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Protein

Elongation factor 2

Gene

LOS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). Involved in cold responses leading to freezing tolerance via the induction of cold-responsive genes (PubMed:9401119, PubMed:12032361).By similarity2 Publications

Pathwayi: polypeptide chain elongation

This protein is involved in the pathway polypeptide chain elongation, which is part of Protein biosynthesis.By similarity
View all proteins of this organism that are known to be involved in the pathway polypeptide chain elongation and in Protein biosynthesis.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 346GTPBy similarity
Nucleotide bindingi104 – 1085GTPSequence analysis
Nucleotide bindingi158 – 1614GTPBy similarity

GO - Molecular functioni

  • copper ion binding Source: TAIR
  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • translation elongation factor activity Source: UniProtKB-KW

GO - Biological processi

  • cold acclimation Source: UniProtKB
  • response to cold Source: UniProtKB
  • response to cytokinin Source: TAIR
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Elongation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-ATH-156902. Peptide chain elongation.
R-ATH-5358493. Synthesis of diphthamide-EEF2.
UniPathwayiUPA00345.

Names & Taxonomyi

Protein namesi
Recommended name:
Elongation factor 2Curated
Short name:
EF-2Curated
Alternative name(s):
Protein LOW EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 11 Publication
Gene namesi
Name:LOS11 Publication
Ordered Locus Names:At1g56070/At1g56075Imported
ORF Names:T6H22.13Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)Imported
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G56070.

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • cytosol Source: TAIR
  • membrane Source: TAIR
  • nucleolus Source: TAIR
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Blocks specifically low temperature-induced transcription of cold-responsive genes such as RD29A (PubMed:9401119, PubMed:12032361). Reduced capacity to develop freezing tolerance but does not impair the vernalization response. Defective in protein synthesis in the cold (PubMed:12032361).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 843843Elongation factor 2PRO_0000435564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei837 – 8371PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9ASR1.
ProMEXiQ9ASR1.

PTM databases

iPTMnetiQ9ASR1.
SwissPalmiQ9ASR1.

Expressioni

Tissue specificityi

Expressed in root, stem, leaves, flowers and siliques.1 Publication

Inductioni

Induced by cold.1 Publication

Interactioni

Subunit structurei

May interact with glutaredoxins (Grxs).1 Publication

Protein-protein interaction databases

IntActiQ9ASR1. 2 interactions.
STRINGi3702.AT1G56070.1.

Structurei

3D structure databases

ProteinModelPortaliQ9ASR1.
SMRiQ9ASR1. Positions 2-843.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 344328tr-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family.PROSITE-ProRule annotation
Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0469. Eukaryota.
COG0480. LUCA.
HOGENOMiHOG000231589.
KOiK03234.
OMAiFTGHVTR.
PhylomeDBiQ9ASR1.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9ASR1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVKFTADELR RIMDYKHNIR NMSVIAHVDH GKSTLTDSLV AAAGIIAQEV
60 70 80 90 100
AGDVRMTDTR ADEAERGITI KSTGISLYYE MTDESLKSFT GARDGNEYLI
110 120 130 140 150
NLIDSPGHVD FSSEVTAALR ITDGALVVVD CIEGVCVQTE TVLRQALGER
160 170 180 190 200
IRPVLTVNKM DRCFLELQVD GEEAYQTFSR VIENANVIMA TYEDPLLGDV
210 220 230 240 250
QVYPEKGTVA FSAGLHGWAF TLTNFAKMYA SKFGVVESKM MERLWGENFF
260 270 280 290 300
DPATRKWSGK NTGSPTCKRG FVQFCYEPIK QIIATCMNDQ KDKLWPMLAK
310 320 330 340 350
LGVSMKNDEK ELMGKPLMKR VMQTWLPAST ALLEMMIFHL PSPHTAQRYR
360 370 380 390 400
VENLYEGPLD DQYANAIRNC DPNGPLMLYV SKMIPASDKG RFFAFGRVFA
410 420 430 440 450
GKVSTGMKVR IMGPNYIPGE KKDLYTKSVQ RTVIWMGKRQ ETVEDVPCGN
460 470 480 490 500
TVAMVGLDQF ITKNATLTNE KEVDAHPIRA MKFSVSPVVR VAVQCKVASD
510 520 530 540 550
LPKLVEGLKR LAKSDPMVVC TMEESGEHIV AGAGELHLEI CLKDLQDDFM
560 570 580 590 600
GGAEIIKSDP VVSFRETVCD RSTRTVMSKS PNKHNRLYME ARPMEEGLAE
610 620 630 640 650
AIDDGRIGPR DDPKIRSKIL AEEFGWDKDL AKKIWAFGPE TTGPNMVVDM
660 670 680 690 700
CKGVQYLNEI KDSVVAGFQW ASKEGPLAEE NMRGICFEVC DVVLHSDAIH
710 720 730 740 750
RGGGQVIPTA RRVIYASQIT AKPRLLEPVY MVEIQAPEGA LGGIYSVLNQ
760 770 780 790 800
KRGHVFEEMQ RPGTPLYNIK AYLPVVESFG FSSQLRAATS GQAFPQCVFD
810 820 830 840
HWEMMSSDPL EPGTQASVLV ADIRKRKGLK EAMTPLSEFE DKL
Length:843
Mass (Da):93,891
Last modified:June 1, 2001 - v1
Checksum:i861551554192B2AB
GO
Isoform 2 (identifier: Q9ASR1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-664: Missing.
     818-828: VLVADIRKRKG → FWWLISGRGRD
     829-843: Missing.

