EIF3G_BOVIN
ID EIF3G_BOVIN Reviewed; 320 AA.
AC Q3ZC12;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 {ECO:0000255|HAMAP-Rule:MF_03006};
GN Synonyms=EIF3S4 {ECO:0000255|HAMAP-Rule:MF_03006};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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 interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of FRAP1 and RAPTOR, 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). Interacts with DHX33; the interaction is
CC independent of RNA (By similarity). {ECO:0000250|UniProtKB:O75821,
CC ECO:0000255|HAMAP-Rule:MF_03006}.
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; BC102984; AAI02985.1; -; mRNA.
DR RefSeq; NP_001073091.1; NM_001079623.2.
DR AlphaFoldDB; Q3ZC12; -.
DR BMRB; Q3ZC12; -.
DR SMR; Q3ZC12; -.
DR STRING; 9913.ENSBTAP00000003545; -.
DR PaxDb; Q3ZC12; -.
DR PeptideAtlas; Q3ZC12; -.
DR PRIDE; Q3ZC12; -.
DR GeneID; 615695; -.
DR KEGG; bta:615695; -.
DR CTD; 8666; -.
DR eggNOG; KOG0122; Eukaryota.
DR InParanoid; Q3ZC12; -.
DR OrthoDB; 1226059at2759; -.
DR Proteomes; UP000009136; Unplaced.
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: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; 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 2: Evidence at transcript 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_0000246085"
FT DOMAIN 239..317
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..234
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:0000250|UniProtKB:O75821, ECO:0000255|HAMAP-
FT Rule:MF_03006"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75821, ECO:0000255|HAMAP-
FT Rule:MF_03006"
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"
SQ SEQUENCE 320 AA; 35655 MW; 11789F369E961BEF CRC64;
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSLEPELLPG APLPPPKEVI
NGNIKTVTEY RIDEDGKKFK IVRTFRIETR KASKAVARRK NWKKFGNSEF DPPGPNVATT
TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK
ELAEQLGLST GEKEKLPGEL EPVQATQNKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT
IRVTNLSEDT RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV
SGFGYDHLIL NVEWAKPSTN
