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P25367

- RNQ1_YEAST

UniProt

P25367 - RNQ1_YEAST

Protein

[PIN+] prion protein RNQ1

Gene

RNQ1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (26 Apr 2004)
      Previous versions | rss
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    Functioni

    Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown.2 Publications

    Keywords - Molecular functioni

    Prion

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29289-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    [PIN+] prion protein RNQ1
    Alternative name(s):
    Rich in asparagine and glutamine protein 1
    Gene namesi
    Name:RNQ1
    Ordered Locus Names:YCL028W
    ORF Names:YCL181, YCL28W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome III

    Organism-specific databases

    CYGDiYCL028w.
    SGDiS000000533. RNQ1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Amyloid, Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405[PIN+] prion protein RNQ1PRO_0000097390Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei143 – 1431Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP25367.
    PeptideAtlasiP25367.

    Expressioni

    Gene expression databases

    GenevestigatoriP25367.

    Interactioni

    Protein-protein interaction databases

    BioGridi30955. 88 interactions.
    DIPiDIP-4323N.
    IntActiP25367. 19 interactions.
    MINTiMINT-516964.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni153 – 402250Prion domain (PrD)Add
    BLAST

    Domaini

    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.

    Phylogenomic databases

    OMAiSNQNYGS.
    OrthoDBiEOG7X3R3V.

    Sequencei

    Sequence statusi: Complete.

    P25367-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTDKLISEA ESHFSQGNHA EAVAKLTSAA QSNPNDEQMS TIESLIQKIA    50
    GYVMDNRSGG SDASQDRAAG GGSSFMNTLM ADSKGSSQTQ LGKLALLATV 100
    MTHSSNKGSS NRGFDVGTVM SMLSGSGGGS QSMGASGLAA LASQFFKSGN 150
    NSQGQGQGQG QGQGQGQGQG QGSFTALASL ASSFMNSNNN NQQGQNQSSG 200
    GSSFGALASM ASSFMHSNNN QNSNNSQQGY NQSYQNGNQN SQGYNNQQYQ 250
    GGNGGYQQQQ GQSGGAFSSL ASMAQSYLGG GQTQSNQQQY NQQGQNNQQQ 300
    YQQQGQNYQH QQQGQQQQQG HSSSFSALAS MASSYLGNNS NSNSSYGGQQ 350
    QANEYGRPQQ NGQQQSNEYG RPQYGGNQNS NGQHESFNFS GNFSQQNNNG 400
    NQNRY 405
    Length:405
    Mass (Da):42,580
    Last modified:April 26, 2004 - v2
    Checksum:i8ED9C40A7DF70F7F
    GO

    Sequence cautioni

    The sequence AAA34615.1 differs from that shown. Reason: Frameshift at position 323.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811A → T in AAA34615. (PubMed:3302672)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti166 – 1694Missing in strain: SCI7.2/b, SCI11.5/a and SCI11.5/c.
    Natural varianti171 – 1722Missing in strain: SCI7.2/a, SCI7.2/d, SCI11.5/b and SCI11.5/d.
    Natural varianti289 – 29911Missing in strain: SCI7.2/b, SCI7.2/d and SCI11.5/c.
    Add
    BLAST
    Natural varianti293 – 30311Missing in strain: SCI9.
    Add
    BLAST
    Natural varianti360 – 3601Q → H in strain: SCI3, SCI4, SCI7.2/a, SCI7.2/b, SCI7.2/d, SCI11.5/a, SCI11.5/b, SCI11.5/c and SCI11.5/d.
    Natural varianti372 – 3721P → PQHNGQQQSNEYGRP in strain: SCI7.2/b, SCI7.2/d and SCI11.5/c.
    Natural varianti383 – 3831Q → H in strain: SCI7.2/b,SCI7.2/d and SCI11.5/c.
    Natural varianti387 – 3871F → L in strain: SCI4.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16717 Genomic DNA. Translation: AAA34615.1. Frameshift.
    X59720 Genomic DNA. Translation: CAC42958.1.
    AY028674 Genomic DNA. Translation: AAK26208.1.
    AY028675 Genomic DNA. Translation: AAK26209.1.
    AY028676 Genomic DNA. Translation: AAK26210.1.
    AY028677 Genomic DNA. Translation: AAK26211.1.
    AY028678 Genomic DNA. Translation: AAK26212.1.
    AY028679 Genomic DNA. Translation: AAK26213.1.
    AY028680 Genomic DNA. Translation: AAK26214.1.
    AY028681 Genomic DNA. Translation: AAK26215.1.
    AY028682 Genomic DNA. Translation: AAK26216.1.
    AY028683 Genomic DNA. Translation: AAK26217.1.
    AY028684 Genomic DNA. Translation: AAK26218.1.
    AY028685 Genomic DNA. Translation: AAK26219.1.
    BK006937 Genomic DNA. Translation: DAA07456.1.
    PIRiS19355.
    RefSeqiNP_009902.2. NM_001178673.1.

