EIF3G_YEAST
ID EIF3G_YEAST Reviewed; 274 AA.
AC Q04067; D6VT58;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
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=Translation initiation factor eIF3 p33 subunit;
DE Short=eIF3 p33;
GN Name=TIF35 {ECO:0000255|HAMAP-Rule:MF_03006}; OrderedLocusNames=YDR429C;
GN ORFNames=D9461.16;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND RNA-BINDING.
RC STRAIN=ATCC 200060 / W303;
RX PubMed=10085088; DOI=10.1074/jbc.274.13.8546;
RA Hanachi P., Hershey J.W.B., Vornlocher H.-P.;
RT "Characterization of the p33 subunit of eukaryotic translation initiation
RT factor-3 from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 274:8546-8553(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP IDENTIFICATION IN THE EIF-3 CORE COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9671501; DOI=10.1128/mcb.18.8.4935;
RA Phan L., Zhang X., Asano K., Anderson J., Vornlocher H.-P., Greenberg J.R.,
RA Qin J., Hinnebusch A.G.;
RT "Identification of a translation initiation factor 3 (eIF3) core complex,
RT conserved in yeast and mammals, that interacts with eIF5.";
RL Mol. Cell. Biol. 18:4935-4946(1998).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP INTERACTION WITH PRT1, AND ASSOCIATION WITH THE 40S RIBOSOME.
RX PubMed=16581774; DOI=10.1128/mcb.26.8.2984-2998.2006;
RA Nielsen K.H., Valasek L., Sykes C., Jivotovskaya A., Hinnebusch A.G.;
RT "Interaction of the RNP1 motif in PRT1 with HCR1 promotes 40S binding of
RT eukaryotic initiation factor 3 in yeast.";
RL Mol. Cell. Biol. 26:2984-2998(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP IDENTIFICATION IN THE EIF-3 COMPLEX WITH NIP1; PRT1; TIF32 AND TIF34.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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
CC (Potential). Binds to the 18S rRNA but non-specifically
CC (PubMed:10085088). {ECO:0000255|HAMAP-Rule:MF_03006,
CC ECO:0000269|PubMed:10085088}.
CC -!- SUBUNIT: The eukaryotic translation initiation factor 3 (eIF-3) core
CC complex is composed of TIF32, PRT1, NIP1, TIF34 and TIF35. The factors
CC eIF-1, eIF-2, eIF-3, TIF5/eIF-5 and methionyl-tRNAi form a multifactor
CC complex (MFC) that may bind to the 40S ribosome.
CC {ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:9671501}.
CC -!- INTERACTION:
CC Q04067; P06103: PRT1; NbExp=14; IntAct=EBI-8958, EBI-8973;
CC Q04067; P40217: TIF34; NbExp=7; IntAct=EBI-8958, EBI-8951;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006,
CC ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000255|HAMAP-
CC Rule:MF_03006}.
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DR EMBL; AF004913; AAB82418.1; -; Genomic_DNA.
DR EMBL; U33007; AAB64884.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12268.1; -; Genomic_DNA.
DR PIR; S69710; S69710.
DR RefSeq; NP_010717.1; NM_001180737.1.
DR PDB; 3JAP; EM; 4.90 A; s=45-96.
DR PDB; 3JAQ; EM; 6.00 A; s=45-96.
DR PDB; 4U1E; X-ray; 2.00 A; G=1-135.
DR PDB; 6FYX; EM; 3.05 A; r=1-274.
DR PDB; 6FYY; EM; 3.05 A; r=1-274.
DR PDB; 6GSM; EM; 5.15 A; r=48-96.
DR PDB; 6GSN; EM; 5.75 A; r=48-96.
DR PDB; 6ZCE; EM; 5.30 A; r=1-274.
DR PDB; 6ZU9; EM; 6.20 A; r=1-135.
DR PDBsum; 3JAP; -.
DR PDBsum; 3JAQ; -.
DR PDBsum; 4U1E; -.
DR PDBsum; 6FYX; -.
DR PDBsum; 6FYY; -.
DR PDBsum; 6GSM; -.
DR PDBsum; 6GSN; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR AlphaFoldDB; Q04067; -.
DR SMR; Q04067; -.
DR BioGRID; 32487; 126.
DR ComplexPortal; CPX-1831; Eukaryotic translation initiation factor 3 core complex.
DR DIP; DIP-1704N; -.
DR IntAct; Q04067; 46.
DR MINT; Q04067; -.
DR STRING; 4932.YDR429C; -.
DR iPTMnet; Q04067; -.
DR MaxQB; Q04067; -.
DR PaxDb; Q04067; -.
DR PRIDE; Q04067; -.
DR EnsemblFungi; YDR429C_mRNA; YDR429C; YDR429C.
DR GeneID; 852039; -.
DR KEGG; sce:YDR429C; -.
DR SGD; S000002837; TIF35.
DR VEuPathDB; FungiDB:YDR429C; -.
DR eggNOG; KOG0122; Eukaryota.
DR GeneTree; ENSGT00510000047802; -.
DR HOGENOM; CLU_034595_0_0_1; -.
DR InParanoid; Q04067; -.
DR OMA; TTKCPFK; -.
DR BioCyc; YEAST:G3O-29968-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q04067; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04067; protein.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
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:SGD.
DR GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:SGD.
DR GO; GO:0002188; P:translation reinitiation; IMP:SGD.
DR GO; GO:0006413; P:translational initiation; IDA:SGD.
DR GO; GO:0006415; P:translational termination; IMP:SGD.
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 3D-structure; Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..274
FT /note="Eukaryotic translation initiation factor 3 subunit
FT G"
FT /id="PRO_0000123514"
FT DOMAIN 191..270
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT REGION 137..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:4U1E"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:4U1E"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:4U1E"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:4U1E"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4U1E"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:4U1E"
SQ SEQUENCE 274 AA; 30501 MW; 340A5285F2C84E06 CRC64;
MSEVAPEEII ENADGSRSII TYKIEDGVKY KITQKVKEVK VLEKVHKSVA ERKNWHKYGS
EKGSPAGPSA VTARLGEEVE LRLSRNWKQA EEERIQKEKA SLTKTGLQCR LCGNDHMTMN
CPFKTILSEL SALEDPATNE GGVEAASEEK AGQVGGAGSI PGQYVPPSRR AGARDPSSDA
YRDSRERDDM CTLKIMQVNE NADENSLREE LLFPFAPIPR VSVVRNKETG KSRGLAFVTF
SSEEVAEQAL RFLDGRGYMN LILRVEWSKP KVKE
