RQC1_YEAST
ID RQC1_YEAST Reviewed; 723 AA.
AC Q05468; D6VSW5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ribosome quality control complex subunit 1 {ECO:0000303|PubMed:23178123};
GN Name=RQC1 {ECO:0000303|PubMed:23178123};
GN OrderedLocusNames=YDR333C {ECO:0000312|SGD:S000002741};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; THR-158 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; THR-158 AND SER-160, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=23178123; DOI=10.1016/j.cell.2012.10.044;
RA Brandman O., Stewart-Ornstein J., Wong D., Larson A., Williams C.C.,
RA Li G.W., Zhou S., King D., Shen P.S., Weibezahn J., Dunn J.G., Rouskin S.,
RA Inada T., Frost A., Weissman J.S.;
RT "A ribosome-bound quality control complex triggers degradation of nascent
RT peptides and signals translation stress.";
RL Cell 151:1042-1054(2012).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=23479637; DOI=10.1073/pnas.1221724110;
RA Defenouillere Q., Yao Y., Mouaikel J., Namane A., Galopier A., Decourty L.,
RA Doyen A., Malabat C., Saveanu C., Jacquier A., Fromont-Racine M.;
RT "Cdc48-associated complex bound to 60S particles is required for the
RT clearance of aberrant translation products.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5046-5051(2013).
CC -!- FUNCTION: Component of the ribosome quality control complex (RQC), a
CC ribosome-associated complex that mediates ubiquitination and extraction
CC of incompletely synthesized nascent chains for proteasomal degradation
CC (PubMed:23178123). RQC1 is essential for the recruitment of CDC48 to
CC ribosomal subunits (PubMed:23479637). {ECO:0000269|PubMed:23178123,
CC ECO:0000269|PubMed:23479637}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC composed of the E3 ubiquitin ligase RKR1/LTN1, RQC1 and RQC2, as well
CC as CDC48 and its ubiquitin-binding cofactors. RQC forms a stable
CC complex with 60S ribosomal subunits (PubMed:23178123, PubMed:23479637).
CC {ECO:0000269|PubMed:23178123, ECO:0000269|PubMed:23479637}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TCF25 family. {ECO:0000305}.
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DR EMBL; U51032; AAB64769.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12175.1; -; Genomic_DNA.
DR PIR; S70098; S70098.
DR RefSeq; NP_010620.3; NM_001180641.3.
DR AlphaFoldDB; Q05468; -.
DR BioGRID; 32390; 108.
DR ComplexPortal; CPX-3265; Ribosome quality control complex.
DR DIP; DIP-4004N; -.
DR IntAct; Q05468; 20.
DR STRING; 4932.YDR333C; -.
DR iPTMnet; Q05468; -.
DR MaxQB; Q05468; -.
DR PaxDb; Q05468; -.
DR PRIDE; Q05468; -.
DR EnsemblFungi; YDR333C_mRNA; YDR333C; YDR333C.
DR GeneID; 851933; -.
DR KEGG; sce:YDR333C; -.
DR SGD; S000002741; RQC1.
DR VEuPathDB; FungiDB:YDR333C; -.
DR eggNOG; KOG2422; Eukaryota.
DR GeneTree; ENSGT00390000005563; -.
DR HOGENOM; CLU_008321_1_1_1; -.
DR InParanoid; Q05468; -.
DR OMA; WPPLTKN; -.
DR BioCyc; YEAST:G3O-29889-MON; -.
DR PRO; PR:Q05468; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05468; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:1990112; C:RQC complex; IDA:SGD.
DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:SGD.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR InterPro; IPR006994; TCF25/Rqc1.
DR PANTHER; PTHR22684; PTHR22684; 1.
DR Pfam; PF04910; Tcf25; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..723
FT /note="Ribosome quality control complex subunit 1"
FT /id="PRO_0000253842"
FT REGION 21..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..108
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 158
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 723 AA; 83426 MW; 8280829BF3A802DB CRC64;
MSSRALRRLQ DDNALLESLL SNSNANKMTS GKSTAGNIQK RENIFSMMNN VRDSDNSTDE
GQMSEQDEEA AAAGERDTQS NGQPKRITLA SKSSRRKKNK KAKRKQKNHT AEAAKDKGSD
DDDDDEEFDK IIQQFKKTDI LKYGKTKNDD TNEEGFFTAS EPEEASSQPW KSFLSLESDP
GFTKFPISCL RHSCKFFQND FKKLDPHTEF KLLFDDISPE SLEDIDSMTS TPVSPQQLKQ
IQRLKRLIRN WGGKDHRLAP NGPGMHPQHL KFTKIRDDWI PTQRGELSMK LLSSDDLLDW
QLWERPLDWK DVIQNDVSQW QKFISFYKFE PLNSDLSKKS MMDFYLSVIV HPDHEALINL
ISSKFPYHVP GLLQVALIFI RQGDRSNTNG LLQRALFVFD RALKANIIFD SLNCQLPYIY
FFNRQFYLAI FRYIQSLAQR GVIGTASEWT KVLWSLSPLE DPLGCRYFLD HYFLLNNDYQ
YIIELSNSPL MNCYKQWNTL GFSLAVVLSF LRINEMSSAR NALLKAFKHH PLQLSELFKE
KLLGDHALTK DLSIDGHSAE NLELKAYMAR FPLLWNRNEE VTFLHDEMSS ILQDYHRGNV
TIDSNDGQDH NNINNLQSPF FIAGIPINLL RFAILSEESS VMAAIPSFIW SDNEVYEFDV
LPPMPTSKES IEVVENIKTF INEKDLAVLQ AERMQDEDLL NQIRQISLQQ YIHENEESNE
NEG
