ERF1X_ARATH
ID ERF1X_ARATH Reviewed; 436 AA.
AC Q39097; B9DFT5; Q94A12; Q9FIJ3;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1-1;
DE Short=Eukaryotic release factor 1-1;
DE Short=eRF1-1;
DE AltName: Full=Omnipotent suppressor protein 1 homolog 1;
DE Short=SUP1 homolog 1;
GN Name=ERF1-1; OrderedLocusNames=At5g47880; ORFNames=MCA23.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Brown C.M., Quigley F.R., Miller W.A.;
RT "Three eukaryotic release factor one (eRF1) homologs from Arabidopsis
RT thaliana Columbia.";
RL (er) Plant Gene Register PGR95-123(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf {ECO:0000312|EMBL:BAH19602.1};
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-182.
RX PubMed=15474304; DOI=10.1016/j.gene.2004.06.053;
RA Chapman B., Brown C.;
RT "Translation termination in Arabidopsis thaliana: characterisation of three
RT versions of release factor 1.";
RL Gene 341:219-225(2004).
RN [7]
RP FUNCTION.
RX PubMed=16113224; DOI=10.1104/pp.105.062695;
RA Petsch K.A., Mylne J., Botella J.R.;
RT "Cosuppression of eukaryotic release factor 1-1 in Arabidopsis affects cell
RT elongation and radial cell division.";
RL Plant Physiol. 139:115-126(2005).
CC -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC (translation) in response to the termination codons UAA, UAG and UGA
CC (PubMed:15474304). Modulates plant growth and development
CC (PubMed:16113224). {ECO:0000269|PubMed:16113224,
CC ECO:0000303|PubMed:15474304}.
CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC {ECO:0000305}.
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DR EMBL; U40217; AAA91169.1; -; mRNA.
DR EMBL; AB016886; BAB11335.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95583.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95584.1; -; Genomic_DNA.
DR EMBL; AY050462; AAK91475.1; -; mRNA.
DR EMBL; AY143968; AAN28907.1; -; mRNA.
DR EMBL; AK316895; BAH19602.1; -; mRNA.
DR RefSeq; NP_001032029.1; NM_001036952.1.
DR RefSeq; NP_199599.1; NM_124162.4.
DR AlphaFoldDB; Q39097; -.
DR SMR; Q39097; -.
DR BioGRID; 20087; 1.
DR STRING; 3702.AT5G47880.2; -.
DR iPTMnet; Q39097; -.
DR PaxDb; Q39097; -.
DR PRIDE; Q39097; -.
DR ProteomicsDB; 221810; -.
DR EnsemblPlants; AT5G47880.1; AT5G47880.1; AT5G47880.
DR EnsemblPlants; AT5G47880.2; AT5G47880.2; AT5G47880.
DR GeneID; 834839; -.
DR Gramene; AT5G47880.1; AT5G47880.1; AT5G47880.
DR Gramene; AT5G47880.2; AT5G47880.2; AT5G47880.
DR KEGG; ath:AT5G47880; -.
DR Araport; AT5G47880; -.
DR TAIR; locus:2160972; AT5G47880.
DR eggNOG; KOG0688; Eukaryota.
DR HOGENOM; CLU_035759_2_1_1; -.
DR InParanoid; Q39097; -.
DR OMA; SVKHFNK; -.
DR OrthoDB; 592406at2759; -.
DR PhylomeDB; Q39097; -.
DR PRO; PR:Q39097; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q39097; baseline and differential.
DR Genevisible; Q39097; AT.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0018444; C:translation release factor complex; IBA:GO_Central.
DR GO; GO:1990825; F:sequence-specific mRNA binding; IBA:GO_Central.
DR GO; GO:0003747; F:translation release factor activity; IGI:TAIR.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IBA:GO_Central.
DR GO; GO:0002184; P:cytoplasmic translational termination; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006415; P:translational termination; IGI:TAIR.
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 Cytoplasm; Growth regulation; Protein biosynthesis; Reference proteome.
FT CHAIN 1..436
FT /note="Eukaryotic peptide chain release factor subunit 1-1"
FT /id="PRO_0000143162"
FT MUTAGEN 182
FT /note="G->A: Loss of peptidyl-tRNA hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:15474304"
FT CONFLICT 121
FT /note="A -> G (in Ref. 1; AAA91169)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="L -> P (in Ref. 4; AAK91475/AAN28907)"
FT CONFLICT 192
FT /note="L -> F (in Ref. 5; BAH19602)"
FT CONFLICT 197
FT /note="R -> S (in Ref. 5; BAH19602)"
SQ SEQUENCE 436 AA; 48723 MW; E77630B26FA2E8AD CRC64;
MGDKNDDDKN IEIWKIKKLI KSLEAARGNG TSMISLIMPP RDQVSRVTKM LGDEYGTASN
IKSRVNRQSV LGAITSAQQR LKLYNRVPPN GLVLYTGTIV NEDGKEKKVT IDFEPFRPIN
ASLYLCDNKF HTEALNELLE SDDKFGFIVM DGNGTLFGTL SGNTREVLHK FSVDLPKKHG
RGGQSALRFA RLRMEKRHNY VRKTAELATQ YYINPATSQP NVSGLILAGS ADFKTELSQS
DMFDPRLAAK ILNVVDVSYG GENGFNQAIE LSAEILANVK FIQEKRLIGK YFEEISQDTG
KYVFGVEDTL NALESGAIET LIVWENLDIN RYVMKNSATG ETVIKHLNKE QEANTENFKV
ADSDLALDVE EKLSLLEWLA NEYRRFGCAL EFVTNKSQEG SQFCRGFGGI GGILRYQLDM
TAFDSEDGEA LDDDSE
