EF2_CRIGR
ID EF2_CRIGR Reviewed; 858 AA.
AC P09445; P05086; Q60423;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 4.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=EEF2; Synonyms=EF2;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2834376; DOI=10.1016/s0021-9258(18)68797-6;
RA Nakanishi T., Kohno K., Ishiura M., Ohashi H., Uchida T.;
RT "Complete nucleotide sequence and characterization of the 5'-flanking
RT region of mammalian elongation factor 2 gene.";
RL J. Biol. Chem. 263:6384-6391(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DIPHTHAMIDE AT HIS-715, RESISTANCE TO
RP DIPHTHERIA TOXIN, AND MUTAGENESIS OF SER-584; ILE-714; GLY-717 AND GLY-719.
RC TISSUE=Ovary;
RX PubMed=7559470; DOI=10.1074/jbc.270.39.23218;
RA Foley B.T., Moehring J.M., Moehring T.J.;
RT "Mutations in the elongation factor 2 gene which confer resistance to
RT diphtheria toxin and Pseudomonas exotoxin A. Genetic and biochemical
RT analyses.";
RL J. Biol. Chem. 270:23218-23225(1995).
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. {ECO:0000269|PubMed:7559470}.
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. {ECO:0000269|PubMed:7559470}.
CC -!- PTM: (Microbial infection) Diphthamide can be ADP-ribosylated by
CC diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein
CC synthesis. {ECO:0000269|PubMed:7559470}.
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 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; M13708; AAA50387.1; -; mRNA.
DR EMBL; J03200; AAA50386.1; -; Genomic_DNA.
DR EMBL; U17362; AAB60497.1; -; mRNA.
DR PIR; A25440; A25440.
DR RefSeq; NP_001230968.1; NM_001244039.1.
DR AlphaFoldDB; P09445; -.
DR SMR; P09445; -.
DR STRING; 10029.NP_001230968.1; -.
DR GeneID; 100689051; -.
DR KEGG; cge:100689051; -.
DR CTD; 1938; -.
DR eggNOG; KOG0469; Eukaryota.
DR OrthoDB; 140796at2759; -.
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:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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; ADP-ribosylation; Cytoplasm; Elongation factor; GTP-binding;
KW Isopeptide bond; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Ubl conjugation.
FT CHAIN 1..858
FT /note="Elongation factor 2"
FT /id="PRO_0000090999"
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 SITE 586..587
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P13639"
FT SITE 605..606
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P13639"
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:0000250|UniProtKB:P13639"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P13639"
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:0000250|UniProtKB:P05197"
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:0000250|UniProtKB:P13639"
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:0000250|UniProtKB:P13639"
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="(Microbial infection) ADP-ribosyldiphthamide"
FT /evidence="ECO:0000269|PubMed:7559470"
FT MOD_RES 715
FT /note="Diphthamide"
FT /evidence="ECO:0000269|PubMed:7559470"
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"
FT MUTAGEN 584
FT /note="S->G: Prevents H-715 diphthamide modification and
FT its subsequent ADP-ribosylation by diphtheria toxin.
FT Prevents inhibition of protein synthesis by diphtheria
FT toxin."
FT /evidence="ECO:0000269|PubMed:7559470"
FT MUTAGEN 714
FT /note="I->N: Prevents H-715 diphthamide modification and
FT its subsequent ADP-ribosylation by diphtheria toxin.
FT Prevents inhibition of protein synthesis by diphtheria
FT toxin."
FT /evidence="ECO:0000269|PubMed:7559470"
FT MUTAGEN 717
FT /note="G->R: Prevents H-715 diphthamide modification and
FT its subsequent ADP-ribosylation by diphtheria toxin.
FT Prevents inhibition of protein synthesis by diphtheria
FT toxin."
FT /evidence="ECO:0000269|PubMed:7559470"
FT MUTAGEN 719
FT /note="G->D: Prevents H-715 diphthamide modification and
FT its subsequent ADP-ribosylation by diphtheria toxin.
FT Prevents inhibition of protein synthesis by diphtheria
FT toxin."
FT /evidence="ECO:0000269|PubMed:7559470"
FT CONFLICT 16
FT /note="E -> K (in Ref. 1; AAA50387 and 3; AAB60497)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="P -> A (in Ref. 1; AAA50387 and 3; AAB60497)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="D -> E (in Ref. 1; AAA50387)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="G -> R (in Ref. 2; AAA50386)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="G -> P (in Ref. 1; AAA50387 and 3; AAB60497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 95297 MW; C3AFAED6EAF64794 CRC64;
MVNFTVDQIR AIMDKEANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR AGETRFTDTR
KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI NLIDSPGHVD FSSEVTAALR
VTDGALVVVD CVSGVCVQTE TVLRQAIAER IKPVLMMNKM DRALLELQLE PEELYQTFQR
IVENVNVIIS TYGEGESGPM GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG
EGQLGPAERA KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV
FDPIMNFRKE 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 GSQVVAETRK
RKGLKEGIPA LDNFLDKL
