EIF3J_DROME
ID EIF3J_DROME Reviewed; 236 AA.
AC Q7K550;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009};
DE Short=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
GN Name=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
GN Synonyms=Adam {ECO:0000255|HAMAP-Rule:MF_03009};
GN ORFNames=CG12131 {ECO:0000312|FlyBase:FBgn0027619};
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=Head;
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 IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PIX, AND ASSOCIATION
RP 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).
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is involved in protein synthesis of a
CC specialized repertoire of mRNAs and, together with other initiation
CC factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S
CC 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_03009}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex. The eIF-3 complex interacts with pix.
CC {ECO:0000255|HAMAP-Rule:MF_03009, ECO:0000269|PubMed:17392269}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit J family. {ECO:0000255|HAMAP-
CC Rule:MF_03009}.
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DR EMBL; AE013599; AAF58867.1; -; Genomic_DNA.
DR EMBL; AY051457; AAK92881.1; -; mRNA.
DR RefSeq; NP_001286260.1; NM_001299331.1.
DR RefSeq; NP_610541.1; NM_136697.3.
DR AlphaFoldDB; Q7K550; -.
DR SMR; Q7K550; -.
DR BioGRID; 61865; 11.
DR IntAct; Q7K550; 3.
DR STRING; 7227.FBpp0087475; -.
DR PaxDb; Q7K550; -.
DR PRIDE; Q7K550; -.
DR DNASU; 36037; -.
DR EnsemblMetazoa; FBtr0088387; FBpp0087475; FBgn0027619.
DR EnsemblMetazoa; FBtr0339425; FBpp0308512; FBgn0027619.
DR GeneID; 36037; -.
DR KEGG; dme:Dmel_CG12131; -.
DR UCSC; CG12131-RA; d. melanogaster.
DR CTD; 8669; -.
DR FlyBase; FBgn0027619; eIF3j.
DR VEuPathDB; VectorBase:FBgn0027619; -.
DR eggNOG; KOG4813; Eukaryota.
DR GeneTree; ENSGT00390000018400; -.
DR HOGENOM; CLU_085806_2_0_1; -.
DR InParanoid; Q7K550; -.
DR OMA; HYGLFLE; -.
DR OrthoDB; 1565510at2759; -.
DR PhylomeDB; Q7K550; -.
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 BioGRID-ORCS; 36037; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Adam; fly.
DR GenomeRNAi; 36037; -.
DR PRO; PR:Q7K550; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0027619; Expressed in embryonic/larval hemocyte (Drosophila) and 62 other tissues.
DR ExpressionAtlas; Q7K550; baseline and differential.
DR Genevisible; Q7K550; DM.
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; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR GO; GO:0006413; P:translational initiation; ISS:FlyBase.
DR Gene3D; 1.10.246.60; -; 1.
DR HAMAP; MF_03009; eIF3j; 1.
DR InterPro; IPR023194; eIF3-like_dom_sf.
DR InterPro; IPR013906; eIF3j.
DR PANTHER; PTHR21681; PTHR21681; 1.
DR Pfam; PF08597; eIF3_subunit; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..236
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J"
FT /id="PRO_0000365135"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 236 AA; 26568 MW; 38DFB4AEFE875C1E CRC64;
MADDWESAAD SEVVIRPTAA ASVNKWEGED EDEDIKDSWE DEEEKKDEEK PTKTEAPAKP
KPNKALKAKL EQQALLEEEA EAKRLANLSP AEKLAEKLRL QKIQEASDLK HAQEAFGVTS
TCGGLDAFNP ETKEEFKEFG ATLSWKVGQF RESEHFPQFV EDLVRSLCVN LSAADIKKVK
MNVEILHSEK LKLEKANAKK PAGKGKGKVT LRTENDDIDG YQKYGNDFTE DYDDFM
