ID   ERF1_MOUSE              Reviewed;         437 AA.
AC   Q8BWY3; Q3TPZ6; Q91VH9;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   27-MAR-2024, entry version 165.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE            Short=Eukaryotic release factor 1;
DE            Short=eRF1;
GN   Name=Etf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH MOLONEY MURINE LEUKEMIA VIRUS REVERSE
RP   TRANSCRIPTASE/RIBONUCLEASE H P80 AND GAG-POL POLYPROTEIN (MICROBIAL
RP   INFECTION).
RX   PubMed=14636559; DOI=10.1016/s0092-8674(03)00805-5;
RA   Orlova M., Yueh A., Leung J., Goff S.P.;
RT   "Reverse transcriptase of Moloney murine leukemia virus binds to eukaryotic
RT   release factor 1 to modulate suppression of translational termination.";
RL   Cell 115:319-331(2003).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   METHYLATION AT GLN-185.
RX   PubMed=20606008; DOI=10.1128/mcb.00218-10;
RA   Liu P., Nie S., Li B., Yang Z.Q., Xu Z.M., Fei J., Lin C., Zeng R.,
RA   Xu G.L.;
RT   "Deficiency in a glutamine-specific methyltransferase for release factor
RT   causes mouse embryonic lethality.";
RL   Mol. Cell. Biol. 30:4245-4253(2010).
RN   [6]
RP   HYDROXYLATION AT LYS-63.
RX   PubMed=24486019; DOI=10.1016/j.molcel.2013.12.028;
RA   Feng T., Yamamoto A., Wilkins S.E., Sokolova E., Yates L.A., Muenzel M.,
RA   Singh P., Hopkinson R.J., Fischer R., Cockman M.E., Shelley J.,
RA   Trudgian D.C., Schoedel J., McCullagh J.S., Ge W., Kessler B.M.,
RA   Gilbert R.J., Frolova L.Y., Alkalaeva E., Ratcliffe P.J., Schofield C.J.,
RA   Coleman M.L.;
RT   "Optimal translational termination requires C4 lysyl hydroxylation of
RT   eRF1.";
RL   Mol. Cell 53:645-654(2014).
CC   -!- FUNCTION: Component of the eRF1-eRF3-GTP ternary complex, a ternary
CC       complex that mediates translation termination in response to the
CC       termination codons. The eRF1-eRF3-GTP complex binds to a stop codon in
CC       the ribosomal A-site. ETF1/ERF1 is responsible for stop codon
CC       recognition and inducing hydrolysis of peptidyl-tRNA. Following GTP
CC       hydrolysis, eRF3 (GSPT1/ERF3A or GSPT2/ERF3B) dissociates, permitting
CC       ETF1/eRF1 to accommodate fully in the A-site, followed by hydrolysis of
CC       peptidyl-tRNA. Component of the transient SURF complex which recruits
CC       UPF1 to stalled ribosomes in the context of nonsense-mediated decay
CC       (NMD) of mRNAs containing premature stop codons. Required for SHFL-
CC       mediated translation termination which inhibits programmed ribosomal
CC       frameshifting (-1PRF) of mRNA from viruses and cellular genes.
CC       {ECO:0000250|UniProtKB:P62495}.
CC   -!- SUBUNIT: Component of the eRF1-eRF3-GTP ternary complex, composed of
CC       ETF1/ERF1 and eRF3 (GSPT1/ERF3A or GSPT2/ERF3B) and GTP. Component of
CC       the transient SURF (SMG1-UPF1-eRF1-eRF3) complex. Interacts with JMJD4.
CC       The ETF1-GSPT1 complex interacts with JMJD4.
CC       {ECO:0000250|UniProtKB:P62495}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Moloney murine leukemia
CC       virus (MoLV) reverse transcriptase/Ribonuclease H p80 (via RT and RNase
CC       domains); this interaction is essential for translational readthrough
CC       of amber codon between viral gag and pol genes. Interacts with MoLV
CC       Gag-Pol precursor. {ECO:0000269|PubMed:14636559}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62495}.
