EIF3I_RABIT
ID EIF3I_RABIT Reviewed; 333 AA.
AC Q5IH81;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=eIF-3-beta {ECO:0000255|HAMAP-Rule:MF_03008};
DE AltName: Full=eIF3 p36 {ECO:0000255|HAMAP-Rule:MF_03008};
GN Name=EIF3I {ECO:0000255|HAMAP-Rule:MF_03008};
GN Synonyms=EIF3S2 {ECO:0000255|HAMAP-Rule:MF_03008};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=16155408; DOI=10.1038/emm.2005.41;
RA Fauchon M.A., Pell T.J., Baxter G.F., Yellon D.M., Latchman D.S.,
RA Hubank M.F., Mayne L.V.;
RT "Representational difference analysis of cDNA identifies novel genes
RT expressed following preconditioning of the heart.";
RL Exp. Mol. Med. 37:311-322(2005).
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}.
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 interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads 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}.
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; AY727926; AAW28137.1; -; mRNA.
DR RefSeq; NP_001075647.1; NM_001082178.1.
DR PDB; 5K0Y; EM; 5.80 A; T=1-329.
DR PDBsum; 5K0Y; -.
DR AlphaFoldDB; Q5IH81; -.
DR SMR; Q5IH81; -.
DR DIP; DIP-61828N; -.
DR IntAct; Q5IH81; 9.
DR STRING; 9986.ENSOCUP00000006589; -.
DR GeneID; 100008959; -.
DR KEGG; ocu:100008959; -.
DR CTD; 8668; -.
DR eggNOG; KOG0643; Eukaryota.
DR InParanoid; Q5IH81; -.
DR OrthoDB; 866359at2759; -.
DR Proteomes; UP000001811; Unplaced.
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:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006413; P:translational initiation; ISS: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 3D-structure; Acetylation; Cytoplasm; Initiation factor; Isopeptide bond;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW Ubl conjugation; WD repeat.
FT CHAIN 1..333
FT /note="Eukaryotic translation initiation factor 3 subunit
FT I"
FT /id="PRO_0000365330"
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 333 AA; 37325 MW; 50D49B0AB7F66A2B CRC64;
MRPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV
LVNVKEHSRQ INDIQLSREM TMFVTASKDN TAKLFDSTTL EHQKTFRTEP PRELAALSPN
YEHVVVGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY
SSGGEDGYVR IHYFDPQYFE FEFEAREAGS PSG
