EF1D1_ARATH
ID EF1D1_ARATH Reviewed; 231 AA.
AC P48006; Q0WWW7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Elongation factor 1-delta 1;
DE Short=EF-1-delta 1;
DE AltName: Full=Elongation factor 1B-beta 1;
DE AltName: Full=eEF-1B beta 1;
GN OrderedLocusNames=At1g30230; ORFNames=F12P21.12;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8666245; DOI=10.1016/0378-1119(95)00837-3;
RA Gidekel M., Jimenez B., Herrera-Estrella L.;
RT "The first intron of the Arabidopsis thaliana gene coding for elongation
RT factor 1 beta contains an enhancer-like element.";
RL Gene 170:201-206(1996).
RN [2]
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 [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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) 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.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P48006-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG50564.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X74733; CAA52751.1; -; Genomic_DNA.
DR EMBL; AC073506; AAG50564.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31195.1; -; Genomic_DNA.
DR EMBL; AK226216; BAE98381.1; -; mRNA.
DR PIR; S37103; S37103.
DR RefSeq; NP_174314.2; NM_102762.5. [P48006-1]
DR AlphaFoldDB; P48006; -.
DR SMR; P48006; -.
DR BioGRID; 25138; 7.
DR STRING; 3702.AT1G30230.2; -.
DR iPTMnet; P48006; -.
DR PaxDb; P48006; -.
DR PRIDE; P48006; -.
DR EnsemblPlants; AT1G30230.1; AT1G30230.1; AT1G30230. [P48006-1]
DR GeneID; 839903; -.
DR Gramene; AT1G30230.1; AT1G30230.1; AT1G30230. [P48006-1]
DR KEGG; ath:AT1G30230; -.
DR Araport; AT1G30230; -.
DR eggNOG; KOG1668; Eukaryota.
DR HOGENOM; CLU_050172_3_0_1; -.
DR InParanoid; P48006; -.
DR OMA; MSKFQLV; -.
DR PhylomeDB; P48006; -.
DR PRO; PR:P48006; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P48006; baseline and differential.
DR Genevisible; P48006; 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: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; Alternative splicing; Elongation factor; Protein biosynthesis;
KW 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 1"
FT /id="PRO_0000155035"
FT DOMAIN 10..73
FT /note="GST C-terminal"
FT REGION 85..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 102
FT /note="A -> P (in Ref. 1; CAA52751)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="E -> Q (in Ref. 1; CAA52751)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="L -> R (in Ref. 1; CAA52751)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25132 MW; 2A928F477BF9E932 CRC64;
MAAFPNLNSD AGLKKLDEHL LTRSYITGYQ ASKDDITVFA ALAKPPTSQY VNASRWYNHI
DALLRISGVS AEGSGVIVEG SAPITEEAVA TPPAADSKDA AADEEDDDDV DLFGEETEEE
KKAAEERAAS VKASTKKKES GKSSVLIDIK PWDDETDMKK LEEAVKSIQM EGLFWGASKL
VPVGYGIKKL QILCTIVDDL VSIDTMIEEQ LTVEPINEYV QSCDIVAFNK I
