CUE3_YEAST
ID CUE3_YEAST Reviewed; 624 AA.
AC P53137; D6VU37;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=RQC trigger complex subunit CUE3 {ECO:0000303|PubMed:28757607};
DE AltName: Full=CUE domain-containing protein 3;
DE AltName: Full=Coupling of ubiquitin conjugation to ER degradation protein 3;
GN Name=CUE3; Synonyms=RQT3 {ECO:0000303|PubMed:28757607};
GN OrderedLocusNames=YGL110C; ORFNames=G3060;
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=9046090;
RX DOI=10.1002/(sici)1097-0061(199701)13:1<85::aid-yea53>3.0.co;2-e;
RA Paoluzi S., Minenkova O., Castagnoli L.;
RT "The genes encoding the transcription factor yTAFII60, the G4p1 protein and
RT a putative glucose transporter are contained in a 12.3 kb DNA fragment on
RT the left arm of Saccharomyces cerevisiae chromosome VII.";
RL Yeast 13:85-91(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
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 [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, 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 [7]
RP FUNCTION, IDENTIFICATION IN THE RQT COMPLEX, INTERACTION WITH UBIQUITIN;
RP SLH1; RQT4 AND HEL2, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 328-PHE--LEU-341.
RX PubMed=28757607; DOI=10.1038/s41467-017-00188-1;
RA Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T.,
RA Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R.,
RA Inada T.;
RT "Ubiquitination of stalled ribosome triggers ribosome-associated quality
RT control.";
RL Nat. Commun. 8:159-159(2017).
RN [8]
RP FUNCTION, INTERACTION WITH RQT4, AND DISRUPTION PHENOTYPE.
RX PubMed=28223409; DOI=10.1261/rna.060897.117;
RA Sitron C.S., Park J.H., Brandman O.;
RT "Asc1, Hel2, and Slh1 couple translation arrest to nascent chain
RT degradation.";
RL RNA 23:798-810(2017).
RN [9]
RP FUNCTION, AND IDENTIFICATION IN THE RQT COMPLEX.
RX PubMed=32203490; DOI=10.1038/s41594-020-0393-9;
RA Matsuo Y., Tesina P., Nakajima S., Mizuno M., Endo A., Buschauer R.,
RA Cheng J., Shounai O., Ikeuchi K., Saeki Y., Becker T., Beckmann R.,
RA Inada T.;
RT "RQT complex dissociates ribosomes collided on endogenous RQC substrate
RT SDD1.";
RL Nat. Struct. Mol. Biol. 27:323-332(2020).
CC -!- FUNCTION: Involved in activation of the ribosome quality control (RQC)
CC pathway, a pathway that degrades nascent peptide chains during
CC problematic translation (PubMed:28757607, PubMed:28223409,
CC PubMed:32203490). As part of the ribosome quality control trigger (RQT)
CC complex, recognizes HEL2-dependent ubiquitination of RPS20 on stalled
CC ribosomes (PubMed:28757607). {ECO:0000269|PubMed:28223409,
CC ECO:0000269|PubMed:28757607, ECO:0000269|PubMed:32203490}.
CC -!- SUBUNIT: Component of the RQT (ribosome quality control trigger)
CC complex, composed of SLH1, CUE3, and RQT4 (PubMed:28757607,
CC PubMed:32203490). Interacts with ubiquitin; the interaction is direct
CC (PubMed:28757607). Interacts with SLH1 (PubMed:28757607). Interacts
CC with RQT4 (PubMed:28757607, PubMed:28223409). Interacts with HEL2
CC (PubMed:28757607). Associates with translating ribosomes
CC (PubMed:28757607, PubMed:28223409). {ECO:0000269|PubMed:28223409,
CC ECO:0000269|PubMed:28757607, ECO:0000269|PubMed:32203490}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Defective activation of the ribosome quality
CC control (RQC) pathway (PubMed:28757607). Mildly defective ribosome
CC stalling induced by RNA arrest sequences (PubMed:28223409). Sensitive
CC to anisomycin (stalls ribosomes in the rotated state)
CC (PubMed:28757607). {ECO:0000269|PubMed:28223409,
CC ECO:0000269|PubMed:28757607}.