Note: No experimental confirmation available.Imported
Show »
Length:213
Mass (Da):23,622
Checksum:i427DB185DA7FB535
GO

Sequence cautioni

The sequence AAF02837.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAD94254.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD94268.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei50 – 664615Missing in isoform 2. VSP_058113Add
BLAST
Alternative sequencei818 – 82811VLVADIRKRKG → FWWLISGRGRD in isoform 2. VSP_058114Add
BLAST
Alternative sequencei829 – 84315Missing in isoform 2. VSP_058115Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009894 Genomic DNA. Translation: AAF02837.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33338.1.
AF367331 mRNA. Translation: AAK32918.1.
AY035011 mRNA. Translation: AAK59516.2.
AY054461 mRNA. Translation: AAK96653.1.
BT000661 mRNA. Translation: AAN31808.1.
BT000722 mRNA. Translation: AAN31864.1.
BT000786 mRNA. Translation: AAN31925.1.
BT002714 mRNA. Translation: AAO11630.1.
BT006187 mRNA. Translation: AAP04170.1.
AK319019 mRNA. Translation: BAH57134.1.
AK220706 mRNA. Translation: BAD93810.1.
AK221896 mRNA. Translation: BAD94254.1. Different initiation.
AK221900 mRNA. Translation: BAD94268.1. Different initiation.
PIRiA96602.
RefSeqiNP_849818.1. NM_179487.1. [Q9ASR1-1]
UniGeneiAt.47544.

Genome annotation databases

EnsemblPlantsiAT1G56070.1; AT1G56070.1; AT1G56070. [Q9ASR1-1]
GeneIDi842058.
KEGGiath:AT1G56070.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC009894 Genomic DNA. Translation: AAF02837.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33338.1.
AF367331 mRNA. Translation: AAK32918.1.
AY035011 mRNA. Translation: AAK59516.2.
AY054461 mRNA. Translation: AAK96653.1.
BT000661 mRNA. Translation: AAN31808.1.
BT000722 mRNA. Translation: AAN31864.1.
BT000786 mRNA. Translation: AAN31925.1.
BT002714 mRNA. Translation: AAO11630.1.
BT006187 mRNA. Translation: AAP04170.1.
AK319019 mRNA. Translation: BAH57134.1.
AK220706 mRNA. Translation: BAD93810.1.
AK221896 mRNA. Translation: BAD94254.1. Different initiation.
AK221900 mRNA. Translation: BAD94268.1. Different initiation.
PIRiA96602.
RefSeqiNP_849818.1. NM_179487.1. [Q9ASR1-1]
UniGeneiAt.47544.

3D structure databases

ProteinModelPortaliQ9ASR1.
SMRiQ9ASR1. Positions 2-843.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9ASR1. 2 interactions.
STRINGi3702.AT1G56070.1.

PTM databases

iPTMnetiQ9ASR1.
SwissPalmiQ9ASR1.

Proteomic databases

PaxDbiQ9ASR1.
ProMEXiQ9ASR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G56070.1; AT1G56070.1; AT1G56070. [Q9ASR1-1]
GeneIDi842058.
KEGGiath:AT1G56070.

Organism-specific databases

TAIRiAT1G56070.

Phylogenomic databases

eggNOGiKOG0469. Eukaryota.
COG0480. LUCA.
HOGENOMiHOG000231589.
KOiK03234.
OMAiFTGHVTR.
PhylomeDBiQ9ASR1.

Enzyme and pathway databases

UniPathwayiUPA00345.
ReactomeiR-ATH-156902. Peptide chain elongation.
R-ATH-5358493. Synthesis of diphthamide-EEF2.

Miscellaneous databases

PROiQ9ASR1.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.240. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR009022. EFG_III-V.
IPR000640. EFG_V.
IPR004161. EFTu-like_2.
IPR031157. G_TR_CS.
IPR027417. P-loop_NTPase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005225. Small_GTP-bd_dom.
IPR000795. TF_GTP-bd_dom.
IPR009000. Transl_B-barrel.
IPR005517. Transl_elong_EFG/EF2_IV.
[Graphical view]
PfamiPF00679. EFG_C. 1 hit.
PF14492. EFG_II. 1 hit.
PF03764. EFG_IV. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
[Graphical view]
PRINTSiPR00315. ELONGATNFCT.
SMARTiSM00838. EFG_C. 1 hit.
SM00889. EFG_IV. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF54980. SSF54980. 2 hits.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS00301. G_TR_1. 1 hit.
PS51722. G_TR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  4. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: cv. Columbia.
    Tissue: Root.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 269-843 (ISOFORM 1).
    Strain: cv. Columbia.
  6. "Genetic analysis of osmotic and cold stress signal transduction in Arabidopsis: interactions and convergence of abscisic acid-dependent and abscisic acid-independent pathways."
    Ishitani M., Xiong L., Stevenson B., Zhu J.-K.
    Plant Cell 9:1935-1949(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: cv. C24.
  7. "An Arabidopsis mutation in translation elongation factor 2 causes superinduction of CBF/DREB1 transcription factor genes but blocks the induction of their downstream targets under low temperatures."
    Guo Y., Xiong L., Ishitani M., Zhu J.-K.
    Proc. Natl. Acad. Sci. U.S.A. 99:7786-7791(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY COLD.
    Strain: cv. C24.
  8. Cited for: INTERACTION WITH GLUTAREDOXINS.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Root.
  10. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.

Entry informationi

Entry nameiEF2_ARATH
AccessioniPrimary (citable) accession number: Q9ASR1
Secondary accession number(s): C0Z355
, Q56WX9, Q56WY3, Q570K2, Q84R07, Q8H145, Q94CA4, Q9SGT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 17, 2016
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.