CC   -!- PTM: Hydroxylation at Lys-63 by JMJD4 promotes its translational
CC       termination efficiency. {ECO:0000305|PubMed:24486019}.
CC   -!- PTM: Methylated at Gln-185 by N6AMT1. {ECO:0000305|PubMed:20606008}.
CC   -!- PTM: Ubiquitinated at Lys-279 via 'Lys-6'-linked polyubiquitin chains
CC       by RNF14 and RNF25 in response to ribosome collisions (ribosome
CC       stalling), leading to its degradation by the proteasome and rescue of
CC       stalled ribosomes. {ECO:0000250|UniProtKB:P62495}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; AK049607; BAC33839.1; -; mRNA.
DR   EMBL; AK164020; BAE37589.1; -; mRNA.
DR   EMBL; BC013717; AAH13717.1; -; mRNA.
DR   CCDS; CCDS29137.1; -.
DR   RefSeq; NP_659115.3; NM_144866.3.
DR   PDB; 5DMQ; X-ray; 4.00 A; B=1-437.
DR   PDB; 5DMR; X-ray; 2.80 A; B=276-437.
DR   PDBsum; 5DMQ; -.
DR   PDBsum; 5DMR; -.
DR   AlphaFoldDB; Q8BWY3; -.
DR   SMR; Q8BWY3; -.
DR   BioGRID; 230388; 9.
DR   ComplexPortal; CPX-670; Translation release factor ERF1-ERF3 complex.
DR   IntAct; Q8BWY3; 2.
DR   STRING; 10090.ENSMUSP00000025218; -.
DR   iPTMnet; Q8BWY3; -.
DR   PhosphoSitePlus; Q8BWY3; -.
DR   SwissPalm; Q8BWY3; -.
DR   EPD; Q8BWY3; -.
DR   jPOST; Q8BWY3; -.
DR   MaxQB; Q8BWY3; -.
DR   PaxDb; 10090-ENSMUSP00000025218; -.
DR   PeptideAtlas; Q8BWY3; -.
DR   ProteomicsDB; 275882; -.
DR   Pumba; Q8BWY3; -.
DR   Antibodypedia; 26674; 235 antibodies from 28 providers.
DR   DNASU; 225363; -.
DR   Ensembl; ENSMUST00000025218.8; ENSMUSP00000025218.8; ENSMUSG00000024360.9.
DR   GeneID; 225363; -.
DR   KEGG; mmu:225363; -.
DR   UCSC; uc008elu.1; mouse.
DR   AGR; MGI:2385071; -.
DR   CTD; 2107; -.
DR   MGI; MGI:2385071; Etf1.
DR   VEuPathDB; HostDB:ENSMUSG00000024360; -.
DR   eggNOG; KOG0688; Eukaryota.
DR   GeneTree; ENSGT00390000009004; -.
DR   HOGENOM; CLU_035759_2_1_1; -.
DR   InParanoid; Q8BWY3; -.
DR   OMA; RCNGSEE; -.
DR   OrthoDB; 144076at2759; -.
DR   PhylomeDB; Q8BWY3; -.
DR   TreeFam; TF105672; -.
DR   Reactome; R-MMU-72764; Eukaryotic Translation Termination.
DR   Reactome; R-MMU-9629569; Protein hydroxylation.
DR   Reactome; R-MMU-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-MMU-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   BioGRID-ORCS; 225363; 30 hits in 77 CRISPR screens.
DR   ChiTaRS; Etf1; mouse.
DR   PRO; PR:Q8BWY3; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q8BWY3; Protein.
DR   Bgee; ENSMUSG00000024360; Expressed in epiblast (generic) and 268 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR   GO; GO:0018444; C:translation release factor complex; ISO:MGI.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; ISO:MGI.
