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P25367

- RNQ1_YEAST

UniProt

P25367 - RNQ1_YEAST

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Protein

[PIN+] prion protein RNQ1

Gene
RNQ1, YCL028W, YCL181, YCL28W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: SGD
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

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

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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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811A → T in AAA34615. 1 Publication

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 108 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 (1 Publication). [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 (1 Publication). [PIN+] promotes de novo [PSI+] formation upon SUP35 overproduction (cross-seeding) (1 Publication). [PIN+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PIN+] propagation (1 Publication).
Present with 1140 molecules/cell in log phase SD medium.

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

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