ERF1_MESAU
ID ERF1_MESAU Reviewed; 437 AA.
AC P62496; P46055;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1;
DE Short=Eukaryotic release factor 1;
DE Short=Protein Cl1;
DE Short=eRF1;
GN Name=ETF1; Synonyms=ERF1, RF1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=9195043; DOI=10.1016/s0300-9084(97)87622-5;
RA Urbero B., Eurwilaichitr L., Stansfield I., Tassan J.P., le Goff X.,
RA Kress M., Tuite M.F.;
RT "Expression of the release factor eRF1 (Sup45p) gene of higher eukaryotes
RT in yeast and mammalian tissues.";
RL Biochimie 79:27-36(1997).
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; X81626; CAA57282.1; -; mRNA.
DR RefSeq; NP_001268599.1; NM_001281670.1.
DR AlphaFoldDB; P62496; -.
DR BMRB; P62496; -.
DR SMR; P62496; -.
DR STRING; 10036.XP_005065344.1; -.
DR GeneID; 101838018; -.
DR CTD; 2107; -.
DR eggNOG; KOG0688; Eukaryota.
DR OrthoDB; 592406at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0018444; C:translation release factor complex; IEA:Ensembl.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IEA:Ensembl.
DR GO; GO:0003747; F:translation release factor activity; IEA:Ensembl.
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:0006479; P:protein methylation; IEA:Ensembl.
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_0000143139"
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; 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
