EIF3I_MOUSE
ID EIF3I_MOUSE Reviewed; 325 AA.
AC Q9QZD9;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 164.
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 subunit 2 {ECO:0000255|HAMAP-Rule:MF_03008};
DE AltName: Full=TGF-beta receptor-interacting protein 1;
DE Short=TRIP-1;
DE AltName: Full=eIF-3-beta {ECO:0000255|HAMAP-Rule:MF_03008};
DE AltName: Full=eIF3 p36 {ECO:0000255|HAMAP-Rule:MF_03008};
GN Name=Eif3i; Synonyms=Eif3s2, Trip1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhou A., Silverman R.H.;
RT "Mouse TRIP-1 gene isolated from murine L-929 cells.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Joseph P., Fan L., Whong W.-Z., Ong T.-M.;
RT "Mus musculus TGF-beta receptor interacting protein 1 (TRIP1).";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic stem cell, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 269-280.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH EIF3B AND EIF4G1.
RX PubMed=16541103; DOI=10.1038/sj.emboj.7601047;
RA Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E.,
RA Lawrence J.C. Jr.;
RT "mTOR-dependent stimulation of the association of eIF4G and eIF3 by
RT insulin.";
RL EMBO J. 25:1659-1668(2006).
RN [7]
RP FUNCTION, CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE
RP EIF-3 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis. The eIF-3 complex associates with the 40S
CC ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC required for disassembly and recycling of post-termination ribosomal
CC complexes and subsequently prevents premature joining of the 40S and
CC 60S ribosomal subunits prior to initiation. The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression.
CC {ECO:0000255|HAMAP-Rule:MF_03008, ECO:0000269|PubMed:17581632}.
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 may interact with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation may lead to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-
CC Rule:MF_03008, ECO:0000269|PubMed:16541103,
CC ECO:0000269|PubMed:17581632}.
CC -!- INTERACTION:
CC Q9QZD9; Q6NZJ6: Eif4g1; NbExp=3; IntAct=EBI-7466616, EBI-8175606;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
CC -!- PTM: Phosphorylated by TGF-beta type II receptor. {ECO:0000255|HAMAP-
CC Rule:MF_03008}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit I family. {ECO:0000255|HAMAP-
CC Rule:MF_03008}.
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DR EMBL; AF188297; AAF01455.1; -; mRNA.
DR EMBL; AF271072; AAF76199.1; -; mRNA.
DR EMBL; AK012375; BAB28197.1; -; mRNA.
DR EMBL; AK002896; BAB22440.1; -; mRNA.
DR EMBL; AK010781; BAB27177.1; -; mRNA.
DR EMBL; BC029625; AAH29625.1; -; mRNA.
DR CCDS; CCDS18698.1; -.
DR RefSeq; NP_061269.1; NM_018799.2.
DR AlphaFoldDB; Q9QZD9; -.
DR SMR; Q9QZD9; -.
DR BioGRID; 207720; 80.
DR IntAct; Q9QZD9; 60.
DR MINT; Q9QZD9; -.
DR STRING; 10090.ENSMUSP00000099653; -.
DR iPTMnet; Q9QZD9; -.
DR PhosphoSitePlus; Q9QZD9; -.
DR SwissPalm; Q9QZD9; -.
DR REPRODUCTION-2DPAGE; Q9QZD9; -.
DR CPTAC; non-CPTAC-3913; -.
DR EPD; Q9QZD9; -.
DR jPOST; Q9QZD9; -.
DR MaxQB; Q9QZD9; -.
DR PaxDb; Q9QZD9; -.
DR PeptideAtlas; Q9QZD9; -.
DR PRIDE; Q9QZD9; -.
DR ProteomicsDB; 277775; -.
DR DNASU; 54709; -.
DR Ensembl; ENSMUST00000102593; ENSMUSP00000099653; ENSMUSG00000028798.
DR GeneID; 54709; -.
DR KEGG; mmu:54709; -.
DR UCSC; uc008uxm.2; mouse.
DR CTD; 8668; -.
DR MGI; MGI:1860763; Eif3i.
DR VEuPathDB; HostDB:ENSMUSG00000028798; -.
DR eggNOG; KOG0643; Eukaryota.
DR GeneTree; ENSGT00940000161371; -.
DR HOGENOM; CLU_043845_0_0_1; -.
DR InParanoid; Q9QZD9; -.
DR OMA; VWFSHNG; -.
DR OrthoDB; 866359at2759; -.
DR PhylomeDB; Q9QZD9; -.
DR TreeFam; TF101515; -.
DR Reactome; R-MMU-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-MMU-72649; Translation initiation complex formation.
DR Reactome; R-MMU-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-MMU-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-MMU-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-MMU-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR BioGRID-ORCS; 54709; 26 hits in 71 CRISPR screens.
DR ChiTaRS; Eif3i; mouse.
DR PRO; PR:Q9QZD9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9QZD9; protein.
DR Bgee; ENSMUSG00000028798; Expressed in floor plate of midbrain and 242 other tissues.
DR ExpressionAtlas; Q9QZD9; baseline and differential.
DR Genevisible; Q9QZD9; MM.
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:UniProtKB.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:MGI.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
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; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Direct protein sequencing; Initiation factor;
KW Isopeptide bond; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..325
FT /note="Eukaryotic translation initiation factor 3 subunit
FT I"
FT /id="PRO_0000051037"
FT REPEAT 8..47
FT /note="WD 1"
FT REPEAT 50..91
FT /note="WD 2"
FT REPEAT 144..183
FT /note="WD 3"
FT REPEAT 186..225
FT /note="WD 4"
FT REPEAT 283..324
FT /note="WD 5"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13347"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13347"
FT MOD_RES 308
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13347"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13347"
SQ SEQUENCE 325 AA; 36461 MW; 2B29405772675CC0 CRC64;
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
FVSFFDLRDP SQIDSNEPYM KIPCNDSKIT SAVWGPLGEC VIAGHESGEL NQYSAKSGEV
LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN
YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY
SSGGEDGYVR IHYFDPQYFE FEFEA
