EIF3I_YEAST
ID EIF3I_YEAST Reviewed; 347 AA.
AC P40217; D6VZW8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit I {ECO:0000255|HAMAP-Rule:MF_03008};
DE Short=eIF3i {ECO:0000255|HAMAP-Rule:MF_03008};
DE AltName: Full=Eukaryotic translation initiation factor 3 39 kDa subunit;
DE Short=eIF-3 39 kDa subunit;
DE Short=eIF3 p39;
GN Name=TIF34 {ECO:0000255|HAMAP-Rule:MF_03008}; OrderedLocusNames=YMR146C;
GN ORFNames=YM9375.16C;
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].
RC STRAIN=W303D;
RX PubMed=8972194; DOI=10.1128/mcb.17.1.145;
RA Naranda T., Kainuma M., Macmillan S.E., Hershey J.W.B.;
RT "The 39-kilodalton subunit of eukaryotic translation initiation factor 3 is
RT essential for the complex's integrity and for cell viability in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:145-153(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, 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 [9]
RP IDENTIFICATION IN THE EIF-3 COMPLEX WITH NIP1; PRT1; TIF32 AND TIF35.
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).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC ribosome. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation.
CC {ECO:0000255|HAMAP-Rule:MF_03008}.
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 P40217; P06103: PRT1; NbExp=17; IntAct=EBI-8951, EBI-8973;
CC P40217; P38249: RPG1; NbExp=8; IntAct=EBI-8951, EBI-8981;
CC P40217; Q04067: TIF35; NbExp=7; IntAct=EBI-8951, EBI-8958;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
CC -!- MISCELLANEOUS: Present with 2400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit I family. {ECO:0000255|HAMAP-
CC Rule:MF_03008}.
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; U56937; AAC49616.1; -; Genomic_DNA.
DR EMBL; Z47071; CAA87361.1; -; Genomic_DNA.
DR EMBL; AY558416; AAS56742.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10042.1; -; Genomic_DNA.
DR PIR; S50403; S50403.
DR RefSeq; NP_013866.1; NM_001182648.1.
DR PDB; 3JAP; EM; 4.90 A; q=1-347.
DR PDB; 3JAQ; EM; 6.00 A; q=1-347.
DR PDB; 3ZWL; X-ray; 2.20 A; B/D=1-347.
DR PDB; 5A5U; EM; 9.00 A; I=1-347.
DR PDB; 6FYX; EM; 3.05 A; s=1-347.
DR PDB; 6FYY; EM; 3.05 A; s=1-347.
DR PDB; 6GSM; EM; 5.15 A; s=1-342.
DR PDB; 6GSN; EM; 5.75 A; s=1-342.
DR PDB; 6ZCE; EM; 5.30 A; l=1-347.
DR PDB; 6ZU9; EM; 6.20 A; l=1-347.
DR PDBsum; 3JAP; -.
DR PDBsum; 3JAQ; -.
DR PDBsum; 3ZWL; -.
DR PDBsum; 5A5U; -.
DR PDBsum; 6FYX; -.
DR PDBsum; 6FYY; -.
DR PDBsum; 6GSM; -.
DR PDBsum; 6GSN; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZU9; -.
DR AlphaFoldDB; P40217; -.
DR SMR; P40217; -.
DR BioGRID; 35322; 391.
DR ComplexPortal; CPX-1831; Eukaryotic translation initiation factor 3 core complex.
DR DIP; DIP-2520N; -.
DR IntAct; P40217; 24.
DR MINT; P40217; -.
DR STRING; 4932.YMR146C; -.
DR iPTMnet; P40217; -.
DR MaxQB; P40217; -.
DR PaxDb; P40217; -.
DR PRIDE; P40217; -.
DR EnsemblFungi; YMR146C_mRNA; YMR146C; YMR146C.
DR GeneID; 855177; -.
DR KEGG; sce:YMR146C; -.
DR SGD; S000004754; TIF34.
DR VEuPathDB; FungiDB:YMR146C; -.
DR eggNOG; KOG0643; Eukaryota.
DR GeneTree; ENSGT00940000167369; -.
DR HOGENOM; CLU_043845_0_1_1; -.
DR InParanoid; P40217; -.
DR OMA; VWFSHNG; -.
DR BioCyc; YEAST:G3O-32838-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
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 EvolutionaryTrace; P40217; -.
DR PRO; PR:P40217; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40217; 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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IBA:GO_Central.
DR GO; GO:0043614; C:multi-eIF complex; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:SGD.
DR GO; GO:0002183; P:cytoplasmic translational initiation; 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 Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03008; eIF3i; 1.
DR InterPro; IPR027525; eIF3i.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..347
FT /note="Eukaryotic translation initiation factor 3 subunit
FT I"
FT /id="PRO_0000051041"
FT REPEAT 8..47
FT /note="WD 1"
FT REPEAT 50..89
FT /note="WD 2"
FT REPEAT 149..190
FT /note="WD 3"
FT REPEAT 194..233
FT /note="WD 4"
FT REPEAT 291..330
FT /note="WD 5"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 24..32
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:3ZWL"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:3ZWL"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:3ZWL"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3ZWL"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:3ZWL"
FT TURN 182..186
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:3ZWL"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:3ZWL"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 296..301
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:3ZWL"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:3ZWL"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:3ZWL"
FT HELIX 332..339
FT /evidence="ECO:0007829|PDB:3ZWL"
SQ SEQUENCE 347 AA; 38755 MW; E6C0D0B275E87622 CRC64;
MKAIKLTGHE RPLTQVKYNK EGDLLFSCSK DSSASVWYSL NGERLGTLDG HTGTIWSIDV
DCFTKYCVTG SADYSIKLWD VSNGQCVATW KSPVPVKRVE FSPCGNYFLA ILDNVMKNPG
SINIYEIERD SATHELTKVS EEPIHKIITH EGLDAATVAG WSTKGKYIIA GHKDGKISKY
DVSNNYEYVD SIDLHEKSIS DMQFSPDLTY FITSSRDTNS FLVDVSTLQV LKKYETDCPL
NTAVITPLKE FIILGGGQEA KDVTTTSANE GKFEARFYHK IFEEEIGRVQ GHFGPLNTVA
ISPQGTSYAS GGEDGFIRLH HFEKSYFDFK YDVEKAAEAK EHMQEAN
