4ET_DROME
ID 4ET_DROME Reviewed; 1010 AA.
AC Q8IH18; L0MLQ9; Q86BR2; Q8IMA1;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Eukaryotic translation initiation factor 4E transporter {ECO:0000303|PubMed:24335285};
DE Short=4E-T {ECO:0000303|PubMed:24335285};
DE Short=Dm4E-T {ECO:0000303|PubMed:24335285};
DE Short=eIF4E transporter {ECO:0000303|PubMed:24335285};
GN Name=4E-T {ECO:0000303|PubMed:24335285, ECO:0000312|FlyBase:FBgn0052016};
GN ORFNames=CG32016 {ECO:0000312|FlyBase:FBgn0052016};
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=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24335285; DOI=10.1093/nar/gkt1265;
RA Kamenska A., Lu W.T., Kubacka D., Broomhead H., Minshall N., Bushell M.,
RA Standart N.;
RT "Human 4E-T represses translation of bound mRNAs and enhances microRNA-
RT mediated silencing.";
RL Nucleic Acids Res. 42:3298-3313(2014).
RN [5]
RP INTERACTION WITH DDX6/ME31B.
RX PubMed=31439631; DOI=10.1101/gad.329219.119;
RA Peter D., Ruscica V., Bawankar P., Weber R., Helms S., Valkov E.,
RA Igreja C., Izaurralde E.;
RT "Molecular basis for GIGYF-Me31B complex assembly in 4EHP-mediated
RT translational repression.";
RL Genes Dev. 33:1355-1360(2019).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 9-44 IN COMPLEX WITH EIF4E1.
RX PubMed=25702871; DOI=10.1016/j.molcel.2015.01.017;
RA Peter D., Igreja C., Weber R., Wohlbold L., Weiler C., Ebertsch L.,
RA Weichenrieder O., Izaurralde E.;
RT "Molecular architecture of 4E-BP translational inhibitors bound to eIF4E.";
RL Mol. Cell 57:1074-1087(2015).
CC -!- FUNCTION: eIF4E1-binding protein that regulates translation and
CC stability of mRNAs in processing bodies (P-bodies) (By similarity).
CC Probably plays a role in P-bodies to coordinate the storage of
CC translationally inactive mRNAs in the cytoplasm and prevent their
CC degradation (By similarity). Acts as a binding platform for multiple
CC RNA-binding proteins. Required for the formation of P-bodies (By
CC similarity). {ECO:0000250|UniProtKB:Q9NRA8}.
CC -!- SUBUNIT: Interacts (via YXXXXLphi motif) with eIF4E1 (PubMed:25702871).
CC Interacts with DDX6/me31B (PubMed:31439631).
CC {ECO:0000269|PubMed:25702871, ECO:0000269|PubMed:31439631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:24335285}.
CC Cytoplasm {ECO:0000269|PubMed:24335285}. Nucleus
CC {ECO:0000269|PubMed:24335285}. Note=Mainly localizes to processing
CC bodies (P-bodies) (PubMed:24335285). Present at low level in other
CC parts of the cytoplasm and in the nucleus (PubMed:24335285).
CC {ECO:0000269|PubMed:24335285}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q8IH18-1; Sequence=Displayed;
CC Name=H;
CC IsoId=Q8IH18-2; Sequence=VSP_060743;
CC -!- TISSUE SPECIFICITY: Expressed in all larval and adult organs and
CC tissues, with highest levels in the ovary.
CC {ECO:0000269|PubMed:24335285}.
CC -!- DOMAIN: The YXXXXLphi motif mediates interaction with eIF4E1.
CC {ECO:0000250|UniProtKB:Q9NRA8}.
CC -!- SIMILARITY: Belongs to the 4E-T/EIF4E-T family. {ECO:0000305}.
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DR EMBL; AE014135; AAF59398.4; -; Genomic_DNA.
DR EMBL; AE014135; AAF59399.3; -; Genomic_DNA.
DR EMBL; AE014135; AAF59400.3; -; Genomic_DNA.
DR EMBL; AE014135; AGB96568.1; -; Genomic_DNA.
DR EMBL; BT001473; AAN71228.1; -; mRNA.
DR RefSeq; NP_001259078.1; NM_001272149.2. [Q8IH18-2]
DR RefSeq; NP_726618.3; NM_166796.2. [Q8IH18-1]
DR RefSeq; NP_726619.2; NM_166797.2. [Q8IH18-1]
DR RefSeq; NP_726620.2; NM_166798.2. [Q8IH18-1]
DR PDB; 4UE9; X-ray; 2.15 A; B=9-44.
DR PDBsum; 4UE9; -.
DR AlphaFoldDB; Q8IH18; -.
DR SMR; Q8IH18; -.
DR IntAct; Q8IH18; 2.
DR STRING; 7227.FBpp0302771; -.
DR PaxDb; Q8IH18; -.
DR DNASU; 43836; -.
