ID EIF3B_BOVIN Reviewed; 786 AA.
AC A7MB16;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
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 {ECO:0000255|HAMAP-Rule:MF_03001};
GN Synonyms=EIF3S9 {ECO:0000255|HAMAP-Rule:MF_03001};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55884}.
CC Note=Localizes to stress granules following cellular stress.
CC {ECO:0000250|UniProtKB:P55884}.
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; BC151284; AAI51285.1; -; mRNA.
DR RefSeq; NP_001095826.1; NM_001102356.1.
DR AlphaFoldDB; A7MB16; -.
DR SMR; A7MB16; -.
DR STRING; 9913.ENSBTAP00000009832; -.
DR PaxDb; 9913-ENSBTAP00000009832; -.
DR PeptideAtlas; A7MB16; -.
DR Ensembl; ENSBTAT00000009832.6; ENSBTAP00000009832.5; ENSBTAG00000007474.6.
DR Ensembl; ENSBTAT00000084055.1; ENSBTAP00000060466.1; ENSBTAG00000007474.6.
DR GeneID; 789999; -.
DR KEGG; bta:789999; -.
DR CTD; 8662; -.
DR VEuPathDB; HostDB:ENSBTAG00000007474; -.
DR VGNC; VGNC:28393; EIF3B.
DR eggNOG; KOG2314; Eukaryota.
DR GeneTree; ENSGT00550000074913; -.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; A7MB16; -.
DR OMA; LWGGPQF; -.
DR OrthoDB; 5479191at2759; -.
DR TreeFam; TF101521; -.
DR Reactome; R-BTA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-BTA-72649; Translation initiation complex formation.
DR Reactome; R-BTA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-BTA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-BTA-72702; Ribosomal scanning and start codon recognition.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000007474; Expressed in choroid plexus and 104 other cell types or tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 EIF3 -RELATED; 1.
DR PANTHER; PTHR14068:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT B; 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; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..786
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000363786"
FT DOMAIN 157..240
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 304..342
FT /note="WD 1"
FT REPEAT 344..389
FT /note="WD 2"
FT REPEAT 393..431
FT /note="WD 3"
FT REPEAT 532..573
FT /note="WD 4"
FT REPEAT 621..666
FT /note="WD 5"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..385
FT /note="Sufficient for interaction with EIF3E"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REGION 142..246
FT /note="Sufficient for interaction with EIF3J"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55884, ECO:0000255|HAMAP-
FT Rule:MF_03001"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
FT MOD_RES 336
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55884"
SQ SEQUENCE 786 AA; 88919 MW; 27B9CA7AF11DF8D1 CRC64;
MQDAENVAAP EAAEQRAEPG PEQAAAEPSP GAEVARPGVQ EAAGGEDAEA GPGPEGPAEP
AADGEGKADA TPGATPPPPE ESSAQLAGEA PAEQAQDAAA EAGSEGAGGD PDGAAEDGGA
DEPSFSDPED FVDDVSEEEL LADVLKDRPQ EADGIDSVIV VDNVPQVGPD RLEKLKNVIH
KIFSKFGKIT NDFYPEEDGR TKGYIFLEYA SPAHALDAVK NADGYKLDKQ HTFRVNLFTD
FDKYMTISDE WDIPEKQPFK DLGNLRYWLE EAECRDQYSV IFESGDRTSI FWNDVKDPVS
IEERARWTET YVRWSPKGTY LATFHQRGIA LWGGEKFKQI QRFSHQGVQL IDFSPCERYL
VTFSPLMDTQ DDPQAIIIWD ILTGQKKRGF HCESSAHWPI FKWSHDGKFF ARMTLDTLSI
YETPSMGLLD KKSLKISGIK DFSWSPGGNI IAFWVPEDKD IPARVTLMQL PTRQEIRVRN
LFNVVDCKLH WQKNGDYLCV KVDRTPKGTQ GVVTNFEIFR MREKQVPVDV VEMKETIIAF
AWEPNGSKFA VLHGEAPRIS VSFYHVKNNG KIELIKMFDK QQANTIFWSP QGQFVVLAGL
RSMNGALAFV DTSDCTVMNI AEHYMASDVE WDPTGRYVVT SVSWWSHKVD NAYWLWTFQG
RLLQKNSKDR FCQLLWRPRP PTLLSQDQIK QIKKDLKKYS KIFEQKDRLS QSKASKELVE
RRRTMMEDFR KYRKMAQELY MEQKNARLEL RGGVDTDELD SNVDDWEEET IEFFVTEEII
PLGNQE
//
