EI3G1_DROME
ID EI3G1_DROME Reviewed; 269 AA.
AC Q9W4X7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit G-1 {ECO:0000312|FlyBase:FBgn0029629};
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit 1 {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF-3 RNA-binding subunit 1 {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 4-1 {ECO:0000255|HAMAP-Rule:MF_03006};
GN Name=eIF3g1 {ECO:0000312|FlyBase:FBgn0029629};
GN Synonyms=eIF3-S4 {ECO:0000255|HAMAP-Rule:MF_03006},
GN eIF3ga {ECO:0000312|FlyBase:FBgn0029629};
GN ORFNames=CG8636 {ECO:0000312|FlyBase:FBgn0029629};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(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. The eIF-3 complex interacts with pix.
CC {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}.
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DR EMBL; AE014298; AAF45796.1; -; Genomic_DNA.
DR EMBL; AY118933; AAM50793.1; -; mRNA.
DR RefSeq; NP_570011.1; NM_130655.2.
DR AlphaFoldDB; Q9W4X7; -.
DR SMR; Q9W4X7; -.
DR BioGRID; 57774; 14.
DR IntAct; Q9W4X7; 2.
DR STRING; 7227.FBpp0070430; -.
DR iPTMnet; Q9W4X7; -.
DR PaxDb; Q9W4X7; -.
DR PRIDE; Q9W4X7; -.
DR DNASU; 31243; -.
DR EnsemblMetazoa; FBtr0070446; FBpp0070430; FBgn0029629.
DR GeneID; 31243; -.
DR KEGG; dme:Dmel_CG8636; -.
DR UCSC; CG8636-RA; d. melanogaster.
DR CTD; 31243; -.
DR FlyBase; FBgn0029629; eIF3g1.
DR VEuPathDB; VectorBase:FBgn0029629; -.
DR eggNOG; KOG0122; Eukaryota.
DR GeneTree; ENSGT00510000047802; -.
DR HOGENOM; CLU_034595_0_0_1; -.
DR InParanoid; Q9W4X7; -.
DR OMA; TTKCPFK; -.
DR OrthoDB; 1226059at2759; -.
DR PhylomeDB; Q9W4X7; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR BioGRID-ORCS; 31243; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 31243; -.
DR PRO; PR:Q9W4X7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029629; Expressed in eye disc (Drosophila) and 49 other tissues.
DR Genevisible; Q9W4X7; DM.
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:FlyBase.
DR GO; GO:0003729; F:mRNA binding; ISS:FlyBase.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:FlyBase.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0000278; P:mitotic cell cycle; HMP:FlyBase.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
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..269
FT /note="Eukaryotic translation initiation factor 3 subunit
FT G-1"
FT /id="PRO_0000365413"
FT DOMAIN 188..266
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006,
FT ECO:0000269|PubMed:17372656, ECO:0000269|PubMed:18327897"
SQ SEQUENCE 269 AA; 29946 MW; 5C41B0B94248B969 CRC64;
MPGVETIKSS WADEVELDYG GLPPTTETVE NGQKYVTEYK YNKDDKKTKV VRTYKISKQV
VPKTVAKRRT WTKFGDSKND KPGPNSQTTM VSEEIIMQFL NSKEDEKAND PLLDPTKNIA
KCRICNGEHW SVNCPYKGTA MDTNMMEKKA SAAAAAAVDA PKSGKYVPPF LKDSQKGALG
MRGRDDTAAI RISNLSESMT EADLEELVKK IGPQSKMYLA RDKNTGLCKG FAYVHFKQRK
DAAAAIEILN GHGYDHLILS VEWSKPQNN