DR EnsemblMetazoa; FBtr0089229; FBpp0088293; FBgn0052016. [Q8IH18-1]
DR EnsemblMetazoa; FBtr0089233; FBpp0088297; FBgn0052016. [Q8IH18-1]
DR EnsemblMetazoa; FBtr0310651; FBpp0302771; FBgn0052016. [Q8IH18-1]
DR EnsemblMetazoa; FBtr0334626; FBpp0306688; FBgn0052016. [Q8IH18-2]
DR GeneID; 43836; -.
DR KEGG; dme:Dmel_CG32016; -.
DR UCSC; CG32016-RA; d. melanogaster.
DR UCSC; CG32016-RB; d. melanogaster. [Q8IH18-1]
DR CTD; 43836; -.
DR FlyBase; FBgn0052016; 4E-T.
DR VEuPathDB; VectorBase:FBgn0052016; -.
DR eggNOG; ENOG502QRQE; Eukaryota.
DR GeneTree; ENSGT00390000012071; -.
DR HOGENOM; CLU_011837_0_0_1; -.
DR InParanoid; Q8IH18; -.
DR OMA; SRGVWDP; -.
DR OrthoDB; 209389at2759; -.
DR PhylomeDB; Q8IH18; -.
DR SignaLink; Q8IH18; -.
DR BioGRID-ORCS; 43836; 0 hits in 1 CRISPR screen.
DR ChiTaRS; 4E-T; fly.
DR GenomeRNAi; 43836; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0052016; Expressed in adult abdomen and 25 other tissues.
DR ExpressionAtlas; Q8IH18; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000932; C:P-body; IDA:FlyBase.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1905536; P:negative regulation of eukaryotic translation initiation factor 4F complex assembly; IDA:FlyBase.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR InterPro; IPR018862; eIF4E-T.
DR PANTHER; PTHR12269; PTHR12269; 2.
DR Pfam; PF10477; EIF4E-T; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..1010
FT /note="Eukaryotic translation initiation factor 4E
FT transporter"
FT /id="PRO_0000450888"
FT REGION 154..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 10..16
FT /note="YXXXXLphi motif"
FT /evidence="ECO:0000250|UniProtKB:Q9NRA8"
FT COMPBIAS 196..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 695..725
FT /note="Missing (in isoform H)"
FT /id="VSP_060743"
FT HELIX 12..17
FT /evidence="ECO:0007829|PDB:4UE9"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:4UE9"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:4UE9"
SQ SEQUENCE 1010 AA; 113890 MW; D3DC8E352F14A006 CRC64;
MDTSKISARY SKVDLLALRY EGKSRQRPQC STRLELQTLG FWKINLNTAA LTVSSAYSNQ
NKNRLSPEAD NSSLICSNSS SISSRRAMRN RERANNYYQR FVPTDSLLIS GEDKDKDALS
HGQPYKLNII DHRSISSSHL MPAFAKRRFV ISKGSNSEES NEGINTCASK GKAASSPSRK
GSELDTAETC LNFVQPDHDQ CMSSSPTFST SRQERRIGSG RLLPRSDNWD YKNEKTVEAS
IENEKETSPN GSGSTSSLNQ HNQSQHRSRT FSGRLVERVP EVTDRRFQYD SKKSFDRQGI
NNRRISGKEP FSTQSRSKRG NSYLIHEEPE WFSAGPKSQL ETIDLHGFED LEKNEERSVT
EDKNNQIQQL DKNLDAQASK DEASMRNSND SLNFREVIPS DEKKHTDENV VTSIQNSTDL
GHPNKNKPIQ MQPSQNPESE FNFDAFLNMH PLDNSVLSND ETGKSDSKGT SRFSRWFRQK
EAANNNEFPG FRESHAQEKR GIPSVKDLEA QMIKVDMRTD LINPIAGSLC QTVQMEKPIA
RDTEAFKKLL QQLGSQARQH HPCNDDCRTI NLSNIANHVH LESKLHQKIN DGHLQQPELS
VNVPTMPTSS HVFLQKRLEI QHLIQRLHCG DVSHDFLEKE LDNPSTPAAT KDVIATVLNE
YSHSKRNPVV TGDPNIFTQQ SFLQPQSVHQ HYSQELHSQN TANHTINQLI SHGNSPTPLA
FTPTSVLRKM TADKDTQSPS TYCQNPQYHV HQQNAKQVGT RENVLEPQLT ATMAVQPRMI
LGGGNFAIGQ NNQHLSPNMS QSRNQQVLKW TSGNMQMVHG KTFGRPILKG GLNSMPHSNS
ALPFTAHKIE MQPIHQPHLQ QQQHRFKAVQ SVESNLNTES VHQNITSPVG WHQLYMQHQQ
QHHHTRQQLS QRVIYGEMHR QSNPQMSPPV PGFSDSSDSG NVIKANSLTS PSYQRDERIS
SPTNQLAQWF SPELLAKASA GKLPLLNVNQ ALSLEEFERS IQHSSGVVHN
