EF2_CAEEL
ID EF2_CAEEL Reviewed; 852 AA.
AC P29691; G3MU53; O17837;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Elongation factor 2;
DE Short=EF-2;
GN Name=eef-2; ORFNames=F25H5.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1930695; DOI=10.1089/dna.1991.10.603;
RA Ofulue E.N., Candido E.P.M.;
RT "Molecular cloning and characterization of the Caenorhabditis elegans
RT elongation factor 2 gene (eft-2).";
RL DNA Cell Biol. 10:603-611(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18413715; DOI=10.1101/gad.1644008;
RA Nukazuka A., Fujisawa H., Inada T., Oda Y., Takagi S.;
RT "Semaphorin controls epidermal morphogenesis by stimulating mRNA
RT translation via eIF2alpha in Caenorhabditis elegans.";
RL Genes Dev. 22:1025-1036(2008).
RN [4]
RP AMPYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=27138431; DOI=10.1371/journal.pgen.1006023;
RA Truttmann M.C., Cruz V.E., Guo X., Engert C., Schwartz T.U., Ploegh H.L.;
RT "The Caenorhabditis elegans protein FIC-1 is an AMPylase that covalently
RT modifies heat-shock 70 family proteins, translation elongation factors and
RT histones.";
RL PLoS Genet. 12:E1006023-E1006023(2016).
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. Involved in the morphogenesis
CC of epidermal tissues. {ECO:0000269|PubMed:18413715}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P29691-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P29691-2; Sequence=VSP_044101;
CC -!- PTM: Phosphorylation by EF-2 kinase completely inactivates EF-2.
CC {ECO:0000250|UniProtKB:P13639}.
CC -!- PTM: AMPylated by fic-1. {ECO:0000269|PubMed:27138431}.
CC -!- DISRUPTION PHENOTYPE: Ray defect. {ECO:0000269|PubMed:18413715}.
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; M86959; AAD03339.1; -; mRNA.
DR EMBL; Z81068; CAB02985.1; -; Genomic_DNA.
DR EMBL; Z81068; CCD31064.1; -; Genomic_DNA.
DR PIR; A40411; A40411.
DR PIR; T21362; T21362.
DR RefSeq; NP_001251010.1; NM_001264081.1.
DR RefSeq; NP_001251011.1; NM_001264082.1.
DR AlphaFoldDB; P29691; -.
DR SMR; P29691; -.
DR BioGRID; 38174; 98.
DR DIP; DIP-26688N; -.
DR IntAct; P29691; 5.
DR MINT; P29691; -.
DR STRING; 6239.F25H5.4a.1; -.
DR iPTMnet; P29691; -.
DR World-2DPAGE; 0020:P29691; -.
DR EPD; P29691; -.
DR PaxDb; P29691; -.
DR PeptideAtlas; P29691; -.
DR EnsemblMetazoa; F25H5.4a.1; F25H5.4a.1; WBGene00001167. [P29691-1]
DR EnsemblMetazoa; F25H5.4a.2; F25H5.4a.2; WBGene00001167. [P29691-1]
DR EnsemblMetazoa; F25H5.4b.1; F25H5.4b.1; WBGene00001167. [P29691-2]
DR GeneID; 172743; -.
DR UCSC; F25H5.4.2; c. elegans. [P29691-1]
DR CTD; 172743; -.
DR WormBase; F25H5.4a; CE15900; WBGene00001167; eef-2. [P29691-1]
DR WormBase; F25H5.4b; CE46149; WBGene00001167; eef-2. [P29691-2]
DR eggNOG; KOG0469; Eukaryota.
DR GeneTree; ENSGT00940000154662; -.
DR HOGENOM; CLU_002794_11_2_1; -.
DR InParanoid; P29691; -.
DR OMA; GVMTQTE; -.
DR OrthoDB; 140796at2759; -.
DR PhylomeDB; P29691; -.
DR Reactome; R-CEL-156902; Peptide chain elongation.
DR Reactome; R-CEL-5358493; Synthesis of diphthamide-EEF2.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR SignaLink; P29691; -.
DR PRO; PR:P29691; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00001167; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..852
FT /note="Elongation factor 2"
FT /id="PRO_0000091008"
FT DOMAIN 17..356
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 116..120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 170..173
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 59
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 709
FT /note="Diphthamide"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..12
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_044101"
FT CONFLICT 132
FT /note="R -> G (in Ref. 1; AAD03339)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="N -> S (in Ref. 1; AAD03339)"
FT /evidence="ECO:0000305"
FT CONFLICT 628..630
FT /note="ILA -> YPG (in Ref. 1; AAD03339)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="D -> A (in Ref. 1; AAD03339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 852 AA; 94796 MW; 849676A861DBC4C4 CRC64;
MVNFTVDEIR ALMDRKRNIR NMSVIAHVDH GKSTLTDSLV SKAGIIAGSK AGETRFTDTR
KDEQERCITI KSTAISLFFE LEKKDLEFVK GENQFETVEV DGKKEKYNGF LINLIDSPGH
VDFSSEVTAA LRVTDGALVV VDCVSGVCVQ TETVLRQAIA ERIKPVLFMN KMDRALLELQ
LGAEELFQTF QRIVENINVI IATYGDDDGP MGPIMVDPSI GNVGFGSGLH GWAFTLKQFA
EMYAGKFGVQ VDKLMKNLWG DRFFDLKTKK WSSTQTDESK RGFCQFVLDP IFMVFDAVMN
IKKDKTAALV EKLGIKLAND EKDLEGKPLM KVFMRKWLPA GDTMLQMIAF HLPSPVTAQK
YRMEMLYEGP HDDEAAVAIK TCDPNGPLMM YISKMVPTSD KGRFYAFGRV FSGKVATGMK
ARIQGPNYVP GKKEDLYEKT IQRTILMMGR FIEPIEDIPS GNIAGLVGVD QYLVKGGTIT
TYKDAHNMRV MKFSVSPVVR VAVEAKNPAD LPKLVEGLKR LAKSDPMVQC IFEESGEHII
AGAGELHLEI CLKDLEEDHA CIPLKKSDPV VSYRETVQSE SNQICLSKSP NKHNRLHCTA
QPMPDGLADD IEGGTVNARD EFKARAKILA EKYEYDVTEA RKIWCFGPDG TGPNLLMDVT
KGVQYLNEIK DSVVAGFQWA TREGVLSDEN MRGVRFNVHD VTLHADAIHR GGGQIIPTAR
RVFYASVLTA EPRLLEPVYL VEIQCPEAAV GGIYGVLNRR RGHVFEESQV TGTPMFVVKA
YLPVNESFGF TADLRSNTGG QAFPQCVFDH WQVLPGDPLE AGTKPNQIVL DTRKRKGLKE
GVPALDNYLD KM
