RQC2_YEAST
ID RQC2_YEAST Reviewed; 1038 AA.
AC Q12532; D6W403;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ribosome quality control complex subunit 2 {ECO:0000303|PubMed:25554787};
DE AltName: Full=Translation-associated element 2 {ECO:0000303|PubMed:20691087};
GN Name=RQC2 {ECO:0000303|PubMed:25554787};
GN Synonyms=TAE2 {ECO:0000303|PubMed:20691087}; OrderedLocusNames=YPL009C;
GN ORFNames=YP8132.04C;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 IDENTIFICATION BY MASS SPECTROMETRY, AND ASSOCIATION WITH RIBOSOMES.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [6]
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797, AND IDENTIFICATION BY
RP 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 [8]
RP FUNCTION.
RX PubMed=20691087; DOI=10.1186/1472-6769-10-6;
RA Alamgir M., Erukova V., Jessulat M., Azizi A., Golshani A.;
RT "Chemical-genetic profile analysis of five inhibitory compounds in yeast.";
RL BMC Chem. Biol. 10:6-6(2010).
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 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).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25349383; DOI=10.1073/pnas.1413882111;
RA Lyumkis D., Oliveira dos Passos D., Tahara E.B., Webb K., Bennett E.J.,
RA Vinterbo S., Potter C.S., Carragher B., Joazeiro C.A.;
RT "Structural basis for translational surveillance by the large ribosomal
RT subunit-associated protein quality control complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:15981-15986(2014).
RN [12]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-9; ASP-98 AND ARG-99.
RX PubMed=25554787; DOI=10.1126/science.1259724;
RA Shen P.S., Park J., Qin Y., Li X., Parsawar K., Larson M.H., Cox J.,
RA Cheng Y., Lambowitz A.M., Weissman J.S., Brandman O., Frost A.;
RT "Protein synthesis. Rqc2p and 60S ribosomal subunits mediate mRNA-
RT independent elongation of nascent chains.";
RL Science 347:75-78(2015).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF ARG-88; ASP-98 AND LYS-534.
RX PubMed=32934225; DOI=10.1038/s41467-020-18327-6;
RA Martin P.B., Kigoshi-Tansho Y., Sher R.B., Ravenscroft G., Stauffer J.E.,
RA Kumar R., Yonashiro R., Mueller T., Griffith C., Allen W., Pehlivan D.,
RA Harel T., Zenker M., Howting D., Schanze D., Faqeih E.A.,
RA Almontashiri N.A.M., Maroofian R., Houlden H., Mazaheri N., Galehdari H.,
RA Douglas G., Posey J.E., Ryan M., Lupski J.R., Laing N.G., Joazeiro C.A.P.,
RA Cox G.A.;
RT "NEMF mutations that impair ribosome-associated quality control are
RT associated with neuromuscular disease.";
RL Nat. Commun. 11:4625-4625(2020).
CC -!- FUNCTION: As part of the ribosome quality control complex (RQC), a
CC ribosome-associated complex, mediates the extraction of incompletely
CC synthesized nascent chains from stalled ribosomes as well as their
CC ubiquitin-mediated proteasomal degradation. Thereby, frees ribosomes
CC from the stalled translation complex and prevents the accumulation of
CC nascent polypeptide chains that are potentially toxic for the cell
CC (PubMed:23178123). RQC2 is responsible for selective recognition of
CC stalled 60S subunits by recognizing an exposed, nascent chain-
CC conjugated tRNA moiety (PubMed:25349383). RQC2 is important for the
CC stable association of the E3 ubiquitin-protein ligase RKR1/LTN1 to the
CC complex (PubMed:23479637). RQC2 is also able to recruit alanine- and
CC threonine-charged tRNA to the A site and directs the elongation of
CC stalled nascent chains independently of mRNA or 40S subunits, leading
CC to non-templated C-terminal Ala and Thr extensions (CAT tails)
CC (PubMed:25554787, PubMed:32934225). CAT tails induce a HSF1-dependent
CC heat shock response (PubMed:25554787). CAT tails also promote the
CC RKR1/LTN1-mediated ubiquitination of incompletely synthesized nascent
CC polypeptides and their subsequent proteasomal degradation
CC (PubMed:32934225). {ECO:0000269|PubMed:20691087,
CC ECO:0000269|PubMed:23178123, ECO:0000269|PubMed:23479637,
CC ECO:0000269|PubMed:25349383, ECO:0000269|PubMed:25554787,
CC ECO:0000269|PubMed:32934225}.
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 associated with the 60S
CC ribosomal subunit (PubMed:23178123, PubMed:23479637, PubMed:25349383).
CC RQC2 binds to the 40S-binding surface of tRNAs (PubMed:25554787).
CC {ECO:0000269|PubMed:23178123, ECO:0000269|PubMed:23479637,
CC ECO:0000269|PubMed:25349383, ECO:0000269|PubMed:25554787}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000305}.
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DR EMBL; U33335; AAB68096.1; -; Genomic_DNA.
DR EMBL; Z48483; CAA88377.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA95032.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11419.1; -; Genomic_DNA.
DR PIR; S52522; S52522.
DR RefSeq; NP_015316.1; NM_001183823.1.
DR AlphaFoldDB; Q12532; -.
DR SMR; Q12532; -.
DR BioGRID; 36168; 198.
DR ComplexPortal; CPX-3265; Ribosome quality control complex.
DR DIP; DIP-6570N; -.
DR IntAct; Q12532; 21.
DR MINT; Q12532; -.
DR STRING; 4932.YPL009C; -.
DR iPTMnet; Q12532; -.
DR MaxQB; Q12532; -.
DR PaxDb; Q12532; -.
