ERF1_MOUSE
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 03-AUG-2022, entry version 156.
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, Pancreas,
RC 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: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA
CC (By similarity). 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 (By similarity).
CC {ECO:0000250|UniProtKB:P62495}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP (By
CC similarity). Component of the transient SURF (SMG1-UPF1-eRF1-eRF3)
CC complex (By similarity). Interacts with JMJD4 (By similarity). The
CC ETF1-GSPT1 complex interacts with JMJD4 (By similarity).
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 -!- 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; Q8BWY3; -.
DR PeptideAtlas; Q8BWY3; -.
DR PRIDE; Q8BWY3; -.
DR ProteomicsDB; 275882; -.
DR Antibodypedia; 26674; 207 antibodies from 28 providers.
DR DNASU; 225363; -.
DR Ensembl; ENSMUST00000025218; ENSMUSP00000025218; ENSMUSG00000024360.
DR GeneID; 225363; -.
DR KEGG; mmu:225363; -.
DR UCSC; uc008elu.1; mouse.
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; RCHGENT; -.
DR OrthoDB; 592406at2759; -.
DR PhylomeDB; Q8BWY3; -.
DR TreeFam; TF105672; -.
DR Reactome; R-MMU-72764; Eukaryotic Translation Termination.
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 72 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 264 other tissues.
DR Genevisible; Q8BWY3; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0018444; C:translation release factor complex; 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:0006479; P:protein methylation; ISO:MGI.
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; 3.30.420.60; -; 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; 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 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
