EIF3B_DROME
ID EIF3B_DROME Reviewed; 690 AA.
AC Q0E940; C0PUW0; Q8MR84;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=eIF3b {ECO:0000255|HAMAP-Rule:MF_03001};
GN Synonyms=eIF3-S9 {ECO:0000255|HAMAP-Rule:MF_03001};
GN ORFNames=CG4878 {ECO:0000312|FlyBase:FBgn0034237};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH PIX, AND ASSOCIATION WITH THE 40S RIBOSOME.
RX PubMed=17392269; DOI=10.1074/jbc.m701361200;
RA Andersen D.S., Leevers S.J.;
RT "The essential Drosophila ATP-binding cassette domain protein, pixie, binds
RT the 40 S ribosome in an ATP-dependent manner and is required for
RT translation initiation.";
RL J. Biol. Chem. 282:14752-14760(2007).
RN [6]
RP INTERACTION WITH MXT.
RX PubMed=23716590; DOI=10.1128/mcb.01354-12;
RA Hernandez G., Miron M., Han H., Liu N., Magescas J., Tettweiler G.,
RA Frank F., Siddiqui N., Sonenberg N., Lasko P.;
RT "Mextli is a novel eukaryotic translation initiation factor 4E-binding
RT protein that promotes translation in Drosophila melanogaster.";
RL Mol. Cell. Biol. 33:2854-2864(2013).
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. The eIF-3 complex interacts with pix
CC (PubMed:17392269). Interacts with mxt (PubMed:23716590).
CC {ECO:0000255|HAMAP-Rule:MF_03001, ECO:0000269|PubMed:17392269,
CC ECO:0000269|PubMed:23716590}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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; AE013599; AAF57842.1; -; Genomic_DNA.
DR EMBL; AY122066; AAM52578.1; -; mRNA.
DR EMBL; BT072816; ACN62419.1; -; mRNA.
DR RefSeq; NP_611228.1; NM_137384.3.
DR RefSeq; NP_725691.1; NM_166239.4.
DR AlphaFoldDB; Q0E940; -.
DR SMR; Q0E940; -.
DR BioGRID; 62670; 33.
DR IntAct; Q0E940; 9.
DR STRING; 7227.FBpp0086098; -.
DR PaxDb; Q0E940; -.
DR PRIDE; Q0E940; -.
DR DNASU; 36981; -.
DR EnsemblMetazoa; FBtr0086941; FBpp0086097; FBgn0034237.
DR EnsemblMetazoa; FBtr0086942; FBpp0086098; FBgn0034237.
DR GeneID; 36981; -.
DR KEGG; dme:Dmel_CG4878; -.
DR UCSC; CG4878-RA; d. melanogaster.
DR UCSC; CG4878-RB; d. melanogaster.
DR CTD; 8662; -.
DR FlyBase; FBgn0034237; eIF3b.
DR VEuPathDB; VectorBase:FBgn0034237; -.
DR eggNOG; KOG2314; Eukaryota.
DR GeneTree; ENSGT00550000074913; -.
DR HOGENOM; CLU_011152_1_0_1; -.
DR InParanoid; Q0E940; -.
DR OMA; NVADCKI; -.
DR OrthoDB; 1194797at2759; -.
DR PhylomeDB; Q0E940; -.
DR Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DME-72649; Translation initiation complex formation.
DR Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
DR SignaLink; Q0E940; -.
DR BioGRID-ORCS; 36981; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 36981; -.
DR PRO; PR:Q0E940; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034237; Expressed in wing disc and 40 other tissues.
DR ExpressionAtlas; Q0E940; baseline and differential.
DR Genevisible; Q0E940; DM.
DR GO; GO:0005829; C:cytosol; ISS:FlyBase.
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:0003729; F:mRNA binding; ISS:FlyBase.
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:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
DR CDD; cd12278; RRM_eIF3B; 1.
DR Gene3D; 2.130.10.10; -; 1.
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 Coiled coil; Cytoplasm; Initiation factor; Protein biosynthesis;
KW Reference proteome; Repeat; RNA-binding; WD repeat.
FT CHAIN 1..690
FT /note="Eukaryotic translation initiation factor 3 subunit
FT B"
FT /id="PRO_0000363797"
FT DOMAIN 57..141
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT REPEAT 207..246
FT /note="WD 1"
FT REPEAT 293..331
FT /note="WD 2"
FT REPEAT 334..369
FT /note="WD 3"
FT REPEAT 442..484
FT /note="WD 4"
FT REPEAT 530..575
FT /note="WD 5"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 595..645
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03001"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 12
FT /note="T -> A (in Ref. 3; AAM52578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 690 AA; 80441 MW; D7536C21C931D778 CRC64;
MAKKKSEEHS GTDANDSDYQ EEPNFDDPPG FVDNISDEDL LGDMLAQRPS EADGVESVVV
VDNIPKVEPV RLEKLKLVIN KLFSNYGEIV NVVYPVDEEG KTKGYAFMEY KQARQAEEAV
KKLNNHRLDK NHTFAVNLFT DFQKYENIPE KWEPPTVQTF KVQSDLYNFI NDPDTYDQYC
VAAETAPNCV QVGFWQNVLP EPFELETRER FTDTFVKWSP LGTYVVTFHK PGVAIWGGSS
FQKIQKFPHP GTQFVEFSPC ENYLVTYGPT PTGQKIIIWD IRTGAEKRSF VADGMSVLSM
FRWSHDDKFV ARMGENSIHI YETPSFYLLD LKSIKIPGIR GFSWSPTDNV IAYWVEEQNQ
IPARVTLMEI PKKREIRNKN LFHVADCKLH WQKSGDYLCV KVDRYSKLKK DKKDLDVKFL
GMFYNFEIFH MREKEIPVDS VEIRELILAF AWEPVGNKFS IIHGETNSSN VSFYEVNKGV
KPSLVKRLEK KSCTHLFWSP RGQFIVMANL TMGTFEFVDS TNDYIITASP DHFRASEVEW
DPTGRYVVTG VSSWKVKEDT GFNMYTFQGR IIKRTILKNF VQFLWRPRPP TLLSEEKQKE
IKKNLKKYYA AFEQKDRLRL TRASKELLEK RSQLRETFME YRNKRIAEWA EQKSRRIMLR
GHVDTDNLET DEVDEEIVEF LVKEEVTLLE
