RQT4_YEAST
ID RQT4_YEAST Reviewed; 530 AA.
AC P36119; D6VX88;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=RQC trigger complex subunit RQT4 {ECO:0000303|PubMed:28757607};
GN Name=RQT4 {ECO:0000303|PubMed:28757607}; OrderedLocusNames=YKR023W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434 AND SER-457, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; SER-431 AND SER-434, 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 [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-509, AND IDENTIFICATION BY
RP 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 [8]
RP FUNCTION, IDENTIFICATION IN THE RQT COMPLEX, INTERACTION WITH SLH1; CUE3
RP AND HEL2, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [9]
RP FUNCTION, INTERACTION WITH CUE3, SUBCELLULAR LOCATION, AND DISRUPTION
RP 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 [10]
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: Functions as part of the RQC trigger (RQT) complex that
CC activates the ribosome quality control (RQC) pathway, a pathway that
CC degrades nascent peptide chains during problematic translation.
CC {ECO:0000269|PubMed:28223409, ECO:0000269|PubMed:28757607,
CC 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 SLH1 (PubMed:28757607). Interacts with
CC CUE3 (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, cytosol {ECO:0000305|PubMed:28223409,
CC ECO:0000305|PubMed:28757607}.
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 1710 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z28248; CAA82095.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09178.1; -; Genomic_DNA.
DR PIR; S38092; S38092.
DR RefSeq; NP_012948.3; NM_001179813.3.
DR AlphaFoldDB; P36119; -.
DR BioGRID; 34155; 75.
DR ComplexPortal; CPX-6643; RQT ribosome-associated quality control trigger complex.
DR DIP; DIP-6275N; -.
DR IntAct; P36119; 7.
DR MINT; P36119; -.
DR STRING; 4932.YKR023W; -.
DR iPTMnet; P36119; -.
DR MaxQB; P36119; -.
DR PaxDb; P36119; -.
DR PRIDE; P36119; -.
DR EnsemblFungi; YKR023W_mRNA; YKR023W; YKR023W.
DR GeneID; 853893; -.
DR KEGG; sce:YKR023W; -.
DR SGD; S000001731; YKR023W.
DR VEuPathDB; FungiDB:YKR023W; -.
DR eggNOG; KOG2845; Eukaryota.
DR GeneTree; ENSGT00390000005300; -.
DR HOGENOM; CLU_042447_0_0_1; -.
DR InParanoid; P36119; -.
DR OMA; YACNCQA; -.
DR BioCyc; YEAST:G3O-31999-MON; -.
DR PRO; PR:P36119; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36119; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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 InterPro; IPR039128; TRIP4-like.
DR InterPro; IPR009349; Znf_C2HC5.
DR PANTHER; PTHR12963; PTHR12963; 1.
DR Pfam; PF06221; zf-C2HC5; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..530
FT /note="RQC trigger complex subunit RQT4"
FT /id="PRO_0000203202"
FT REGION 75..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 530 AA; 60799 MW; 57515FA658E7535A CRC64;
MTRKQAIDYA IKQVPQILPL EESDVKALCE QVLSTSSDDP EQIASKFLEF LGHEDLSFEF
VMKFNELLNQ NDKKEEKKTK NVHLEHTAPT SWKNESKQPT NNYINKKGDE KPKKLKDEKK
SSTTRPTVQP SNQSTQSNPI KEKKEHRSKG KLQSLQEIDE AIKMLELRDS GSSKNCNCQG
TRHPVFDIAP NCLHCGKVVC VIEGLNKGKC GHCHEQLISD NERTQMVEIL NQEKNELNGS
SSSLSNASNG ANVPKKKTKT YKITSGMGKN LFAEQDKLFD FIERKRERER KRNEVLKLQE
EKEESEAKER QASEHDHKAE ENPELLAAQE RLDRLLYFQD TSAERTKIID NASDFDMNQE
VGLWGSARER ALALKKQQRN LRKWEKVEKE RNGRREKYVV SMNIGSNGKV TMTEVPKDTE
NVIAGSDDDI SDISDEEDIS DLKHIHALKS EINTTKSLEN LHLQSKAWDY ERDKKQFDRP
TYVKKNSDTA QQNRKTEEKA HDMQAYDLKS RVQVDQNADA SVEQNILAVL
