ID   ERF1Y_BRAOB             Reviewed;         435 AA.
AC   D2K759;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Eukaryotic peptide chain release factor subunit 1-2 {ECO:0000305};
DE            Short=BoeRF1-2 {ECO:0000303|PubMed:21175633};
DE            Short=Eukaryotic release factor 1-2 {ECO:0000303|PubMed:21175633};
GN   Name=ERF1-2 {ECO:0000305};
OS   Brassica oleracea var. botrytis (Cauliflower).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH OR.
RX   PubMed=21175633; DOI=10.1111/j.1469-8137.2010.03578.x;
RA   Zhou X., Sun T.H., Wang N., Ling H.Q., Lu S., Li L.;
RT   "The cauliflower Orange gene enhances petiole elongation by suppressing
RT   expression of eukaryotic release factor 1.";
RL   New Phytol. 190:89-100(2011).
CC   -!- FUNCTION: Directs the termination of nascent peptide synthesis
CC       (translation) in response to the termination codons UAA, UAG and UGA
CC       (By similarity). Modulates plant growth and development
CC       (PubMed:21175633). {ECO:0000250|UniProtKB:Q39097,
CC       ECO:0000269|PubMed:21175633}.
CC   -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP
CC       (Probable). Interacts with OR (PubMed:21175633).
CC       {ECO:0000269|PubMed:21175633, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q39097}.
CC   -!- MISCELLANEOUS: Plants silencing ERF1-2 show increased elongation of the
CC       leaf petiole. {ECO:0000269|PubMed:21175633}.
CC   -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family.
CC       {ECO:0000305}.
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DR   EMBL; GU183403; ACZ71034.1; -; mRNA.
DR   AlphaFoldDB; D2K759; -.
DR   SMR; D2K759; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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.
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 1-2"
FT                   /id="PRO_0000438018"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LPV8"
SQ   SEQUENCE   435 AA;  48916 MW;  57CB8C2DCA67683B CRC64;
     MADQEADTNI EIWKIKKLIK GLESARGNGT SMISLIMPPR DQVSRVTKML GDEYGTASNI
     KSRVNRQSVL SAITSAQQRL KLYNKVPTNG LVLYTGTIVN DDGKEKKVTF DFEPFRPINA
     SLYLCDNKFH TGALNELLES DDKFGFIVMD GNGTLFGTLS GNTREVLHKF TVDLPKKHGR
     GGQSALRFAR LRMEKRHNYV RKTAELATQF YINPATSQPN VAGLILAGSA DFKTELSQSE
     LFDPRLQAKI LNVVDVSYGG ENGFNQAIEL SAEILSNVKF IQEKKLIGKY FEEISQDTGK
     YVFGVEDTLK ALEMGAIETL IVWENLDINR YELKNSTSGE IVVKHFGKDQ ETDQSNFHDA
     ETNAELEVQE KMPLLEWFAN EYKRFGCTLE FVTNKSQEGS QFCRGFGGIG GMLRYQLDMR
     TFDELSDGEV YEDSD