EIF3G_MOUSE
ID EIF3G_MOUSE Reviewed; 320 AA.
AC Q9Z1D1; Q9R079;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 171.
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};
DE AltName: Full=eIF-3-delta {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=eIF3 p42 {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=eIF3 p44 {ECO:0000255|HAMAP-Rule:MF_03006};
GN Name=Eif3g; Synonyms=Eif3p42, Eif3s4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Asano K., Hershey J.W.B., Hinnebusch A.G.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1;
RA Valentijn L.J., Hoff E.I., Baas F.;
RT "5'-AMP-activated protein kinase subunit beta interacts with the p42
RT subunit of translation initiation factor eIF3.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP FUNCTION, CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE
RP EIF-3 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP INTERACTION WITH DHX33.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is required for several
CC steps in the initiation of protein synthesis. The eIF-3 complex
CC associates with the 40S ribosome and facilitates the recruitment of
CC eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
CC initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly and
CC recycling of post-termination ribosomal complexes and subsequently
CC prevents premature joining of the 40S and 60S ribosomal subunits prior
CC to initiation. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation,
CC including cell cycling, differentiation and apoptosis, and uses
CC different modes of RNA stem-loop binding to exert either translational
CC activation or repression. This subunit can bind 18S rRNA.
CC {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17581632}.
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. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC may interact with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation may lead to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Interacts (via C-terminus) with
CC AIFM1 (via N-terminus) (By similarity). Interacts with DHX33; the
CC interaction is independent of RNA (PubMed:26100019).
CC {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:26100019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03006}. Cytoplasm, perinuclear
CC region {ECO:0000255|HAMAP-Rule:MF_03006}. Note=Colocalizes with AIFM1
CC in the nucleus and perinuclear region. {ECO:0000255|HAMAP-
CC Rule:MF_03006}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03006}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000255|HAMAP-
CC Rule:MF_03006}.
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DR EMBL; U70733; AAD00176.1; -; mRNA.
DR EMBL; AF108214; AAF14221.1; -; mRNA.
DR EMBL; BC008511; AAH08511.1; -; mRNA.
DR CCDS; CCDS40547.1; -.
DR RefSeq; NP_058572.2; NM_016876.3.
DR AlphaFoldDB; Q9Z1D1; -.
DR SMR; Q9Z1D1; -.
DR BioGRID; 207295; 54.
DR IntAct; Q9Z1D1; 7.
DR MINT; Q9Z1D1; -.
DR STRING; 10090.ENSMUSP00000004206; -.
DR iPTMnet; Q9Z1D1; -.
DR PhosphoSitePlus; Q9Z1D1; -.
DR SwissPalm; Q9Z1D1; -.
DR REPRODUCTION-2DPAGE; Q9Z1D1; -.
DR EPD; Q9Z1D1; -.
DR jPOST; Q9Z1D1; -.
DR MaxQB; Q9Z1D1; -.
DR PaxDb; Q9Z1D1; -.
DR PRIDE; Q9Z1D1; -.
DR ProteomicsDB; 275654; -.
DR Antibodypedia; 12724; 286 antibodies from 30 providers.
DR DNASU; 53356; -.
DR Ensembl; ENSMUST00000004206; ENSMUSP00000004206; ENSMUSG00000070319.
DR GeneID; 53356; -.
DR KEGG; mmu:53356; -.
DR UCSC; uc009ojm.1; mouse.
DR CTD; 8666; -.
DR MGI; MGI:1858258; Eif3g.
DR VEuPathDB; HostDB:ENSMUSG00000070319; -.
DR eggNOG; KOG0122; Eukaryota.
DR GeneTree; ENSGT00510000047802; -.
DR HOGENOM; CLU_034595_0_0_1; -.
DR InParanoid; Q9Z1D1; -.
DR OMA; TTKCPFK; -.
DR OrthoDB; 1226059at2759; -.
DR PhylomeDB; Q9Z1D1; -.
DR TreeFam; TF101516; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR BioGRID-ORCS; 53356; 30 hits in 110 CRISPR screens.
DR ChiTaRS; Eif3g; mouse.
DR PRO; PR:Q9Z1D1; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9Z1D1; protein.
DR Bgee; ENSMUSG00000070319; Expressed in dorsal pancreas and 263 other tissues.
DR ExpressionAtlas; Q9Z1D1; baseline and differential.
DR Genevisible; Q9Z1D1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; ISO:MGI.
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; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..320
FT /note="Eukaryotic translation initiation factor 3 subunit
FT G"
FT /id="PRO_0000123511"
FT DOMAIN 239..317
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75821"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75821"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75821, ECO:0000255|HAMAP-
FT Rule:MF_03006"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75821"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75821"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75821"
FT CONFLICT 17..18
FT /note="EE -> AA (in Ref. 1; AAD00176)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="E -> Q (in Ref. 1; AAD00176)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="K -> T (in Ref. 1; AAD00176)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="K -> T (in Ref. 1; AAD00176)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="I -> P (in Ref. 1; AAD00176)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="E -> S (in Ref. 1; AAD00176)"
FT /evidence="ECO:0000305"
FT CONFLICT 222..223
FT /note="AS -> PA (in Ref. 1; AAD00176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 320 AA; 35638 MW; 1B46670351E489AC CRC64;
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLPTGD TSPEPELLPG DPLPPPKEVI
NGNIKTVTEY KIEEDGKKFK IVRTFRIETR KASKAVARRK NWKKFGNSEF DPPGPNVATT
TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK
ELAEQLGLST GEKEKLPGEL EPVQAAQSKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT
IRVTNLSEDT RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV
SGFGYDHLIL NVEWAKPSTN