CC -!- MISCELLANEOUS: Present with 6300 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X97644; CAA66242.1; -; Genomic_DNA.
DR EMBL; Z72632; CAA96817.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07998.1; -; Genomic_DNA.
DR PIR; S64118; S64118.
DR RefSeq; NP_011405.1; NM_001180975.1.
DR AlphaFoldDB; P53137; -.
DR SMR; P53137; -.
DR BioGRID; 33141; 118.
DR ComplexPortal; CPX-6643; RQT ribosome-associated quality control trigger complex.
DR DIP; DIP-5379N; -.
DR IntAct; P53137; 2.
DR MINT; P53137; -.
DR STRING; 4932.YGL110C; -.
DR iPTMnet; P53137; -.
DR MaxQB; P53137; -.
DR PaxDb; P53137; -.
DR PRIDE; P53137; -.
DR EnsemblFungi; YGL110C_mRNA; YGL110C; YGL110C.
DR GeneID; 852768; -.
DR KEGG; sce:YGL110C; -.
DR SGD; S000003078; CUE3.
DR VEuPathDB; FungiDB:YGL110C; -.
DR eggNOG; ENOG502RV3A; Eukaryota.
DR HOGENOM; CLU_030292_0_0_1; -.
DR InParanoid; P53137; -.
DR OMA; EGWARMI; -.
DR BioCyc; YEAST:G3O-30608-MON; -.
DR PRO; PR:P53137; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53137; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:UniProtKB.
DR GO; GO:0032790; P:ribosome disassembly; IC:ComplexPortal.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR CDD; cd14373; CUE_Cue3p_like; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR041808; Cue3_CUE.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR PROSITE; PS51140; CUE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..624
FT /note="RQC trigger complex subunit CUE3"
FT /id="PRO_0000202749"
FT DOMAIN 316..359
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 366..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..615
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 328..341
FT /note="FPQFSKYQLSQTLL->AAQFSKYQLSQTAA: Abolishes ubiquitin
FT binding. Defective activation of the ribosome quality
FT control (RQC) pathway."
FT /evidence="ECO:0000269|PubMed:28757607"
SQ SEQUENCE 624 AA; 72043 MW; 9A1F679562A367E3 CRC64;
MLSRYNRVIE INGGNADISL PIVKFPPFKL RAQLIEKDPV VWLHLIETYV TYFEYLMQGA
NVELLDESTL DHLRLFLRTY LHEIADEEGK LLSLGINHDV SEQLYLLKGW IFSLIKKCGL
LHLQIFGDSL WNLIKVYVRR NPDSIRGLID GSLKPRINTQ RVQLDKSYQV QQHLKQLIES
GKFKRIDLRC VEDLLSAKSM QPNKFAENFF TANWIEILEA LWAKGQGRGH KEARELIIIS
LFSVSADRLL KITKELGISN FETLALYPLL GTMLINEGVH KRLPDLKSKL LFLNLGGLSM
DEGDHMSYPT SSGTEVNEEQ LSALMELFPQ FSKYQLSQTL LAYDNNIELV TNKIFEDPTI
IEAFSREPAE EEVEPVSDGD NASFTEELSI LDRGDSSKNK ELDKKIISEG VPDELRNKTL
TRALKLLYEA DEDERDDTYD EADVNRSDPS KRIGLQEDEE SYDTKDDSNE VRQDHNYHIV
EAYLWNLLKE DPKLFERSKR GTKVRKTMKE MTSWSDEKIE GWCRMLERSP TRARLLEKKF
MFKGNSKTGK TSYVHNRDSQ NDGNVVKEQA KQKKSENIKK HEPQSTEQKK RQHAKNEKRK
GARANHNRKK GHDKKLARAG NNAI
