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   25-MAY-2022, entry version 81.
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: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA, UAG and UGA.
CC       Component of the transient SURF complex which recruits UPF1 to stalled
CC       ribosomes in the context of nonsense-mediated decay (NMD) of mRNAs
CC       containing premature stop codons. Required for SHFL-mediated
CC       translation termination which inhibits programmed ribosomal
CC       frameshifting (-1PRF) of mRNA from viruses and cellular genes.
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   -!- 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   -!- 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   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; 3.30.420.60; -; 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   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