RNQ1_YEAST
ID RNQ1_YEAST Reviewed; 405 AA.
AC P25367; D6VQY7; Q8NKJ9; Q8TF94; Q8TFA2; Q8TFC8; Q8TFP4; Q8TFP5; Q8TFP6;
AC Q8TFP7; Q8TFP8;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=[PIN+] prion protein RNQ1;
DE AltName: Full=Rich in asparagine and glutamine protein 1;
GN Name=RNQ1; OrderedLocusNames=YCL028W; ORFNames=YCL181, YCL28W;
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].
RX PubMed=3302672; DOI=10.1128/mcb.7.7.2316-2328.1987;
RA Trueheart J., Boeke J.D., Fink G.R.;
RT "Two genes required for cell fusion during yeast conjugation: evidence for
RT a pheromone-induced surface protein.";
RL Mol. Cell. Biol. 7:2316-2328(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1897318; DOI=10.1002/yea.320070513;
RA Rad M.R., Luetzenkirchen K., Xu G., Kleinhans U., Hollenberg C.P.;
RT "The complete sequence of a 11,953 bp fragment from C1G on chromosome III
RT encompasses four new open reading frames.";
RL Yeast 7:533-538(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [4]
RP SEQUENCE REVISION TO 360.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-405.
RC STRAIN=SCI11.5/a, SCI11.5/b, SCI11.5/c, SCI11.5/d, SCI16, SCI3, SCI4,
RC SCI7.2/a, SCI7.2/b, SCI7.2/d, SCI9, and SCI9*;
RX PubMed=12890024; DOI=10.1046/j.1365-2958.2003.03608.x;
RA Resende C.G., Outeiro T.F., Sands L., Lindquist S., Tuite M.F.;
RT "Prion protein gene polymorphisms in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 49:1005-1017(2003).
RN [7]
RP PRION FORMATION.
RX PubMed=9335589; DOI=10.1093/genetics/147.2.507;
RA Derkatch I.L., Bradley M.E., Zhou P., Chernoff Y.O., Liebman S.W.;
RT "Genetic and environmental factors affecting the de novo appearance of the
RT [PSI+] prion in Saccharomyces cerevisiae.";
RL Genetics 147:507-519(1997).
RN [8]
RP FUNCTION, IDENTIFICATION AS A PRION, AND AGGREGATION.
RX PubMed=10678178; DOI=10.1016/s1097-2765(00)80412-8;
RA Sondheimer N., Lindquist S.L.;
RT "Rnq1: an epigenetic modifier of protein function in yeast.";
RL Mol. Cell 5:163-172(2000).
RN [9]
RP FUNCTION, AND AGGREGATION.
RX PubMed=11511345; DOI=10.1016/s0092-8674(01)00427-5;
RA Derkatch I.L., Bradley M.E., Hong J.Y., Liebman S.W.;
RT "Prions affect the appearance of other prions: the story of [PIN(+)].";
RL Cell 106:171-182(2001).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
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 [12]
RP PRION PROPAGATION.
RX PubMed=17097676; DOI=10.1016/j.jmb.2006.10.069;
RA Patel B.K., Liebman S.W.;
RT "'Prion-proof' for [PIN+]: infection with in vitro-made amyloid aggregates
RT of Rnq1p-(132-405) induces [PIN+].";
RL J. Mol. Biol. 365:773-782(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-84, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [15]
RP STRUCTURE BY NMR OF 153-405.
RX PubMed=18268327; DOI=10.1073/pnas.0712032105;
RA Wickner R.B., Dyda F., Tycko R.;
RT "Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-
RT register beta-sheet structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2403-2408(2008).
CC -!- FUNCTION: Transferable epigenetic modifier which forms a prion
CC responsible for the non-Mendelian trait [PIN+]. The native function of
CC the soluble protein is unknown. {ECO:0000269|PubMed:10678178,
CC ECO:0000269|PubMed:11511345}.
CC -!- INTERACTION:
CC P25367; P25367: RNQ1; NbExp=6; IntAct=EBI-21708, EBI-21708;
CC P25367; P25294: SIS1; NbExp=2; IntAct=EBI-21708, EBI-17244;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
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.
CC -!- MISCELLANEOUS: [PIN+], also known as [RNQ+], is the prion form of RNQ1
CC (PubMed:10678178). [PIN+] is the result of a conformational change of
CC the cellular RNQ1 protein that becomes self-propagating and infectious.
CC This conformational change generates a form of RNQ1 that assembles into
CC amyloid fibrils (PubMed:17097676). [PIN+] promotes de novo [PSI+]
CC formation upon SUP35 overproduction (cross-seeding) (PubMed:11511345).
CC [PIN+] can be cured by GdnHCl and by deletion of the molecular
CC chaperone HSP104, which is required for [PIN+] propagation
CC (PubMed:10678178). {ECO:0000305|PubMed:10678178,
CC ECO:0000305|PubMed:11511345, ECO:0000305|PubMed:17097676}.
