ID ERF1_PONAB Reviewed; 437 AA.
AC Q5R4C7;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 08-NOV-2023, entry version 86.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE Short=Eukaryotic release factor 1;
DE Short=eRF1;
GN Name=ETF1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62495}.
CC -!- PTM: Hydroxylation at Lys-63 by JMJD4 promotes its translational
CC termination efficiency. {ECO:0000250|UniProtKB:P62495}.
CC -!- PTM: Methylated at Gln-185 by N6AMT1. {ECO:0000250|UniProtKB:P62495}.
CC -!- PTM: Ubiquitinated via 'Lys-6'-linked polyubiquitin chains by RNF14 and
CC RNF25 in response to ribosome collisions (ribosome stalling), leading
CC to its degradation by the proteasome and rescue of stalled ribosomes.
CC {ECO:0000250|UniProtKB:P62495}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000305}.
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DR EMBL; CR861324; CAH93389.1; -; mRNA.
DR RefSeq; NP_001126989.1; NM_001133517.1.
DR AlphaFoldDB; Q5R4C7; -.
DR BMRB; Q5R4C7; -.
DR SMR; Q5R4C7; -.
DR STRING; 9601.ENSPPYP00000017698; -.
DR GeneID; 100174012; -.
DR KEGG; pon:100174012; -.
DR CTD; 2107; -.
DR eggNOG; KOG0688; Eukaryota.
DR InParanoid; Q5R4C7; -.
DR OrthoDB; 144076at2759; -.
DR Proteomes; UP000001595; Unplaced.
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; 3.30.960.10; 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.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydroxylation; Isopeptide bond; Methylation;
KW Nonsense-mediated mRNA decay; Phosphoprotein; Protein biosynthesis;
KW 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_0000143141"
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:0000250|UniProtKB:P62495"
FT MOD_RES 185
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250|UniProtKB:P62495"
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"
SQ SEQUENCE 437 AA; 48973 MW; 9EFE0D706D759D1B 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 FGEISQDTGK
YCFGVEDTLK ALEMGAVEIL IVYENLDIMR YVLHCQGTEE EKILYLTPEQ EKDKSHFTDK
ETGQEHELIE SMPLLEWFAN NYKKFGATLE IVTDKSQEGS QFVKGFGGIG GILRYRVDFQ
GMEYQGGDDE FFDLDDY
//
