Acids Res. 31:5831-5837(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REPRESSION OF HYPOXIC GENES, INDUCTION.
[10]"Combinatorial repression of the hypoxic genes of Saccharomyces cerevisiae by DNA binding proteins Rox1 and Mot3."
Klinkenberg L.G., Mennella T.A., Luetkenhaus K., Zitomer R.S.
Eukaryot. Cell 4:649-660(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"A systematic survey identifies prions and illuminates sequence features of prionogenic proteins."
Alberti S., Halfmann R., King O., Kapila A., Lindquist S.
Cell 137:146-158(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PRION FORMATION.
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25279 Genomic DNA. Translation: AAC49982.1.
Z48952 Genomic DNA. Translation: CAA88795.1.
AY693209 Genomic DNA. Translation: AAT93228.1.
BK006946 Genomic DNA. Translation: DAA09968.1.
PIRS52830.
RefSeqNP_013786.1. NM_001182568.1.

3D structure databases

ProteinModelPortalP54785.
SMRP54785. Positions 339-432.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35245. 115 interactions.
IntActP54785. 26 interactions.
MINTMINT-4497702.
STRING4932.YMR070W.

Proteomic databases

MaxQBP54785.
PaxDbP54785.
PeptideAtlasP54785.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR070W; YMR070W; YMR070W.
GeneID855092.
KEGGsce:YMR070W.

Organism-specific databases

CYGDYMR070w.
SGDS000004674. MOT3.

Phylogenomic databases

eggNOGNOG255610.
OMAASYISHY.
OrthoDBEOG757D9C.

Enzyme and pathway databases

BioCycYEAST:G3O-32772-MONOMER.

Gene expression databases

GenevestigatorP54785.

Family and domain databases

Gene3D3.30.160.60. 2 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 2 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio978399.

Entry information

Entry nameMOT3_YEAST
AccessionPrimary (citable) accession number: P54785
Secondary accession number(s): D6VZP4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families