EF1G_CAEEL
ID EF1G_CAEEL Reviewed; 398 AA.
AC P54412; Q2PJ76; Q8I4K9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable elongation factor 1-gamma;
DE Short=EF-1-gamma;
DE AltName: Full=eEF-1B gamma;
GN Name=eef-1G {ECO:0000312|WormBase:F17C11.9a};
GN ORFNames=F17C11.9 {ECO:0000312|WormBase:F17C11.9a};
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 [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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX PubMed=22579749; DOI=10.1016/j.jprot.2012.04.038;
RA Tohsato Y., Monobe K., Suzuki K., Hayano T., Kawasaki I., Ito M.;
RT "Comparative proteomic analysis reveals differentially expressed proteins
RT in Caenorhabditis elegans pgl-1 mutants grown at 20 degrees C and 25
RT degrees C.";
RL J. Proteomics 75:4792-4801(2012).
RN [3]
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: Probably plays a role in anchoring the complex to other
CC cellular components. {ECO:0000250|UniProtKB:P29547}.
CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and
CC gamma. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:F17C11.9a};
CC IsoId=P54412-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F17C11.9b};
CC IsoId=P54412-2; Sequence=VSP_053653, VSP_053654;
CC Name=c {ECO:0000312|WormBase:F17C11.9c};
CC IsoId=P54412-3; Sequence=VSP_053655;
CC -!- PTM: AMPylated by fic-1. {ECO:0000269|PubMed:27138431}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in 100% sterility
CC at 25 degrees Celsius. {ECO:0000269|PubMed:22579749}.
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DR EMBL; Z72507; CAA96631.1; -; Genomic_DNA.
DR EMBL; Z72507; CAD56569.1; -; Genomic_DNA.
DR EMBL; Z72507; CAJ55245.1; -; Genomic_DNA.
DR PIR; T21061; T21061.
DR RefSeq; NP_001041100.1; NM_001047635.4. [P54412-3]
DR RefSeq; NP_505800.1; NM_073399.5. [P54412-1]
DR RefSeq; NP_872125.1; NM_182325.6.
DR AlphaFoldDB; P54412; -.
DR SMR; P54412; -.
DR BioGRID; 44550; 54.
DR DIP; DIP-24841N; -.
DR IntAct; P54412; 5.
DR STRING; 6239.F17C11.9a; -.
DR EPD; P54412; -.
DR PaxDb; P54412; -.
DR PeptideAtlas; P54412; -.
DR EnsemblMetazoa; F17C11.9a.1; F17C11.9a.1; WBGene00008920. [P54412-1]
DR EnsemblMetazoa; F17C11.9b.1; F17C11.9b.1; WBGene00008920. [P54412-2]
DR EnsemblMetazoa; F17C11.9b.2; F17C11.9b.2; WBGene00008920. [P54412-2]
DR EnsemblMetazoa; F17C11.9b.3; F17C11.9b.3; WBGene00008920. [P54412-2]
DR EnsemblMetazoa; F17C11.9c.1; F17C11.9c.1; WBGene00008920. [P54412-3]
DR GeneID; 179522; -.
DR KEGG; cel:CELE_F17C11.9; -.
DR UCSC; F17C11.9a; c. elegans.
DR CTD; 179522; -.
DR WormBase; F17C11.9a; CE05656; WBGene00008920; eef-1G. [P54412-1]
DR WormBase; F17C11.9b; CE32385; WBGene00008920; eef-1G. [P54412-2]
DR WormBase; F17C11.9c; CE39492; WBGene00008920; eef-1G. [P54412-3]
DR eggNOG; KOG0867; Eukaryota.
DR eggNOG; KOG1627; Eukaryota.
DR GeneTree; ENSGT00390000007552; -.
DR InParanoid; P54412; -.
DR OMA; TRWYETI; -.
DR OrthoDB; 1341490at2759; -.
DR PhylomeDB; P54412; -.
DR PRO; PR:P54412; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00008920; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.30.70.1010; -; 1.
DR InterPro; IPR001662; EF1B_G_C.
DR InterPro; IPR036433; EF1B_G_C_sf.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004046; GST_C.
DR Pfam; PF00647; EF1G; 1.
DR Pfam; PF00043; GST_C; 1.
DR SMART; SM01183; EF1G; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF89942; SSF89942; 1.
DR PROSITE; PS50040; EF1G_C; 1.
DR PROSITE; PS50405; GST_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Elongation factor; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..398
FT /note="Probable elongation factor 1-gamma"
FT /id="PRO_0000208823"
FT DOMAIN 66..199
FT /note="GST C-terminal"
FT DOMAIN 239..398
FT /note="EF-1-gamma C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519"
FT REGION 210..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..25
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053653"
FT VAR_SEQ 26..44
FT /note="KTVTLAGDAAPADKFPLGV -> MLLQLTSSHLELYVLIYLD (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_053654"
FT VAR_SEQ 119..151
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_053655"
SQ SEQUENCE 398 AA; 44388 MW; 943174C4CABE96E8 CRC64;
MTGKLYGNKD NFRTQKVLIA AKLANKTVTL AGDAAPADKF PLGVTPAFEG DALLFGAESI
GLHLTGTSAN AETVQWLQFA EGYLLPAVLG YVLPSVSAAN FDKKTVEQYK NELNGQLQVL
DRVLVKKTYL VGERLSLADV SVALDLLPAF QYVLDANARK SIVNVTRWFR TVVNQPAVKE
VLGEVSLASS VAQFNQAKFT ELSAKVAKSA PKAEKPKKEA KPAAAAAQPE DDEPKEEKSK
DPFQDMPKGT FVLDNFKRSY SNEDTATKAI PHFWENFDAD NWSIWKCEYK YPEDLTLAFM
SCNLINGMYQ RLEKLKKNAF ASMILFGTDN NSTISGIWVW KGDKLAFELS PDWQVDYESY
TWTKLDAKSD ATKKEVNEYL MWEGDFGGKK FNQGKIFK
