ERF1Y_ARATH
ID ERF1Y_ARATH Reviewed; 434 AA.
AC Q9LPV8; Q147G8; Q39098; Q39223; Q41987;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Eukaryotic peptide chain release factor subunit 1-2;
DE Short=Eukaryotic release factor 1-2;
DE Short=eRF1-2;
DE AltName: Full=Omnipotent suppressor protein 1 homolog 2;
DE Short=SUP1 homolog 2;
GN Name=ERF1-2; OrderedLocusNames=At1g12920; ORFNames=F13K23.17;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 131-434.
RC STRAIN=cv. C24; TISSUE=Flower;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 131-201.
RC STRAIN=cv. Columbia; TISSUE=Flower bud;
RX PubMed=8281187; DOI=10.1046/j.1365-313x.1993.04061051.x;
RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., Guerrier D.,
RA Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., Raynal M.,
RA Cooke R., Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C.,
RA Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.;
RT "An inventory of 1152 expressed sequence tags obtained by partial
RT sequencing of cDNAs from Arabidopsis thaliana.";
RL Plant J. 4:1051-1061(1993).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF GLY-180.
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 [9]
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).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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; AC012187; AAF78496.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28949.1; -; Genomic_DNA.
DR EMBL; AY034963; AAK59469.1; -; mRNA.
DR EMBL; BT026125; ABG48481.1; -; mRNA.
DR EMBL; AY086623; AAM63682.1; -; mRNA.
DR EMBL; X69374; CAA49171.1; -; mRNA.
DR EMBL; U40218; AAA91170.1; -; mRNA.
DR EMBL; Z18188; CAA79125.1; -; mRNA.
DR PIR; H86262; H86262.
DR PIR; S31445; S31445.
DR RefSeq; NP_172752.1; NM_101163.2.
DR AlphaFoldDB; Q9LPV8; -.
DR SMR; Q9LPV8; -.
DR BioGRID; 23090; 5.
DR IntAct; Q9LPV8; 2.
DR STRING; 3702.AT1G12920.1; -.
DR iPTMnet; Q9LPV8; -.
DR PaxDb; Q9LPV8; -.
DR PRIDE; Q9LPV8; -.
DR ProteomicsDB; 221811; -.
DR EnsemblPlants; AT1G12920.1; AT1G12920.1; AT1G12920.
DR GeneID; 837850; -.
DR Gramene; AT1G12920.1; AT1G12920.1; AT1G12920.
DR KEGG; ath:AT1G12920; -.
DR Araport; AT1G12920; -.
DR TAIR; locus:2010341; AT1G12920.
DR eggNOG; KOG0688; Eukaryota.
DR HOGENOM; CLU_035759_2_1_1; -.
DR InParanoid; Q9LPV8; -.
DR OMA; GQEMEVV; -.
DR OrthoDB; 592406at2759; -.
DR PhylomeDB; Q9LPV8; -.
DR PRO; PR:Q9LPV8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LPV8; baseline and differential.
DR Genevisible; Q9LPV8; AT.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005576; C:extracellular region; 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:0007744|PubMed:22223895"
FT CHAIN 2..434
FT /note="Eukaryotic peptide chain release factor subunit 1-2"
FT /id="PRO_0000143163"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 180
FT /note="G->A: Loss of peptidyl-tRNA hydrolytic activity."
FT /evidence="ECO:0000269|PubMed:15474304"
SQ SEQUENCE 434 AA; 48941 MW; 63454371B158D851 CRC64;
MAEEADTNIE IWKIKKLIKG LESARGNGTS MISLIMPPRD QVSRVTKMLG DEYGTASNIK
SRVNRQSVLS AITSAQQRLK LYNKVPTNGL VLYTGTIVND DGKEKKVTFD FEPFRPINAS
LYLCDNKFHT EALNELLESD DKFGFIVMDG NGTLFGTLSG NTREVLHKFT VDLPKKHGRG
GQSALRFARL RMEKRHNYVR KTAELATQFY INPATSQPNV SGLILAGSAD FKTELSQSEL
FDPRLQAKIL NVVDVSYGGE NGFNQAIELS AEILSNVKFI QEKKLIGKYF EEISQDTGKY
VFGVEDTLKA LEMGAIETLI VWENLDINRY ELKNSTTGEM VVKHFGKDQE SDTSNFHDSE
TNAELEVQEK MPLLEWFANE YKRFGCTLEF VTNKSQEGSQ FCRGFGGIGG MLRYQLDMRT
FDELSDTEVY EDSD
