EF2_RABIT
ID EF2_RABIT Reviewed; 35 AA.
AC P55823;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
DE Flags: Fragment;
GN Name=EEF2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP PROTEIN SEQUENCE OF 2-35.
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=8579355; DOI=10.1006/abbi.1996.0039;
RA Deshpande K.L., Seubert P.H., Tillman D.M., Farkas W.R., Katze J.R.;
RT "Cloning and characterization of cDNA encoding the rabbit tRNA-guanine
RT transglycosylase 60-kilodalton subunit.";
RL Arch. Biochem. Biophys. 326:1-7(1996).
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.
CC -!- SUBUNIT: Component of the mRNA surveillance SURF complex, at least
CC composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8
CC and SMG9. Interacts with RBPMS2. {ECO:0000250|UniProtKB:P13639}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13639}. Nucleus
CC {ECO:0000250|UniProtKB:P13639}. Note=Phosphorylation by CSK promotes
CC cleavage and SUMOylation-dependent nuclear translocation of the C-
CC terminal cleavage product. {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2; it
CC requires prior phosphorylation by CDK2 at Ser-595 during mitotic
CC prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic
CC cleavage, and nuclear translocation if the C-terminal fragment.
CC {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-
CC ammonio)propyl]histidine (By similarity).
CC {ECO:0000250|UniProtKB:P05197}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: Proteolytically processed at two sites following phosphorylation
CC by CSK. {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: SUMOylated following phosphorylation by CSK, promotes proteolytic
CC cleavage. {ECO:0000250|UniProtKB:P13639}.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family. EF-
CC G/EF-2 subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P55823; -.
DR SMR; P55823; -.
DR InParanoid; P55823; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Elongation factor; GTP-binding;
KW Nucleotide-binding; Nucleus; Protein biosynthesis; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8579355"
FT CHAIN 2..>35
FT /note="Elongation factor 2"
FT /id="PRO_0000091003"
FT BINDING 26..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT NON_TER 35
SQ SEQUENCE 35 AA; 3813 MW; FE72F343B557203B CRC64;
MVNFTVDQIS AIMDKKANIS NMSVIARVDD GKSTL
