EIF3B_CAEEL
ID EIF3B_CAEEL Reviewed; 725 AA.
AC Q9XWI6; Q7K785;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 2.
DT 03-AUG-2022, entry version 149.
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};
GN Name=eif-3.B {ECO:0000255|HAMAP-Rule:MF_03001,
GN ECO:0000312|WormBase:Y54E2A.11a};
GN ORFNames=Y54E2A.11 {ECO:0000312|WormBase:Y54E2A.11a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=17411345; DOI=10.1371/journal.pgen.0030056;
RA Curran S.P., Ruvkun G.;
RT "Lifespan regulation by evolutionarily conserved genes essential for
RT viability.";
RL PLoS Genet. 3:E56-E56(2007).
CC -!- FUNCTION: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is involved in protein
CC synthesis of a specialized repertoire of mRNAs and, together with other
CC initiation factors, stimulates binding of mRNA and methionyl-tRNAi to
CC the 40S 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_03001}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03001}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y54E2A.11a};
CC IsoId=Q9XWI6-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y54E2A.11b};
CC IsoId=Q9XWI6-2; Sequence=VSP_047618, VSP_047619;
CC -!- DISRUPTION PHENOTYPE: Extended lifespan in adults.
CC {ECO:0000269|PubMed:17411345}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit B family. {ECO:0000255|HAMAP-
CC Rule:MF_03001}.
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DR EMBL; BX284602; CAA21681.2; -; Genomic_DNA.
DR EMBL; BX284602; CAE46682.2; -; Genomic_DNA.
DR PIR; T27148; T27148.
DR RefSeq; NP_001022469.2; NM_001027298.5. [Q9XWI6-1]
DR RefSeq; NP_001022470.2; NM_001027299.5.
DR AlphaFoldDB; Q9XWI6; -.
DR SMR; Q9XWI6; -.
DR BioGRID; 40419; 28.
DR DIP; DIP-26989N; -.
DR IntAct; Q9XWI6; 2.
DR STRING; 6239.Y54E2A.11a.1; -.
DR EPD; Q9XWI6; -.
DR PaxDb; Q9XWI6; -.
DR PeptideAtlas; Q9XWI6; -.
DR PRIDE; Q9XWI6; -.
DR EnsemblMetazoa; Y54E2A.11.1; Y54E2A.11.1; WBGene00001225. [Q9XWI6-1]
DR EnsemblMetazoa; Y54E2A.11.2; Y54E2A.11.2; WBGene00001225. [Q9XWI6-1]
DR GeneID; 175138; -.
DR KEGG; cel:CELE_Y54E2A.11; -.
DR UCSC; Y54E2A.11a.2; c. elegans.
DR CTD; 175138; -.
DR WormBase; Y54E2A.11a; CE47851; WBGene00001225; eif-3.B. [Q9XWI6-1]
DR WormBase; Y54E2A.11b; CE47908; WBGene00001225; eif-3.B. [Q9XWI6-2]
DR eggNOG; KOG2314; Eukaryota.
DR GeneTree; ENSGT00550000074913; -.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; Q9XWI6; -.
DR OMA; NVADCKI; -.
DR OrthoDB; 1194797at2759; -.
DR PhylomeDB; Q9XWI6; -.
DR Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CEL-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-CEL-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-CEL-72702; Ribosomal scanning and start codon recognition.
DR PRO; PR:Q9XWI6; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001225; Expressed in larva and 4 other tissues.
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:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
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:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.120.10.30; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03001; eIF3b; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR011400; EIF3B.
DR InterPro; IPR034363; eIF3B_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
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 PIRSF; PIRSF036424; eIF3b; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..725
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000363789"
FT DOMAIN 46..130
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 202..240
FT /note="WD 1"
FT REPEAT 242..280
FT /note="WD 2"
FT REPEAT 354..395
FT /note="WD 3"
FT REPEAT 462..504
FT /note="WD 4"
FT REPEAT 510..552
FT /note="WD 5"
FT REPEAT 554..594
FT /note="WD 6"
FT VAR_SEQ 149..193
FT /note="YNDVGDLWWWLQNERCRDQFAISHDKLGVPTVGVFTNMKGNDPEL -> KTT
FT LVPTVSLIPTFNTLISRRVRPTLLPTPLRKSRTAGETVRRIV (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_047618"
FT VAR_SEQ 194..725
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_047619"
SQ SEQUENCE 725 AA; 83065 MW; C73A8E862A32F887 CRC64;
MVEIDFNKEN EEDFSDPPGF VDDVTDDVLV PDVLHKKPTI DEFEDNCVFI AGIPVVGADR
LGKLQSVLKK VLERLDPAVK LYIPPSPEGG CLGVLLTEWA DQRSAQFAVK SLNGYAFDKN
HTFTARSFKD MKQLEAPSDH WTTPEKQAYN DVGDLWWWLQ NERCRDQFAI SHDKLGVPTV
GVFTNMKGND PELAGDADKA ERANWTETVF TWSPHGSYLS TIHKQGIILW GGKDYARAHR
FAHTNVQYID FSPCETYLVT YAAPEESNSW GDCEKDSLRI WDVRTGELKK AFSTFELTGR
TQLPTWPFFR WSFDEKYFAC LKAPEKDKLE REQKINGISI FESEKFELYE GRPVNIENIK
QFEWSPTSTV LAYYSECTDA VPAEFGLLQV PSMQRLRSAR VHNVADAQMF WQKSGKRLAF
YTMRFKKKEY RETGEVKYVG GCQYHVDIFE IDKKDVSLMN LPLSEPFIHF DWDPEGDKFC
VLVGNTAKAT PQVYKIEANS HAPKLVSKLD AGVHFNEVQF APKGGWLAVL AKVSAGGNVY
FIDTSLSEAK RTNVIEHPLF NKGYWDPTGR YFVTCSTLGG RAGADLGYRI FTFQGRELCR
KNLDRLAQFK WRPRPPVKLS EQKQREIKKN LKKTAAKFIK QDDDEKCRAS QEVVEKRRKI
MAAFDIIRSR NREQLDATRD ERISLRNGVD TEAQLDEDEF VDEEITIALS TSKTQAPLTE
EEMRD