CC -!- MISCELLANEOUS: Present with 1140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA34615.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M16717; AAA34615.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X59720; CAC42958.1; -; Genomic_DNA.
DR EMBL; AY028674; AAK26208.1; -; Genomic_DNA.
DR EMBL; AY028675; AAK26209.1; -; Genomic_DNA.
DR EMBL; AY028676; AAK26210.1; -; Genomic_DNA.
DR EMBL; AY028677; AAK26211.1; -; Genomic_DNA.
DR EMBL; AY028678; AAK26212.1; -; Genomic_DNA.
DR EMBL; AY028679; AAK26213.1; -; Genomic_DNA.
DR EMBL; AY028680; AAK26214.1; -; Genomic_DNA.
DR EMBL; AY028681; AAK26215.1; -; Genomic_DNA.
DR EMBL; AY028682; AAK26216.1; -; Genomic_DNA.
DR EMBL; AY028683; AAK26217.1; -; Genomic_DNA.
DR EMBL; AY028684; AAK26218.1; -; Genomic_DNA.
DR EMBL; AY028685; AAK26219.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07456.1; -; Genomic_DNA.
DR PIR; S19355; S19355.
DR RefSeq; NP_009902.2; NM_001178673.1.
DR AlphaFoldDB; P25367; -.
DR SMR; P25367; -.
DR BioGRID; 30955; 122.
DR DIP; DIP-4323N; -.
DR IntAct; P25367; 38.
DR MINT; P25367; -.
DR STRING; 4932.YCL028W; -.
DR iPTMnet; P25367; -.
DR MaxQB; P25367; -.
DR PaxDb; P25367; -.
DR PRIDE; P25367; -.
DR EnsemblFungi; YCL028W_mRNA; YCL028W; YCL028W.
DR GeneID; 850329; -.
DR KEGG; sce:YCL028W; -.
DR SGD; S000000533; RNQ1.
DR VEuPathDB; FungiDB:YCL028W; -.
DR eggNOG; ENOG502S2FC; Eukaryota.
DR HOGENOM; CLU_702391_0_0_1; -.
DR InParanoid; P25367; -.
DR OMA; GNDDNKY; -.
DR BioCyc; YEAST:G3O-29289-MON; -.
DR PRO; PR:P25367; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25367; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
PE 1: Evidence at protein level;
KW Amyloid; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Prion;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..405
FT /note="[PIN+] prion protein RNQ1"
FT /id="PRO_0000097390"
FT REGION 149..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..402
FT /note="Prion domain (PrD)"
FT REGION 185..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT VARIANT 166..169
FT /note="Missing (in strain: SCI7.2/b, SCI11.5/a and SCI11.5/
FT c)"
FT VARIANT 171..172
FT /note="Missing (in strain: SCI7.2/a, SCI7.2/d, SCI11.5/b
FT and SCI11.5/d)"
FT VARIANT 289..299
FT /note="Missing (in strain: SCI7.2/b, SCI7.2/d and SCI11.5/
FT c)"
FT VARIANT 293..303
FT /note="Missing (in strain: SCI9)"
FT VARIANT 360
FT /note="Q -> H (in strain: SCI3, SCI4, SCI7.2/a, SCI7.2/b,
FT SCI7.2/d, SCI11.5/a, SCI11.5/b, SCI11.5/c and SCI11.5/d)"
FT VARIANT 372
FT /note="P -> PQHNGQQQSNEYGRP (in strain: SCI7.2/b, SCI7.2/d
FT and SCI11.5/c)"
FT VARIANT 383
FT /note="Q -> H (in strain: SCI7.2/b,SCI7.2/d and SCI11.5/c)"
FT VARIANT 387
FT /note="F -> L (in strain: SCI4)"
FT CONFLICT 181
FT /note="A -> T (in Ref. 1; AAA34615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 42580 MW; 8ED9C40A7DF70F7F CRC64;
MDTDKLISEA ESHFSQGNHA EAVAKLTSAA QSNPNDEQMS TIESLIQKIA GYVMDNRSGG
SDASQDRAAG GGSSFMNTLM ADSKGSSQTQ LGKLALLATV MTHSSNKGSS NRGFDVGTVM
SMLSGSGGGS QSMGASGLAA LASQFFKSGN NSQGQGQGQG QGQGQGQGQG QGSFTALASL
ASSFMNSNNN NQQGQNQSSG GSSFGALASM ASSFMHSNNN QNSNNSQQGY NQSYQNGNQN
SQGYNNQQYQ GGNGGYQQQQ GQSGGAFSSL ASMAQSYLGG GQTQSNQQQY NQQGQNNQQQ
YQQQGQNYQH QQQGQQQQQG HSSSFSALAS MASSYLGNNS NSNSSYGGQQ QANEYGRPQQ
NGQQQSNEYG RPQYGGNQNS NGQHESFNFS GNFSQQNNNG NQNRY