DR PRIDE; Q12532; -.
DR EnsemblFungi; YPL009C_mRNA; YPL009C; YPL009C.
DR GeneID; 856098; -.
DR KEGG; sce:YPL009C; -.
DR SGD; S000005930; RQC2.
DR VEuPathDB; FungiDB:YPL009C; -.
DR eggNOG; KOG2030; Eukaryota.
DR GeneTree; ENSGT00390000018516; -.
DR HOGENOM; CLU_003612_1_1_1; -.
DR InParanoid; Q12532; -.
DR OMA; MGAWWVN; -.
DR BioCyc; YEAST:G3O-33928-MON; -.
DR PRO; PR:Q12532; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12532; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:1990112; C:RQC complex; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0043023; F:ribosomal large subunit binding; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0140708; P:CAT tailing; IMP:UniProtKB.
DR GO; GO:0043043; P:peptide biosynthetic process; IMP: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:UniProtKB.
DR InterPro; IPR021846; NFACT-C.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR Pfam; PF11923; NFACT-C; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1038
FT /note="Ribosome quality control complex subunit 2"
FT /id="PRO_0000244627"
FT REGION 459..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 350..383
FT /evidence="ECO:0000255"
FT COILED 713..768
FT /evidence="ECO:0000255"
FT COILED 830..912
FT /evidence="ECO:0000255"
FT COMPBIAS 482..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..760
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 9
FT /note="D->A: Abolishes CAT tail synthesis and heat shock
FT response, but still binds to 60S ribosomal subunits and
FT supports LTN1-dependent ubiquitination of nascent chains;
FT when associated with A-98 and A-99."
FT /evidence="ECO:0000269|PubMed:25554787"
FT MUTAGEN 88
FT /note="R->S: No effect on protein abundance. Decreased CAT
FT tail synthesis. No effect on ribosome-associated ubiquitin-
FT dependent protein catabolic process."
FT /evidence="ECO:0000269|PubMed:32934225"
FT MUTAGEN 98
FT /note="D->A: Abolishes CAT tail synthesis and heat shock
FT response, but still binds to 60S ribosomal subunits and
FT supports LTN1-dependent ubiquitination of nascent chains;
FT when associated with A-9 and A-99."
FT /evidence="ECO:0000269|PubMed:25554787"
FT MUTAGEN 98
FT /note="D->Y: No effect on protein abundance. Loss of CAT
FT tail synthesis. Loss of ribosome-associated ubiquitin-
FT dependent protein catabolic process."
FT /evidence="ECO:0000269|PubMed:32934225"
FT MUTAGEN 99
FT /note="R->A: Abolishes CAT tail synthesis and heat shock
FT response, but still binds to 60S ribosomal subunits and
FT supports LTN1-dependent ubiquitination of nascent chains;
FT when associated with A-9 and A-98."
FT /evidence="ECO:0000269|PubMed:25554787"
FT MUTAGEN 534
FT /note="K->G: No effect on protein abundance. Decreased CAT
FT tail synthesis."
FT /evidence="ECO:0000269|PubMed:32934225"
SQ SEQUENCE 1038 AA; 119069 MW; C0ADE76922F26BE0 CRC64;
MKQRISALDL LLLARELKQD LEGYRLSNIY NIADSSKQFL LKFNKPDSKL NVVVDCGLRI
YLTEFSRPIP PTPSGFVVKL RKHLKAKRLT ALKQVDQDRI LVLQFADGHF YLVLEFFSAG
NVILLDENRR IMALQRVVLE HENKVGQIYE MFDESLFTTN NESADESIEK NRKAEYTSEL
VNEWIKAVQA KYESDITVIK QLNIQGKEGA KKKKVKVPSI HKLLLSKVPH LSSDLLSKNL
KVFNIDPSES CLNLLEETDS LAELLNSTQL EYNQLLTTTD RKGYILAKRN ENYISEKDTA
DLEFIYDTFH PFKPYINGGD TDSSCIIEVE GPYNRTLDKF FSTIESSKYA LRIQNQESQA
QKKIDDARAE NDRKIQALLD VQELNERKGH LIIENAPLIE EVKLAVQGLI DQQMDWNTIE
KLIKSEQKKG NRIAQLLNLP LNLKQNKISV KLDLSSKELN TSSDEDNESE GNTTDSSSDS
DSEDMESSKE RSTKSMKRKS NEKINVTIDL GLSAYANATE YFNIKKTSAQ KQKKVEKNVG
KAMKNIEVKI DQQLKKKLKD SHSVLKKIRT PYFFEKYSWF ISSEGFLVMM GKSPAETDQI
YSKYIEDDDI YMSNSFNSHV WIKNPEKTEV PPNTLMQAGI LCMSSSEAWS KKISSSPWWC
FAKNVSKFDG SDNSILPEGA FRLKNENDQN HLPPAQLVMG FGFLWKVKTS GNEDNGDDDE
EEEEEEEEEE EEEEEEEEEE EEEKEEEEKE EEQQQDEDDS NEVNGLEKGG DSNDSTKNNS
FEHDNLEKDI EKHCTISSDT DSDSGNAKAK NDNSSTQRIL DEPGVPISLI ENINSNVRGK
RGKLKKIQKK YADQDETERL LRLEALGTLK GIEKQQQRKK EEIMKREVRE DRKNKREKQR
RLQALKFTKK EKARVNYDKH KSELKPSLDK GDVVDDIIPV FAPWPALLKY KYKVKIQPGS
AKKTKTLTEI LHYFKSRPLD GSSTDNEMDW PQEHEMIKGL KEQDLVLLLC VDKLKVTIAG
QKSTKNGGNS SKKGKKKR
