EIF3G_DANRE
ID EIF3G_DANRE Reviewed; 293 AA.
AC Q6DRC4; A8E573; Q7ZUH3;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit G {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF3g {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF-3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 4 {ECO:0000255|HAMAP-Rule:MF_03006};
GN Name=eif3g; Synonyms=eif3s4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA Hopkins N.;
RT "Identification of 315 genes essential for early zebrafish development.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation. This
CC subunit can bind 18S rRNA. {ECO:0000255|HAMAP-Rule:MF_03006}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: eif3a, eif3b, eif3c,
CC eif3d, eif3e, eif3f, eif3g, eif3h, eif3i, eif3j, eif3k, eif3l and
CC eif3m. {ECO:0000255|HAMAP-Rule:MF_03006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000255|HAMAP-
CC Rule:MF_03006}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI53490.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY648835; AAT68153.1; -; mRNA.
DR EMBL; BC049046; AAH49046.1; -; mRNA.
DR EMBL; BC153489; AAI53490.1; ALT_FRAME; mRNA.
DR RefSeq; NP_957293.1; NM_200999.1.
DR AlphaFoldDB; Q6DRC4; -.
DR SMR; Q6DRC4; -.
DR STRING; 7955.ENSDARP00000027672; -.
DR PaxDb; Q6DRC4; -.
DR PRIDE; Q6DRC4; -.
DR Ensembl; ENSDART00000018071; ENSDARP00000027672; ENSDARG00000016889.
DR GeneID; 393974; -.
DR KEGG; dre:393974; -.
DR CTD; 8666; -.
DR ZFIN; ZDB-GENE-040426-1076; eif3g.
DR eggNOG; KOG0122; Eukaryota.
DR GeneTree; ENSGT00510000047802; -.
DR HOGENOM; CLU_034595_0_0_1; -.
DR InParanoid; Q6DRC4; -.
DR OMA; TTKCPFK; -.
DR OrthoDB; 1226059at2759; -.
DR PhylomeDB; Q6DRC4; -.
DR TreeFam; TF101516; -.
DR Reactome; R-DRE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DRE-72649; Translation initiation complex formation.
DR Reactome; R-DRE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DRE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DRE-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DRE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q6DRC4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000016889; Expressed in somite and 30 other tissues.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR CDD; cd12933; eIF3G; 1.
DR CDD; cd12408; RRM_eIF3G_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03006; eIF3g; 1.
DR InterPro; IPR017334; eIF3_g.
DR InterPro; IPR024675; eIF3g_N.
DR InterPro; IPR034240; eIF3G_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF12353; eIF3g; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037949; Transl_init_eIF-3_RNA-bind; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT CHAIN 1..293
FT /note="Eukaryotic translation initiation factor 3 subunit
FT G"
FT /id="PRO_0000365397"
FT DOMAIN 212..290
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 124
FT /note="K -> E (in Ref. 2; AAH49046)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="F -> L (in Ref. 2; AAH49046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 32844 MW; CA7895D3313E9B7E CRC64;
MPSIEFDDSK PSWADQVEEE GDEGSLPSPK ETVKGNIKTV TEYKIDDDGQ KFKIIRTFKI
ETRKASKAVA RRKNWKKFGN SEYDAPGPNV ATTTVSDDVF MTFISSKEDL NAQDQDEDPM
NKLKGQKIVS CRICKGDHWT TRCPYKDTLG PMQKELAEQL GLSTGEKEKA AEPEPAQPVQ
NKTGKYVPPS LRDGGTRRGE SMQPNRRADD NATIRVTNLS EDTRETDLQE LFRPFGSISR
IYLAKDKNTG QSKGFAFISF HRREDAARAI AGVSGFGYDH LILNVEWAKP SNN