EIF3B_RAT
ID EIF3B_RAT Reviewed; 797 AA.
AC Q4G061;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001};
DE Short=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 9 {ECO:0000255|HAMAP-Rule:MF_03001};
DE AltName: Full=eIF-3-eta {ECO:0000255|HAMAP-Rule:MF_03001};
GN Name=Eif3b; Synonyms=Eif3s9;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; SER-40; SER-75; SER-79;
RP SER-114; SER-117; SER-135; SER-137 AND SER-147, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is required for several
CC steps in the initiation of protein synthesis. The eIF-3 complex
CC associates with the 40S ribosome and facilitates the recruitment of
CC eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
CC initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly and
CC recycling of post-termination ribosomal complexes and subsequently
CC prevents premature joining of the 40S and 60S ribosomal subunits prior
CC to initiation. The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation,
CC including cell cycling, differentiation and apoptosis, and uses
CC different modes of RNA stem-loop binding to exert either translational
CC activation or repression. {ECO:0000255|HAMAP-Rule:MF_03001}.
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. Also interacts with UPF2 and
CC HNRPD. Interacts with METTL3. Interacts with DDX3X (By similarity).
CC {ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- DOMAIN: The RRM domain mediates interaction with EIF3J.
CC {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; BC098728; AAH98728.1; -; mRNA.
DR RefSeq; NP_001026810.1; NM_001031640.1.
DR AlphaFoldDB; Q4G061; -.
DR SMR; Q4G061; -.
DR BioGRID; 252584; 2.
DR IntAct; Q4G061; 7.
DR MINT; Q4G061; -.
DR STRING; 10116.ENSRNOP00000057188; -.
DR iPTMnet; Q4G061; -.
DR PhosphoSitePlus; Q4G061; -.
DR jPOST; Q4G061; -.
DR PaxDb; Q4G061; -.
DR PRIDE; Q4G061; -.
DR Ensembl; ENSRNOT00000060444; ENSRNOP00000057188; ENSRNOG00000001253.
DR GeneID; 288516; -.
DR KEGG; rno:288516; -.
DR UCSC; RGD:1309018; rat.
DR CTD; 8662; -.
DR RGD; 1309018; Eif3b.
DR eggNOG; KOG2314; Eukaryota.
DR GeneTree; ENSGT00550000074913; -.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; Q4G061; -.
DR OMA; NVADCKI; -.
DR OrthoDB; 1194797at2759; -.
DR Reactome; R-RNO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-RNO-72649; Translation initiation complex formation.
DR Reactome; R-RNO-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-RNO-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-RNO-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-RNO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q4G061; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001253; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q4G061; RN.
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:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:RGD.
DR GO; GO:0031369; F:translation initiation factor binding; IEA:InterPro.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; ISO:RGD.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; ISO:RGD.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03001; eIF3b; 1.
DR InterPro; IPR011400; EIF3B.
DR InterPro; IPR034363; eIF3B_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR013979; TIF_beta_prop-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR14068; PTHR14068; 1.
DR Pfam; PF08662; eIF2A; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF036424; eIF3b; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..797
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000223480"
FT DOMAIN 168..251
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 315..353
FT /note="WD 1"
FT REPEAT 355..400
FT /note="WD 2"
FT REPEAT 404..442
FT /note="WD 3"
FT REPEAT 543..584
FT /note="WD 4"
FT REPEAT 632..677
FT /note="WD 5"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..396
FT /note="Sufficient for interaction with EIF3E"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REGION 153..257
FT /note="Sufficient for interaction with EIF3J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT COMPBIAS 43..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ9"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ9, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ9"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ9"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8JZQ9"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 271
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
FT MOD_RES 347
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
SQ SEQUENCE 797 AA; 90911 MW; DACAA7CABE41EBA2 CRC64;
MQDAENVAAP EAAEERAEPA RQQPVSESPP TDEAAGSGGS EVGRTEDAEE DAEARPEPEV
RAKPAAQSEE ETAASPAASP TPQSAQEPSA PGKAEAGGEQ ARHPSARAEE EGGSDGSAAE
AEPRALENGE ADEPSFSDPE DFVDDVSEEE LLGDVLKDRP QEADGIDSVI VVDNVPQVGP
DRLEKLKNVI HKIFSKFGKI INDYYPEEDG KTKGYIFLEY ASPAHAVDAV KNADGYKLDK
QHTFRVNLFT DFDKYMTISD EWDIPEKQPF KDLGNLRYWL EEAECRDQYS VIFESGDRTS
IFWNDVKDPV SIEERARWTE TYVRWSPKGT YLATFHQRGI ALWGGDKFKQ IQRFSHQGVQ
LIDFSPCERY LVTFSPLMDT QDDPQAIIIW DILTGHKKRG FHCESSAHWP IFKWSHDGKF
FARMTLDTLS IYETPSMGLL DKKSLKISGI KDFSWSPGGN IIAFWVPEDK DIPARVTLMQ
LPTRQEIRVR NLFNVVDCKL HWQKNGDYLC VKVDRTPKGT QGVVTNFEIF RMREKQVPVD
VVEMKETIIA FAWEPNGSKF AVLHGEAPRI SVSFYHVKSN GKIELIKMFD KQQANTIFWS
PQGQFVVLAG LRSMNGALAF VDTSDCTVMN IAEHYMASDV EWDPTGRYVV TSVSWWSHKV
DNAYWLWTFQ GRLLQKNNKD RFCQLLWRPR PPTLLSQDQI KQIKKDLKKY SKIFEQKDRL
SQSKASKELV ERRRTMMEDF RQYRKMAQEL YMKQKNERLE LRGGVDTDEL DSNVDDWEEE
TIEFFVTEEV IPLGSQE
