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Database: UniProt
Entry: P40217
LinkDB: P40217
Original site: P40217 
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   07-APR-2021, entry version 182.
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}.
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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   SMR; P40217; -.
DR   BioGRID; 35322; 369.
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   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 ATPase 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; IPR017986; WD40_repeat_dom.
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:0007744|PDB:3ZWL"
FT   STRAND          13..18
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          24..32
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          34..38
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   TURN            39..41
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          44..48
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          55..60
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          64..71
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          74..80
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   TURN            81..83
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          86..91
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          96..101
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          105..112
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          121..129
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   TURN            131..133
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          136..139
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          144..148
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          156..161
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   HELIX           163..165
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          167..172
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          175..181
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   TURN            182..186
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          187..193
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          199..204
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          208..215
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          218..224
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   TURN            225..227
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          230..235
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          240..245
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          247..256
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          267..269
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          274..279
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   TURN            280..282
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          285..290
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          296..301
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          305..312
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   STRAND          315..322
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   HELIX           324..327
FT                   /evidence="ECO:0007744|PDB:3ZWL"
FT   HELIX           332..339
FT                   /evidence="ECO:0007744|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
//
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