    Genome annotation databases

    EnsemblFungiiYCL028W; YCL028W; YCL028W.
    GeneIDi850329.
    KEGGisce:YCL028W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M16717 Genomic DNA. Translation: AAA34615.1 . Frameshift.
    X59720 Genomic DNA. Translation: CAC42958.1 .
    AY028674 Genomic DNA. Translation: AAK26208.1 .
    AY028675 Genomic DNA. Translation: AAK26209.1 .
    AY028676 Genomic DNA. Translation: AAK26210.1 .
    AY028677 Genomic DNA. Translation: AAK26211.1 .
    AY028678 Genomic DNA. Translation: AAK26212.1 .
    AY028679 Genomic DNA. Translation: AAK26213.1 .
    AY028680 Genomic DNA. Translation: AAK26214.1 .
    AY028681 Genomic DNA. Translation: AAK26215.1 .
    AY028682 Genomic DNA. Translation: AAK26216.1 .
    AY028683 Genomic DNA. Translation: AAK26217.1 .
    AY028684 Genomic DNA. Translation: AAK26218.1 .
    AY028685 Genomic DNA. Translation: AAK26219.1 .
    BK006937 Genomic DNA. Translation: DAA07456.1 .
    PIRi S19355.
    RefSeqi NP_009902.2. NM_001178673.1.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 30955. 88 interactions.
    DIPi DIP-4323N.
    IntActi P25367. 19 interactions.
    MINTi MINT-516964.

    Proteomic databases

    MaxQBi P25367.
    PeptideAtlasi P25367.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YCL028W ; YCL028W ; YCL028W .
    GeneIDi 850329.
    KEGGi sce:YCL028W.

    Organism-specific databases

    CYGDi YCL028w.
    SGDi S000000533. RNQ1.

    Phylogenomic databases

    OMAi SNQNYGS.
    OrthoDBi EOG7X3R3V.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29289-MONOMER.

    Miscellaneous databases

    NextBioi 965757.

    Gene expression databases

    Genevestigatori P25367.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Two genes required for cell fusion during yeast conjugation: evidence for a pheromone-induced surface protein."
      Trueheart J., Boeke J.D., Fink G.R.
      Mol. Cell. Biol. 7:2316-2328(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete sequence of a 11,953 bp fragment from C1G on chromosome III encompasses four new open reading frames."
      Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.
      Yeast 7:533-538(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The complete DNA sequence of yeast chromosome III."
      Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
      , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
      Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Valles G., Volckaerts G.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 360.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Prion protein gene polymorphisms in Saccharomyces cerevisiae."
      Resende C.G., Outeiro T.F., Sands L., Lindquist S., Tuite M.F.
      Mol. Microbiol. 49:1005-1017(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-405.
      Strain: SCI11.5/a, SCI11.5/b, SCI11.5/c, SCI11.5/d, SCI16, SCI3, SCI4, SCI7.2/a, SCI7.2/b, SCI7.2/d, SCI9 and SCI9*.
    7. "Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae."
      Derkatch I.L., Bradley M.E., Zhou P., Chernoff Y.O., Liebman S.W.
      Genetics 147:507-519(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRION FORMATION.
    8. "Rnq1: an epigenetic modifier of protein function in yeast."
      Sondheimer N., Lindquist S.L.
      Mol. Cell 5:163-172(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION AS A PRION, AGGREGATION.
    9. "Prions affect the appearance of other prions: the story of [PIN(+)]."
      Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W.
      Cell 106:171-182(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AGGREGATION.
    10. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    12. "'Prion-proof' for [PIN+]: infection with in vitro-made amyloid aggregates of Rnq1p-(132-405) induces [PIN+]."
      Patel B.K., Liebman S.W.
      J. Mol. Biol. 365:773-782(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRION PROPAGATION.
    13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure."
      Wickner R.B., Dyda F., Tycko R.
      Proc. Natl. Acad. Sci. U.S.A. 105:2403-2408(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 153-405.

    Entry informationi

    Entry nameiRNQ1_YEAST
    AccessioniPrimary (citable) accession number: P25367
    Secondary accession number(s): D6VQY7
    , Q8NKJ9, Q8TF94, Q8TFA2, Q8TFC8, Q8TFP4, Q8TFP5, Q8TFP6, Q8TFP7, Q8TFP8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    [PIN+], also known as [RNQ+], is the prion form of RNQ1 (PubMed:10678178). [PIN+] is the result of a conformational change of the cellular RNQ1 protein that becomes self-propagating and infectious. This conformational change generates a form of RNQ1 that assembles into amyloid fibrils (PubMed:17097676). [PIN+] promotes de novo [PSI+] formation upon SUP35 overproduction (cross-seeding) (PubMed:11511345). [PIN+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PIN+] propagation (PubMed:10678178).3 Publications
    Present with 1140 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome III
      Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

    External Data

    Dasty 3