GPCRDB: Swiss-Prot entry
ID RNQ1_YEAST STANDARD; PRT; 405 AA.
AC P25367; Q8NKJ9; Q8TF94; Q8TFA2; Q8TFC8; Q8TFP4; Q8TFP5; Q8TFP6;
AC Q8TFP7; Q8TFP8;
DT 01-MAY-1992 (Rel. 22, Created)
DT 05-JUL-2004 (Rel. 44, Last sequence update)
DT 01-FEB-2005 (Rel. 46, Last annotation update)
DE [PIN+] prion protein RNQ1 (Rich in asparagine and glutamine protein
DE 1).
GN Name=RNQ1; OrderedLocusNames=YCL028W; ORFNames=YCL28W, YCL181;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=87286864; PubMed=3302672 [NCBI, ExPASy, EBI, Israel, Japan];
RA Trueheart J., Boeke J.D., Fink G.R.;
RT "Two genes required for cell fusion during yeast conjugation: evidence
RT for a pheromone-induced surface protein.";
RL Mol. Cell. Biol. 7:2316-2328(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=91377317; PubMed=1897318 [NCBI, ExPASy, EBI, Israel, Japan];
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
RT III encompasses four new open reading frames.";
RL Yeast 7:533-538(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c;
RX MEDLINE=92244356; PubMed=1574125 [NCBI, ExPASy, EBI, Israel, Japan]; 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.J.P., Brown R., Buhler J.-M.,
RA Carignani G., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B.,
RA De Haan M., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E.,
RA Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C.A., Faye G., Feldmann H., Fiers W.,
RA Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
RA Fuller L.J., Gent M.E., Gigot D., Gilliquet V., Glansdorff N.,
RA Goffeau A., Grenson M., Grisanti P., Grivell L.A., Haasemann M.,
RA Hatat D., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S.,
RA Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jackman P.,
RA Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A.,
RA Kleinhans U., Kreisl P., Lafranchi G., Lewis C., van der Linden C.G.,
RA Lucchini G., Lutzenkirchen K., Maat C., Mannhaupt G., Manzano M.E.,
RA Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A.,
RA Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Navas L.,
RA Newlon C.S., Olson M.V., Pallier C., Panzeri L., Pearson B.M.,
RA Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P.,
RA Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F.,
RA Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B.,
RA Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C.,
RA Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A.,
RA Thireos G., Triano L.N., Urrestarazu L.A., Valle G., Vetter I.,
RA van Vliet-Reedijk J.C., Volckaert G., Vreken P., Warmington J.R.,
RA von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G.,
RA Zimmermann F.K., 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 NUCLEOTIDE SEQUENCE 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 MEDLINE=22773310; PubMed=12890024 [NCBI, ExPASy, EBI, Israel, Japan];
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 [6]
RP FUNCTION, IDENTIFICATION AS A PRION, AND AGGREGATION.
RX PubMed=10678178 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S1097-2765(00)80412-8;
RA Sondheimer N., Lindquist S.;
RT "Rnq1: an epigenetic modifier of protein function in yeast.";
RL Mol. Cell 5:163-172(2000).
RN [7]
RP FUNCTION, AND AGGREGATION.
RX MEDLINE=21402415; PubMed=11511345 [NCBI, ExPASy, EBI, Israel, Japan]; 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
RT [PIN(+)].";
RL Cell 106:171-182(2001).
RN [8]
RP SUBCELLULAR LOCATION.
RX MEDLINE=22923954; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]; 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).
CC -!- FUNCTION: Transferable epigenetic modifier which forms a prion
CC responsible for the non-Mendelian trait [PIN(+)]. Exists in
CC nonprion soluble and insoluble aggregate states. The heritable
CC insoluble prion state is dominant and requires the presence of
CC HSP104 chaperone. The heritable form is transmitted between cells
CC through the cytoplasm and inherited in a non-Mendelian manner.
CC -!- SUBUNIT: Aggregates to form fibers. Shows self-seeded process of
CC protein polymerization. The de novo appearance of aggregates
CC requires the precence of other prions.
CC -!- SUBCELLULAR LOCATION: Nuclear and cytoplasmic.
CC -!- CAUTION: Ref.1 sequence differs from that shown due to a
CC frameshift in position 323.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; M16717; AAA34615.1; ALT_FRAME. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X59720; CAC42958.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028674; AAK26208.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028675; AAK26209.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028676; AAK26210.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028677; AAK26211.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028678; AAK26212.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028679; AAK26213.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028680; AAK26214.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028681; AAK26215.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028682; AAK26216.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028683; AAK26217.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028684; AAK26218.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AY028685; AAK26219.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; S19355; S19355.
DR IntAct; P25367; -.
DR GermOnline; 138864; -.
DR SGD; S000000533; RNQ1.
DR GO; GO:0005829; C:cytosol; IDA.
DR CMR; P25367.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR BLOCKS; P25367.
DR ProtoNet; P25367.
DR ProtoMap; P25367.
DR PRESAGE; P25367.
DR DIP; P25367.
DR ModBase; P25367.
DR SMR; P25367.
DR GeneCensus; YCL028W.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Complete proteome; Nuclear protein; Prion.
FT DOMAIN 153 402 Gln-rich.
FT DOMAIN 186 246 Asn-rich.
FT VARIANT 166 169 Missing (in strain SCI7.2/b, strain
FT SCI11.5/a and strain SCI11.5/c).
FT VARIANT 171 172 Missing (in strain SCI7.2/a, strain
FT SCI7.2/d, strain SCI11.5/b and strain
FT SCI11.5/d).
FT VARIANT 289 299 Missing (in strain SCI7.2/b, strain
FT SCI7.2/d and strain SCI11.5/c).
FT VARIANT 293 303 Missing (in strain SCI9).
FT VARIANT 360 360 Q -> H (in strain SCI3, strain SCI4,
FT strain SCI7.2/a, strain SCI7.2/b, strain
FT SCI7.2/d, strain SCI11.5/a, strain
FT SCI11.5/b, strain SCI11.5/c and strain
FT SCI11.5/d).
FT VARIANT 372 372 P -> PQHNGQQQSNEYGRP (in strain SCI7.2/b,
FT strain SCI7.2/d and strain SCI11.5/c).
FT VARIANT 383 383 Q -> H (in strain SCI7.2/b,strain SCI7.2/
FT d and strain SCI11.5/c).
FT VARIANT 387 387 F -> L (in strain SCI4).
FT CONFLICT 181 181 A -> T (in Ref. 1).
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
//