DR   GO; GO:1990825; F:sequence-specific mRNA binding; ISO:MGI.
DR   GO; GO:0003747; F:translation release factor activity; ISO:MGI.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central.
DR   GO; GO:0008079; F:translation termination factor activity; ISS:UniProtKB.
DR   GO; GO:0002184; P:cytoplasmic translational termination; IBA:GO_Central.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006449; P:regulation of translational termination; ISO:MGI.
DR   GO; GO:0006415; P:translational termination; ISO:MGI.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.30.960.10; eRF1 domain 1; 1.
DR   Gene3D; 3.30.420.60; eRF1 domain 2; 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; IPR004403; Peptide_chain-rel_eRF1/aRF1.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   NCBIfam; TIGR03676; aRF1_eRF1; 1.
DR   PANTHER; PTHR10113:SF10; EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1; 1.
DR   PANTHER; PTHR10113; PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1; 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; L30e-like; 1.
DR   SUPFAM; SSF55481; N-terminal domain of eukaryotic peptide chain release factor subunit 1, ERF1; 1.
DR   SUPFAM; SSF53137; Translational machinery components; 1.
DR   Genevisible; Q8BWY3; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Host-virus interaction;
KW   Hydroxylation; Isopeptide bond; Methylation; Nonsense-mediated mRNA decay;
KW   Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62495"
FT   CHAIN           2..437
FT                   /note="Eukaryotic peptide chain release factor subunit 1"
FT                   /id="PRO_0000143140"
FT   MOTIF           61..64
FT                   /note="NIKS motif; plays an important role in translational
FT                   termination"
FT                   /evidence="ECO:0000250|UniProtKB:P62495"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P62495"
FT   MOD_RES         63
FT                   /note="4-hydroxylysine"
FT                   /evidence="ECO:0000269|PubMed:24486019"
FT   MOD_RES         185
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000305|PubMed:20606008"
FT   MOD_RES         347
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62495"
FT   CROSSLNK        87
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62495"
FT   CROSSLNK        279
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P62495"
FT   CROSSLNK        404
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P62495"
FT   CONFLICT        40
FT                   /note="P -> Q (in Ref. 2; AAH13717)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="E -> K (in Ref. 1; BAC33839)"
FT                   /evidence="ECO:0000305"
FT   HELIX           283..295
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          301..304
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   HELIX           305..313
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          317..323
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          329..334
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          336..339
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          341..346
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          368..373
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   HELIX           374..381
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   HELIX           382..384
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          388..392
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          394..396
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   HELIX           397..406
FT                   /evidence="ECO:0007829|PDB:5DMR"
FT   STRAND          409..415
FT                   /evidence="ECO:0007829|PDB:5DMR"
SQ   SEQUENCE   437 AA;  49031 MW;  CECC50D100E59D19 CRC64;
     MADDPSAADR NVEIWKIKKL IKSLEAARGN GTSMISLIIP PKDQISRVAK MLADEFGTAS
     NIKSRVNRLS VLGAITSVQQ RLKLYNKVPP NGLVVYCGTI VTEEGKEKKV NIDFEPFKPI
     NTSLYLCDNK FHTEALTALL SDDSKFGFIV IDGSGALFGT LQGNTREVLH KFTVDLPKKH
     GRGGQSALRF ARLRMEKRHN YVRKVAETAV QLFISGDKVN VAGLVLAGSA DFKTELSQSD
     MFDQRLQSKV LKLVDISYGG ENGFNQAIEL STEVLSNVKF IQEKKLIGRY FDEISQDTGK
     YCFGVEDTLK ALEMGAVEIL IVYENLDIMR YVLHCQGTEE EKILYLTPEQ EKDKSHFTDK
     ETGQEHELIE SMPLLEWFAN NYKKFGATLE IVTDKSQEGS QFVKGFGGIG GILRYRVDFQ
     GMEYQGGDDE FFDLDDY
//