P25367 (RNQ1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
[PIN+] prion protein RNQ1

Alternative name(s):
Rich in asparagine and glutamine protein 1

Gene names

Name:	RNQ1
Ordered Locus Names:	YCL028W
ORF Names:	YCL181, YCL28W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	405 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transferable epigenetic modifier which forms a prion responsible for the non-Mendelian trait [PIN+]. The native function of the soluble protein is unknown. Ref.8 Ref.9
Subcellular location	Cytoplasm. Nucleus Ref.10.
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.
Miscellaneous	[PIN+], also known as [RNQ+], is the prion form of RNQ1 (Ref.8). [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 (Ref.12). [PIN+] promotes de novo [PSI+] formation upon SUP35 overproduction (cross-seeding) (Ref.9). [PIN+] can be cured by GdnHCl and by deletion of the molecular chaperone HSP104, which is required for [PIN+] propagation (Ref.8). Present with 1140 molecules/cell in log phase SD medium.
Sequence caution	The sequence AAA34615.1 differs from that shown. Reason: Frameshift at position 323.

Ontologies

Keywords
Cellular component	Amyloid Cytoplasm Nucleus
Molecular function	Prion
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytosol Inferred from direct assay Ref.9. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 405	405	[PIN+] prion protein RNQ1		PRO_0000097390
Regions
	Region	153 – 402	250	Prion domain (PrD)
Amino acid modifications
	Modified residue	143	1	Phosphoserine Ref.13
Natural variations
	Natural variant	166 – 169	4	Missing in strain: SCI7.2/b, SCI11.5/a and SCI11.5/c.
	Natural variant	171 – 172	2	Missing in strain: SCI7.2/a, SCI7.2/d, SCI11.5/b and SCI11.5/d.
	Natural variant	289 – 299	11	Missing in strain: SCI7.2/b, SCI7.2/d and SCI11.5/c.
	Natural variant	293 – 303	11	Missing in strain: SCI9.
	Natural variant	360	1	Q → 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 variant	372	1	P → PQHNGQQQSNEYGRP in strain: SCI7.2/b, SCI7.2/d and SCI11.5/c.
	Natural variant	383	1	Q → H in strain: SCI7.2/b,SCI7.2/d and SCI11.5/c.
	Natural variant	387	1	F → L in strain: SCI4.
Experimental info
	Sequence conflict	181	1	A → T in AAA34615. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25367 [UniParc]. Last modified April 26, 2004. Version 2. Checksum: 8ED9C40A7DF70F7F	FASTA	405	42,580
	10 20 30 40 50 60 MDTDKLISEA ESHFSQGNHA EAVAKLTSAA QSNPNDEQMS TIESLIQKIA GYVMDNRSGG 70 80 90 100 110 120 SDASQDRAAG GGSSFMNTLM ADSKGSSQTQ LGKLALLATV MTHSSNKGSS NRGFDVGTVM 130 140 150 160 170 180 SMLSGSGGGS QSMGASGLAA LASQFFKSGN NSQGQGQGQG QGQGQGQGQG QGSFTALASL 190 200 210 220 230 240 ASSFMNSNNN NQQGQNQSSG GSSFGALASM ASSFMHSNNN QNSNNSQQGY NQSYQNGNQN 250 260 270 280 290 300 SQGYNNQQYQ GGNGGYQQQQ GQSGGAFSSL ASMAQSYLGG GQTQSNQQQY NQQGQNNQQQ 310 320 330 340 350 360 YQQQGQNYQH QQQGQQQQQG HSSSFSALAS MASSYLGNNS NSNSSYGGQQ QANEYGRPQQ 370 380 390 400 NGQQQSNEYG RPQYGGNQNS NGQHESFNFS GNFSQQNNNG NQNRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]	"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].
[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, MASS SPECTROMETRY.
[14]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S19355.
RefSeq	NP_009902.2. NM_001178673.1.
3D structure databases
ProteinModelPortal	P25367.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-4323N.
IntAct	P25367. 29 interactions.
MINT	MINT-516964.
Proteomic databases
PeptideAtlas	P25367.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YCL028W; YCL028W; YCL028W.
GeneID	850329.
KEGG	sce:YCL028W.
Organism-specific databases
CYGD	YCL028w.
SGD	S000000533. RNQ1.
Phylogenomic databases
GeneTree	ENSGT00660000096134.
OrthoDB	EOG4Q5D0B.
Gene expression databases
Genevestigator	P25367.
GermOnline	YCL028W. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other
NextBio	965757.

Entry information

Entry name

RNQ1_YEAST

Accession

Primary (citable) accession number: P25367
Secondary accession number(s): D6VQY7 , Q8NKJ9, Q8TF94, Q8TFA2, Q8TFC8, Q8TFP4, Q8TFP5, Q8TFP6, Q8TFP7, Q8TFP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	April 26, 2004
Last modified:	April 3, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program