EF2_ARATH
ID EF2_ARATH Reviewed; 843 AA.
AC Q9ASR1; C0Z355; Q56WX9; Q56WY3; Q570K2; Q84R07; Q8H145; Q94CA4; Q9SGT4;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Elongation factor 2 {ECO:0000305};
DE Short=EF-2 {ECO:0000305};
DE AltName: Full=Protein LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 1 {ECO:0000303|PubMed:9401119};
GN Name=LOS1 {ECO:0000303|PubMed:9401119};
GN OrderedLocusNames=At1g56070/At1g56075 {ECO:0000312|Araport:AT1G56070};
GN ORFNames=T6H22.13 {ECO:0000312|EMBL:AAF02837.1};
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 {ECO:0000312|EMBL:AAK32918.1};
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 269-843 (ISOFORM 1).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. C24;
RX PubMed=9401119; DOI=10.2307/3870555;
RA Ishitani M., Xiong L., Stevenson B., Zhu J.-K.;
RT "Genetic analysis of osmotic and cold stress signal transduction in
RT Arabidopsis: interactions and convergence of abscisic acid-dependent and
RT abscisic acid-independent pathways.";
RL Plant Cell 9:1935-1949(1997).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY COLD.
RC STRAIN=cv. C24;
RX PubMed=12032361; DOI=10.1073/pnas.112040099;
RA Guo Y., Xiong L., Ishitani M., Zhu J.-K.;
RT "An Arabidopsis mutation in translation elongation factor 2 causes
RT superinduction of CBF/DREB1 transcription factor genes but blocks the
RT induction of their downstream targets under low temperatures.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7786-7791(2002).
RN [8]
RP INTERACTION WITH GLUTAREDOXINS.
RX PubMed=15998247; DOI=10.1089/ars.2005.7.919;
RA Rouhier N., Villarejo A., Srivastava M., Gelhaye E., Keech O., Droux M.,
RA Finkemeier I., Samuelsson G., Dietz K.J., Jacquot J.P., Wingsle G.;
RT "Identification of plant glutaredoxin targets.";
RL Antioxid. Redox Signal. 7:919-929(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step
CC during translation elongation. During this step, the ribosome changes
CC from the pre-translocational (PRE) to the post-translocational (POST)
CC state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound
CC deacylated tRNA move to the P and E sites, respectively. Catalyzes the
CC coordinated movement of the two tRNA molecules, the mRNA and
CC conformational changes in the ribosome (By similarity). Involved in
CC cold responses leading to freezing tolerance via the induction of cold-
CC responsive genes (PubMed:9401119, PubMed:12032361).
CC {ECO:0000250|UniProtKB:P32324, ECO:0000269|PubMed:12032361,
CC ECO:0000269|PubMed:9401119}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000250|UniProtKB:P32324}.
CC -!- SUBUNIT: May interact with glutaredoxins (Grxs).
CC {ECO:0000269|PubMed:15998247}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32324}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ASR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ASR1-2; Sequence=VSP_058113, VSP_058114, VSP_058115;
CC -!- TISSUE SPECIFICITY: Expressed in root, stem, leaves, flowers and
CC siliques. {ECO:0000269|PubMed:12032361}.
CC -!- INDUCTION: Induced by cold. {ECO:0000269|PubMed:12032361}.
CC -!- DISRUPTION PHENOTYPE: Blocks specifically low temperature-induced
CC transcription of cold-responsive genes such as RD29A (PubMed:9401119,
CC PubMed:12032361). Reduced capacity to develop freezing tolerance but
CC does not impair the vernalization response. Defective in protein
CC synthesis in the cold (PubMed:12032361). {ECO:0000269|PubMed:12032361,
CC ECO:0000269|PubMed:9401119}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02837.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD94254.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD94268.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC009894; AAF02837.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33338.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58611.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM58612.1; -; Genomic_DNA.
DR EMBL; AF367331; AAK32918.1; -; mRNA.
DR EMBL; AY035011; AAK59516.2; -; mRNA.
DR EMBL; AY054461; AAK96653.1; -; mRNA.
DR EMBL; BT000661; AAN31808.1; -; mRNA.
DR EMBL; BT000722; AAN31864.1; -; mRNA.
DR EMBL; BT000786; AAN31925.1; -; mRNA.
DR EMBL; BT002714; AAO11630.1; -; mRNA.
DR EMBL; BT006187; AAP04170.1; -; mRNA.
DR EMBL; AK319019; BAH57134.1; -; mRNA.
DR EMBL; AK220706; BAD93810.1; -; mRNA.
DR EMBL; AK221896; BAD94254.1; ALT_INIT; mRNA.
DR EMBL; AK221900; BAD94268.1; ALT_INIT; mRNA.
DR PIR; A96602; A96602.
DR RefSeq; NP_001321033.1; NM_001333759.1. [Q9ASR1-1]
DR RefSeq; NP_001321034.1; NM_001333760.1. [Q9ASR1-1]
DR RefSeq; NP_849818.1; NM_179487.2. [Q9ASR1-1]
DR AlphaFoldDB; Q9ASR1; -.
