EF2_RAT
ID EF2_RAT Reviewed; 858 AA.
AC P05197; P97619;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=Eef2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-694.
RC TISSUE=Liver;
RX PubMed=2721670; DOI=10.1016/0014-5793(89)80447-8;
RA Oleinikov A.V., Jokhadze G.G., Alakhov Y.B.;
RT "Primary structure of rat liver elongation factor 2 deduced from the cDNA
RT sequence.";
RL FEBS Lett. 248:131-136(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-10 AND 581-594, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fibroblast;
RA Bienvenut W.V., von Kriegsheim A., Kolch W.;
RL Submitted (JUN-2009) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 163-180; 288-299 AND 606-625, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 516-858.
RX PubMed=3014523; DOI=10.1073/pnas.83.14.4978;
RA Kohno K., Uchida T., Ohkubo H., Nakanishi S., Nakanishi T., Fukui T.,
RA Ohtsuka E., Ikehara M., Okada Y.;
RT "Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA
RT sequence: homology with GTP-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:4978-4982(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 508-558.
RC STRAIN=Wistar Kyoto; TISSUE=Aortic smooth muscle;
RA Adams L.A., Werny I., Schwartz S.M.;
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 550-858.
RC STRAIN=Noble;
RA Too C.K.L.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 702-716, AND DIPHTHAMIDE AT HIS-715.
RC TISSUE=Liver;
RX PubMed=4368673; DOI=10.1016/s0021-9258(19)42331-4;
RA Robinson E.A., Henriksen O., Maxwell E.S.;
RT "Elongation factor 2. Amino acid sequence at the site of adenosine
RT diphosphate ribosylation.";
RL J. Biol. Chem. 249:5088-5093(1974).
RN [9]
RP PROTEIN SEQUENCE OF 3-19 AND 51-60, AND PHOSPHORYLATION.
RC TISSUE=Pancreas;
RX PubMed=3693353; DOI=10.1016/s0021-9258(18)45377-x;
RA Nairn A.C., Palfrey H.C.;
RT "Identification of the major Mr 100,000 substrate for calmodulin-dependent
RT protein kinase III in mammalian cells as elongation factor-2.";
RL J. Biol. Chem. 262:17299-17303(1987).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; THR-59; SER-325; THR-435
RP AND SER-502, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-
CC ammonio)propyl]histidine. {ECO:0000269|PubMed:4368673}.
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: 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 -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P13639}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-G/EF-2
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; BC066661; AAH66661.1; -; mRNA.
DR EMBL; K03502; AAA41106.1; -; mRNA.
DR EMBL; Y07504; CAA68805.1; -; mRNA.
DR EMBL; U75403; AAB19107.1; -; mRNA.
DR EMBL; AF000576; AAD05363.1; -; mRNA.
DR PIR; S04007; EFRT2.
DR RefSeq; NP_058941.1; NM_017245.2.
DR AlphaFoldDB; P05197; -.
DR SMR; P05197; -.
DR BioGRID; 248199; 11.
DR IntAct; P05197; 9.
DR MINT; P05197; -.
DR STRING; 10116.ENSRNOP00000041821; -.
DR iPTMnet; P05197; -.
DR PhosphoSitePlus; P05197; -.
DR World-2DPAGE; 0004:P05197; -.
DR jPOST; P05197; -.
DR PaxDb; P05197; -.
DR PRIDE; P05197; -.
DR Ensembl; ENSRNOT00000047450; ENSRNOP00000041821; ENSRNOG00000020266.
DR GeneID; 29565; -.
DR KEGG; rno:29565; -.
DR UCSC; RGD:61979; rat.
DR CTD; 1938; -.
DR RGD; 61979; Eef2.
DR eggNOG; KOG0469; Eukaryota.
DR GeneTree; ENSGT00940000154662; -.
DR HOGENOM; CLU_002794_11_1_1; -.
DR InParanoid; P05197; -.
DR OMA; MGGAEIN; -.
DR OrthoDB; 140796at2759; -.
DR PhylomeDB; P05197; -.
DR TreeFam; TF300575; -.
DR Reactome; R-RNO-156902; Peptide chain elongation.
DR Reactome; R-RNO-5358493; Synthesis of diphthamide-EEF2.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8876725; Protein methylation.
DR PRO; PR:P05197; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000020266; Expressed in spleen and 19 other tissues.
DR Genevisible; P05197; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0042788; C:polysomal ribosome; IDA:RGD.
DR GO; GO:0005844; C:polysome; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008097; F:5S rRNA binding; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISO:RGD.
DR GO; GO:0002039; F:p53 binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0043022; F:ribosome binding; IDA:RGD.
DR GO; GO:0003723; F:RNA binding; IDA:RGD.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:1990416; P:cellular response to brain-derived neurotrophic factor stimulus; IEP:RGD.
DR GO; GO:0014009; P:glial cell proliferation; IEP:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IMP:RGD.
DR GO; GO:0045727; P:positive regulation of translation; IDA:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0051593; P:response to folic acid; IEP:RGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEP:RGD.
DR GO; GO:0003009; P:skeletal muscle contraction; IEP:RGD.
DR GO; GO:0006414; P:translational elongation; ISO:RGD.
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 Acetylation; Cytoplasm; Direct protein sequencing; Elongation factor;
KW GTP-binding; Isopeptide bond; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..858
FT /note="Elongation factor 2"
FT /id="PRO_0000091004"
FT DOMAIN 17..362
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 26..33
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 104..108
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 158..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 57
FT /note="Phosphothreonine; by EEF2K"
FT /evidence="ECO:0000269|PubMed:3693353,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 152
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 235
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 239
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 265
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 272
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 272
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 275
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 373
FT /note="Phosphotyrosine; by CSK"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 445
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 525
FT /note="N6,N6,N6-trimethyllysine; by EEF2KMT"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 572
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 595
FT /note="Phosphoserine; by CDK2"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT MOD_RES 619
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P58252"
FT MOD_RES 715
FT /note="Diphthamide"
FT /evidence="ECO:0000269|PubMed:4368673"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT CROSSLNK 322
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT CROSSLNK 529
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P13639"
SQ SEQUENCE 858 AA; 95284 MW; D6F7A61BADD4B137 CRC64;
MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLE PEELYQTFQR
IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG
EGQLGAAERA KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV
FDAIMNFRKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL LQMITIHLPS
PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK MVPTSDKGRF YAFGRVFSGV
VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV
KTGTITTFEH AHNMRVMKFS VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE
SGEHIIAGAG ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN
RLYMKARPFP DGLAEDIDKG EVSARQELKA RARYLAEKYE WDVAEARKIW CFGPDGTGPN
ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV RFDVHDVTLH ADAIHRGGGQ
IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ CPEQVVGGIY GVLNRKRGHV FEESQVAGTP
MFVVKAYLPV NESFGFTADL RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK
RKGLKEGIPA LDNFLDKL
