EF1D2_ARATH
ID EF1D2_ARATH Reviewed; 231 AA.
AC Q9SI20; Q7GA96; Q8LB45;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Elongation factor 1-delta 2;
DE Short=EF-1-delta 2;
DE AltName: Full=Elongation factor 1B-beta 2;
DE AltName: Full=eEF-1B beta 2;
GN OrderedLocusNames=At2g18110; ORFNames=F8D23.11, T27K22.2;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
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: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound
CC to EF-1-alpha to GTP. {ECO:0000250}.
CC -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta (1B-alpha=beta'),
CC delta (1B-beta), and gamma (1B-gamma). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; AC006201; AAM15146.1; -; Genomic_DNA.
DR EMBL; AC007212; AAD31355.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06727.1; -; Genomic_DNA.
DR EMBL; AY065159; AAL38335.1; -; mRNA.
DR EMBL; AY081568; AAM10130.1; -; mRNA.
DR EMBL; AY087429; AAM64977.1; -; mRNA.
DR PIR; D84560; D84560.
DR RefSeq; NP_179402.1; NM_127367.3.
DR AlphaFoldDB; Q9SI20; -.
DR SMR; Q9SI20; -.
DR BioGRID; 1680; 4.
DR IntAct; Q9SI20; 1.
DR STRING; 3702.AT2G18110.1; -.
DR iPTMnet; Q9SI20; -.
DR PaxDb; Q9SI20; -.
DR PRIDE; Q9SI20; -.
DR ProteomicsDB; 221916; -.
DR EnsemblPlants; AT2G18110.1; AT2G18110.1; AT2G18110.
DR GeneID; 816323; -.
DR Gramene; AT2G18110.1; AT2G18110.1; AT2G18110.
DR KEGG; ath:AT2G18110; -.
DR Araport; AT2G18110; -.
DR TAIR; locus:2053144; AT2G18110.
DR eggNOG; KOG1668; Eukaryota.
DR HOGENOM; CLU_050172_3_0_1; -.
DR InParanoid; Q9SI20; -.
DR OMA; WSYTDSK; -.
DR OrthoDB; 1464823at2759; -.
DR PhylomeDB; Q9SI20; -.
DR PRO; PR:Q9SI20; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SI20; baseline and differential.
DR Genevisible; Q9SI20; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR Pfam; PF00736; EF1_GNE; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR PROSITE; PS00824; EF1BD_1; 1.
DR PROSITE; PS00825; EF1BD_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Elongation factor; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..231
FT /note="Elongation factor 1-delta 2"
FT /id="PRO_0000155036"
FT DOMAIN 11..73
FT /note="GST C-terminal"
FT REGION 82..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 50
FT /note="F -> Y (in Ref. 4; AAM64977)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> I (in Ref. 4; AAM64977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25266 MW; 13FBCFD7130DA200 CRC64;
MAAFPNLNSG SGLKKLDEHL LTRSYITGYQ ASKDDITVFT ALSKPPTSEF VNVSRWFNHI
DALLRISGVS AEGSGVIVEG SSPITEEAVA TPPAADSKDT AAEEEDDDDV DLFGEETEEE
KKAAEERAAS VKASTKKKES GKSSVLMDIK PWDDETDMKK LEEAVRSIQM EGLFWGASKL
VPVGYGIKKL HIMCTIVDDL VSIDTMIEEQ LTVEPINEYV QSCDIVAFNK I
