ERF1Z_ARATH
ID ERF1Z_ARATH Reviewed; 435 AA.
AC P35614;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1-3;
DE Short=Eukaryotic release factor 1-3;
DE Short=eRF1-3;
DE AltName: Full=Omnipotent suppressor protein 1 homolog 3;
DE Short=SUP1 homolog 3;
GN Name=ERF1-3; OrderedLocusNames=At3g26618; ORFNames=MFE16.17;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia; TISSUE=Shoot;
RX PubMed=8932388; DOI=10.1093/nar/24.21.4313;
RA Quigley F., Dao P., Cottet A., Mache R.;
RT "Sequence analysis of an 81 kb contig from Arabidopsis thaliana chromosome
RT III.";
RL Nucleic Acids Res. 24:4313-4318(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND MUTAGENESIS OF GLY-181.
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; X69375; CAA49172.1; -; Genomic_DNA.
DR EMBL; X98130; CAA66813.1; -; Genomic_DNA.
DR EMBL; X97486; CAA66118.1; -; mRNA.
DR EMBL; AB026648; BAB01727.1; -; Genomic_DNA.
DR EMBL; AB028611; BAB01727.1; JOINED; Genomic_DNA.
DR EMBL; CP002686; AEE77187.1; -; Genomic_DNA.
DR EMBL; AY050352; AAK91369.1; -; mRNA.
DR EMBL; AY116942; AAM51576.1; -; mRNA.
DR PIR; S31328; S31328.
DR RefSeq; NP_189295.3; NM_113572.4.
DR AlphaFoldDB; P35614; -.
DR SMR; P35614; -.
DR BioGRID; 7603; 2.
DR STRING; 3702.AT3G26618.1; -.
DR iPTMnet; P35614; -.
DR PaxDb; P35614; -.
DR PRIDE; P35614; -.
DR ProteomicsDB; 221861; -.
DR EnsemblPlants; AT3G26618.1; AT3G26618.1; AT3G26618.
DR GeneID; 822273; -.
DR Gramene; AT3G26618.1; AT3G26618.1; AT3G26618.
DR KEGG; ath:AT3G26618; -.
DR Araport; AT3G26618; -.
DR TAIR; locus:2088857; AT3G26618.
DR eggNOG; KOG0688; Eukaryota.
DR HOGENOM; CLU_035759_2_1_1; -.
DR InParanoid; P35614; -.
DR OMA; RCHGENT; -.
DR OrthoDB; 592406at2759; -.
DR PhylomeDB; P35614; -.
DR PRO; PR:P35614; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P35614; baseline and differential.
DR Genevisible; P35614; AT.
DR GO; GO:0005829; C:cytosol; 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 Acetylation; Cytoplasm; Growth regulation; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LPV8"
FT CHAIN 2..435
FT /note="Eukaryotic peptide chain release factor subunit 1-3"
FT /id="PRO_0000143164"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9LPV8"
FT MUTAGEN 181
FT /note="G->A: Loss of peptidyl-tRNA hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:15474304"
SQ SEQUENCE 435 AA; 49007 MW; 4B9D1617D5BDB34E CRC64;
MADQESDKNI EIWKIKKLIK GLETARGNGT SMISLIMPPR DQVARVTKML ADEYGTASNI
KSRVNRQSVL SAITSAQQRL KLYNKVPPNG LVLYTGTIVT DDGKEKKVTI DFEPFKPINA
SLYLCDNKFH TEPLNELLES DDKFGFIVMD GNGTLFGTLS GNTREVLHKF TVDLPKKHGR
GGQSALRFAR LRMEKRHNYV RKTAELATQF YINPATSQPN VSGLILAGSA DFKTELSQSE
LFDPRLQAKI LNVVDVSYGG ENGFNQAIEL SAEILSNVKF IQEKKLIGKY FEEISQDTGK
YVFGVEDTLK ALEMGAVETL IVWENLDINR YELKNNTTGE IVIKHLGKDQ ENNQSNFHDA
ETNAELEVQE KMPLLEWFAN EYKRFGCTLE FVTNKSQEGS QFCRGFGGIG GLLRYQLDMR
TFDELSDGEV YEDSD
