ID   ERF1_XENLA              Reviewed;         437 AA.
AC   P35615; Q5D031;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 99.
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 homolog;
DE            Short=SUP1 homolog;
GN   Name=etf1; Synonyms=cl1, erf1;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Egg;
RX   PubMed=8474443; DOI=10.1128/mcb.13.5.2815-2821.1993;
RA   Tassan J.P., le Guellec K., Kress M., Faure M., Camonis J., Jacquet M.,
RA   Philippe M.;
RT   "In Xenopus laevis, the product of a developmentally regulated mRNA is
RT   structurally and functionally homologous to a Saccharomyces cerevisiae
RT   protein involved in translation fidelity.";
RL   Mol. Cell. Biol. 13:2815-2821(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION.
RX   PubMed=7990965; DOI=10.1038/372701a0;
RA   Frolova L., Le Goff X., Rasmussen H.H., Cheprergin S., Drugeon G.,
RA   Haenni A.-L., Celis J.E., Philippe M., Justesen J., Kisselev L.;
RT   "A highly conserved eukaryotic protein family possessing properties of
RT   polypeptide chain release factor.";
RL   Nature 372:701-703(1994).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA, UAG and UGA
CC       (PubMed:7990965). Component of the transient SURF complex which
CC       recruits UPF1 to stalled ribosomes in the context of nonsense-mediated
CC       decay (NMD) of mRNAs containing premature stop codons (By similarity).
CC       Required for SHFL-mediated translation termination which inhibits
CC       programmed ribosomal frameshifting (-1PRF) of mRNA from viruses and
CC       cellular genes. {ECO:0000250|UniProtKB:P62495,
CC       ECO:0000269|PubMed:7990965}.
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). {ECO:0000250|UniProtKB:P62495}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62495}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; X54055; CAA37987.1; -; mRNA.
DR   EMBL; Z14253; CAA78620.1; -; mRNA.
DR   EMBL; BC068651; AAH68651.1; -; mRNA.
DR   PIR; A48061; A48061.
DR   RefSeq; NP_001084363.1; NM_001090894.1.
DR   AlphaFoldDB; P35615; -.
DR   BMRB; P35615; -.
DR   SMR; P35615; -.
DR   BioGRID; 100786; 1.
DR   IntAct; P35615; 1.
DR   MaxQB; P35615; -.
DR   DNASU; 399462; -.
DR   GeneID; 399462; -.
DR   KEGG; xla:399462; -.
DR   CTD; 399462; -.
DR   Xenbase; XB-GENE-5744946; etf1.S.
DR   OMA; RCHGENT; -.
DR   OrthoDB; 592406at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 399462; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR   GO; GO:0008079; F:translation termination factor activity; ISS:UniProtKB.
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; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Cytoplasm; Nonsense-mediated mRNA decay; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..437
FT                   /note="Eukaryotic peptide chain release factor subunit 1"
FT                   /id="PRO_0000143144"
FT   MOTIF           61..64
FT                   /note="NIKS motif; plays an important role in translational
FT                   termination"
FT                   /evidence="ECO:0000250|UniProtKB:P62495"
SQ   SEQUENCE   437 AA;  49011 MW;  3ED3DE92492839FB 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 IVYENLDTMR YVLRCNGSEE EKTLYLTPEQ EKDKSHFIDK
     ETGQEHELIE SMPLLEWFAN SYKKFGATLE IVTDKSQEGS QFVKGFGGIG GILRYRVDFQ
     GMDYQGVDDE FFDLDDY