ERF1_YEAST
ID ERF1_YEAST Reviewed; 437 AA.
AC P12385; D6VQD9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE Short=Eukaryotic release factor 1;
DE Short=eRF1;
DE AltName: Full=Omnipotent suppressor protein 1;
GN Name=SUP45; Synonyms=SAL4, SUP1; OrderedLocusNames=YBR143C;
GN ORFNames=YBR1120;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=3526282; DOI=10.1093/nar/14.13.5187;
RA Breining P., Piepersberg W.;
RT "Yeast omnipotent suppressor SUP1 (SUP45): nucleotide sequence of the
RT wildtype and a mutant gene.";
RL Nucleic Acids Res. 14:5187-5197(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3037308;
RA Surguchev A.P., Telkov M.V., Smirnov V.N., Breining P., Piepersberg W.;
RT "Nucleotide sequence of mutant and wild-type alelles of the SUP1 gene and
RT comparison of transcripts of SUP1 and SUP2 genes.";
RL Mol. Biol. (Mosk.) 21:347-358(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-432.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=8109177; DOI=10.1002/yea.320091115;
RA Miosga T., Zimmermann F.K.;
RT "Sequence and function analysis of a 2.73 kb fragment of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 9:1273-1277(1993).
RN [6]
RP FUNCTION.
RX PubMed=7556078; DOI=10.1002/j.1460-2075.1995.tb00111.x;
RA Stansfield I., Jones K.M., Kushnirov V.V., Dagkesamanskaya A.R.,
RA Poznyakovski A.I., Paushkin S.V., Nierras C.R., Cox B.S.,
RA Ter-Avanesyan M.D., Tuite M.F.;
RT "The products of the SUP45 (eRF1) and SUP35 genes interact to mediate
RT translation termination in Saccharomyces cerevisiae.";
RL EMBO J. 14:4365-4373(1995).
RN [7]
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 [8]
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 [9]
RP METHYLATION AT GLN-182, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15509572; DOI=10.1074/jbc.m407252200;
RA Heurgue-Hamard V., Champ S., Mora L., Merkulova-Rainon T., Kisselev L.L.,
RA Buckingham R.H.;
RT "The glutamine residue of the conserved GGQ motif in Saccharomyces
RT cerevisiae release factor eRF1 is methylated by the product of the YDR140w
RT gene.";
RL J. Biol. Chem. 280:2439-2445(2005).
RN [10]
RP INTERACTION WITH TPA1.
RX PubMed=16809762; DOI=10.1128/mcb.02448-05;
RA Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M.;
RT "Tpa1p is part of an mRNP complex that influences translation termination,
RT mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 26:5237-5248(2006).
RN [11]
RP METHYLATION AT GLN-182, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16321977; DOI=10.1074/jbc.m507651200;
RA Polevoda B., Span L., Sherman F.;
RT "The yeast translation release factors Mrf1p and Sup45p (eRF1) are
RT methylated, respectively, by the methyltransferases Mtq1p and Mtq2p.";
RL J. Biol. Chem. 281:2562-2571(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, 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 [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-331, 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).
CC -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA.
CC {ECO:0000250, ECO:0000269|PubMed:7556078}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP. Interacts
CC with TPA1. {ECO:0000269|PubMed:16809762}.
CC -!- INTERACTION:
CC P12385; Q03195: RLI1; NbExp=5; IntAct=EBI-6533, EBI-35146;
CC P12385; P05453: SUP35; NbExp=4; IntAct=EBI-6533, EBI-6540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: N5-methylated on Gln-182 by MTQ2. {ECO:0000269|PubMed:15509572,
CC ECO:0000269|PubMed:16321977}.
CC -!- MISCELLANEOUS: Present with 13100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000305}.
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DR EMBL; X04082; CAA27719.1; -; Genomic_DNA.
DR EMBL; M28042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z36012; CAA85101.1; -; Genomic_DNA.
DR EMBL; X73531; CAA51935.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07259.1; -; Genomic_DNA.
DR PIR; S46014; S46014.
DR RefSeq; NP_009701.3; NM_001178491.3.
DR PDB; 4CRM; EM; 8.75 A; X=140-421.
DR PDB; 4CRN; EM; 9.10 A; X=1-437.
DR PDBsum; 4CRM; -.
DR PDBsum; 4CRN; -.
DR AlphaFoldDB; P12385; -.
DR SMR; P12385; -.
DR BioGRID; 32843; 149.
DR ComplexPortal; CPX-435; Translation release factor ERF1-ERF3 complex.
DR DIP; DIP-800N; -.
DR IntAct; P12385; 46.
DR MINT; P12385; -.
DR STRING; 4932.YBR143C; -.
DR iPTMnet; P12385; -.
DR MaxQB; P12385; -.
DR PaxDb; P12385; -.
DR PRIDE; P12385; -.
DR EnsemblFungi; YBR143C_mRNA; YBR143C; YBR143C.
DR GeneID; 852440; -.
DR KEGG; sce:YBR143C; -.
DR SGD; S000000347; SUP45.
DR VEuPathDB; FungiDB:YBR143C; -.
DR eggNOG; KOG0688; Eukaryota.
DR GeneTree; ENSGT00390000009004; -.
DR HOGENOM; CLU_035759_2_1_1; -.
DR InParanoid; P12385; -.
DR OMA; GQEMEVV; -.
DR BioCyc; YEAST:G3O-29097-MON; -.
DR Reactome; R-SCE-72764; Eukaryotic Translation Termination.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P12385; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P12385; protein.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0018444; C:translation release factor complex; IDA:SGD.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IBA:GO_Central.
DR GO; GO:0003747; F:translation release factor activity; IDA:SGD.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IMP:SGD.
DR GO; GO:0002184; P:cytoplasmic translational termination; IBA:GO_Central.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:SGD.
DR GO; GO:0006415; P:translational termination; IDA:SGD.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR Gene3D; 3.30.960.10; -; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR024049; eRF1_1_sf.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR PANTHER; PTHR10113; PTHR10113; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR SMART; SM01194; eRF1_1; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF55481; SSF55481; 1.
DR TIGRFAMs; TIGR03676; aRF1/eRF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Methylation; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..437
FT /note="Eukaryotic peptide chain release factor subunit 1"
FT /id="PRO_0000143167"
FT MOD_RES 182
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:15509572,
FT ECO:0000269|PubMed:16321977"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 41
FT /note="Q -> L (in Ref. 1; CAA27719 and 2; M28042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 437 AA; 49006 MW; 9B59133EE3B1F61E CRC64;
MDNEVEKNIE IWKVKKLVQS LEKARGNGTS MISLVIPPKG QIPLYQKMLT DEYGTASNIK
SRVNRLSVLS AITSTQQKLK LYNTLPKNGL VLYCGDIITE DGKEKKVTFD IEPYKPINTS
LYLCDNKFHT EVLSELLQAD DKFGFIVMDG QGTLFGSVSG NTRTVLHKFT VDLPKKHGRG
GQSALRFARL REEKRHNYVR KVAEVAVQNF ITNDKVNVKG LILAGSADFK TDLAKSELFD
PRLACKVISI VDVSYGGENG FNQAIELSAE ALANVKYVQE KKLLEAYFDE ISQDTGKFCY
GIDDTLKALD LGAVEKLIVF ENLETIRYTF KDAEDNEVIK FAEPEAKDKS FAIDKATGQE
MDVVSEEPLI EWLAANYKNF GATLEFITDK SSEGAQFVTG FGGIGAMLRY KVNFEQLVDE
SEDEYYDEDE GSDYDFI