DR SMR; Q9ASR1; -.
DR IntAct; Q9ASR1; 2.
DR MINT; Q9ASR1; -.
DR STRING; 3702.AT1G56070.1; -.
DR iPTMnet; Q9ASR1; -.
DR MetOSite; Q9ASR1; -.
DR SwissPalm; Q9ASR1; -.
DR PaxDb; Q9ASR1; -.
DR PRIDE; Q9ASR1; -.
DR ProMEX; Q9ASR1; -.
DR ProteomicsDB; 247078; -. [Q9ASR1-1]
DR EnsemblPlants; AT1G56070.1; AT1G56070.1; AT1G56070. [Q9ASR1-1]
DR EnsemblPlants; AT1G56070.2; AT1G56070.2; AT1G56070. [Q9ASR1-1]
DR EnsemblPlants; AT1G56070.3; AT1G56070.3; AT1G56070. [Q9ASR1-1]
DR GeneID; 842058; -.
DR Gramene; AT1G56070.1; AT1G56070.1; AT1G56070. [Q9ASR1-1]
DR Gramene; AT1G56070.2; AT1G56070.2; AT1G56070. [Q9ASR1-1]
DR Gramene; AT1G56070.3; AT1G56070.3; AT1G56070. [Q9ASR1-1]
DR KEGG; ath:AT1G56070; -.
DR Araport; AT1G56070; -.
DR TAIR; locus:2205235; AT1G56070.
DR eggNOG; KOG0469; Eukaryota.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; Q9ASR1; -.
DR OMA; GVMTQTE; -.
DR PhylomeDB; Q9ASR1; -.
DR UniPathway; UPA00345; -.
DR PRO; PR:Q9ASR1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ASR1; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:UniProtKB.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041095; EFG_II.
DR InterPro; IPR035647; EFG_III/V.
DR InterPro; IPR000640; EFG_V-like.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR Pfam; PF00679; EFG_C; 1.
DR Pfam; PF14492; EFG_III; 1.
DR Pfam; PF03764; EFG_IV; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SMART; SM00838; EFG_C; 1.
DR SMART; SM00889; EFG_IV; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..843
FT /note="Elongation factor 2"
FT /id="PRO_0000435564"
FT DOMAIN 17..344
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 29..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O67618"
FT BINDING 104..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:O67618"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
FT VAR_SEQ 50..664
FT /note="Missing (in isoform 2)"
FT /id="VSP_058113"
FT VAR_SEQ 818..828
FT /note="VLVADIRKRKG -> FWWLISGRGRD (in isoform 2)"
FT /id="VSP_058114"
FT VAR_SEQ 829..843
FT /note="Missing (in isoform 2)"
FT /id="VSP_058115"
SQ SEQUENCE 843 AA; 93891 MW; 861551554192B2AB CRC64;
MVKFTADELR RIMDYKHNIR NMSVIAHVDH GKSTLTDSLV AAAGIIAQEV AGDVRMTDTR
ADEAERGITI KSTGISLYYE MTDESLKSFT GARDGNEYLI NLIDSPGHVD FSSEVTAALR
ITDGALVVVD CIEGVCVQTE TVLRQALGER IRPVLTVNKM DRCFLELQVD GEEAYQTFSR
VIENANVIMA TYEDPLLGDV QVYPEKGTVA FSAGLHGWAF TLTNFAKMYA SKFGVVESKM
MERLWGENFF DPATRKWSGK NTGSPTCKRG FVQFCYEPIK QIIATCMNDQ KDKLWPMLAK
LGVSMKNDEK ELMGKPLMKR VMQTWLPAST ALLEMMIFHL PSPHTAQRYR VENLYEGPLD
DQYANAIRNC DPNGPLMLYV SKMIPASDKG RFFAFGRVFA GKVSTGMKVR IMGPNYIPGE
KKDLYTKSVQ RTVIWMGKRQ ETVEDVPCGN TVAMVGLDQF ITKNATLTNE KEVDAHPIRA
MKFSVSPVVR VAVQCKVASD LPKLVEGLKR LAKSDPMVVC TMEESGEHIV AGAGELHLEI
CLKDLQDDFM GGAEIIKSDP VVSFRETVCD RSTRTVMSKS PNKHNRLYME ARPMEEGLAE
AIDDGRIGPR DDPKIRSKIL AEEFGWDKDL AKKIWAFGPE TTGPNMVVDM CKGVQYLNEI
KDSVVAGFQW ASKEGPLAEE NMRGICFEVC DVVLHSDAIH RGGGQVIPTA RRVIYASQIT
AKPRLLEPVY MVEIQAPEGA LGGIYSVLNQ KRGHVFEEMQ RPGTPLYNIK AYLPVVESFG
FSSQLRAATS GQAFPQCVFD HWEMMSSDPL EPGTQASVLV ADIRKRKGLK EAMTPLSEFE
DKL
