IF4E3_ARATH
ID IF4E3_ARATH Reviewed; 240 AA.
AC Q9C7P6;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Eukaryotic translation initiation factor 4E-3 {ECO:0000303|PubMed:16343979};
DE AltName: Full=eIF-4E-3 {ECO:0000303|PubMed:16343979};
DE AltName: Full=eIF4E-3 {ECO:0000303|PubMed:16343979};
DE AltName: Full=mRNA cap-binding protein {ECO:0000305};
GN Name=EIF4E3 {ECO:0000303|PubMed:16343979};
GN OrderedLocusNames=At1g29550 {ECO:0000312|Araport:AT1G29550};
GN ORFNames=F15D2.13 {ECO:0000312|EMBL:AAG51734.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP REVIEW, AND SUBUNIT.
RX PubMed=16343979; DOI=10.1016/j.tplants.2005.11.004;
RA Robaglia C., Caranta C.;
RT "Translation initiation factors: a weak link in plant RNA virus
RT infection.";
RL Trends Plant Sci. 11:40-45(2006).
CC -!- FUNCTION: Component of the protein complex eIF4F, which is involved in
CC the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal
CC secondary structure and recruitment of mRNA to the ribosome (By
CC similarity). Recognizes and binds the 7-methylguanosine-containing mRNA
CC cap during an early step in the initiation of protein synthesis and
CC facilitates ribosome binding by inducing the unwinding of the mRNAs
CC secondary structures (By similarity). {ECO:0000250|UniProtKB:P48599}.
CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions
CC (PubMed:16343979). It is composed of at least EIF4A, EIF4E and EIF4G
CC (PubMed:16343979). EIF4E is also known to interact with other partners
CC (PubMed:16343979). In higher plants two isoforms of EIF4F have been
CC identified, named isoform EIF4F and isoform EIF(iso)4F
CC (PubMed:16343979). Isoform EIF4F has subunits p220 and p26, whereas
CC isoform EIF(iso)4F has subunits p82 and p28 (PubMed:16343979).
CC {ECO:0000269|PubMed:16343979}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:K0P2S0}. Cytoplasm
CC {ECO:0000250|UniProtKB:K0P2S0}.
CC -!- PTM: According to the redox status, the Cys-138-Cys-176 disulfide
CC bridge may have a role in regulating protein function by affecting its
CC ability to bind capped mRNA. {ECO:0000250|UniProtKB:P29557}.
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC068667; AAG51734.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31102.1; -; Genomic_DNA.
DR PIR; E86418; E86418.
DR RefSeq; NP_174248.1; NM_102695.3.
DR AlphaFoldDB; Q9C7P6; -.
DR SMR; Q9C7P6; -.
DR STRING; 3702.AT1G29550.1; -.
DR PaxDb; Q9C7P6; -.
DR PRIDE; Q9C7P6; -.
DR ProteomicsDB; 250678; -.
DR EnsemblPlants; AT1G29550.1; AT1G29550.1; AT1G29550.
DR GeneID; 839832; -.
DR Gramene; AT1G29550.1; AT1G29550.1; AT1G29550.
DR KEGG; ath:AT1G29550; -.
DR Araport; AT1G29550; -.
DR TAIR; locus:2013748; AT1G29550.
DR eggNOG; KOG1670; Eukaryota.
DR HOGENOM; CLU_043552_2_1_1; -.
DR InParanoid; Q9C7P6; -.
DR OMA; EIYQVEY; -.
DR OrthoDB; 1394271at2759; -.
DR PhylomeDB; Q9C7P6; -.
DR PRO; PR:Q9C7P6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7P6; baseline and differential.
DR Genevisible; Q9C7P6; AT.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IEA:UniProt.
DR Gene3D; 3.30.760.10; -; 1.
DR InterPro; IPR023398; TIF_eIF4e-like.
DR InterPro; IPR001040; TIF_eIF_4E.
DR InterPro; IPR019770; TIF_eIF_4E_CS.
DR PANTHER; PTHR11960; PTHR11960; 1.
DR Pfam; PF01652; IF4E; 1.
DR SUPFAM; SSF55418; SSF55418; 1.
DR PROSITE; PS00813; IF4E; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Initiation factor; Nucleus;
KW Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..240
FT /note="Eukaryotic translation initiation factor 4E-3"
FT /id="PRO_0000193656"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..68
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 75..111
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT REGION 159..168
FT /note="EIF4G-binding"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83..88
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT BINDING 115
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT BINDING 133..134
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT BINDING 183..188
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:P29557"
FT BINDING 228..232
FT /ligand="mRNA"
FT /ligand_id="ChEBI:CHEBI:33699"
FT /ligand_part="N(7)-methylguanosine 5'-triphosphate group"
FT /ligand_part_id="ChEBI:CHEBI:74429"
FT /ligand_part_note="m7GTP residue in mRNA cap"
FT /evidence="ECO:0000250|UniProtKB:Q00LS8"
FT DISULFID 138..176
FT /evidence="ECO:0000250|UniProtKB:P29557"
SQ SEQUENCE 240 AA; 27141 MW; 473358D3D46B9458 CRC64;
MVVTDSPVSG IMADQNIDPN TTTSPSPKEK HVSAIKAISG DEKAPSKEKK NYASKKSTTV
IQKSHCFQNS WTFWFDNPSS KSNQVIWGSS LRSLYTFGTI EEFWSLYNNI HPPTKWVSGA
DLYCFKDKIE PKWEDPICAN GGKWSMMFPK ATLECNWLNT LLALVGEQFD QGDEICGAVL
NFRARGDRIS LWTKNAANEE AQLSIGKQWK ELLGYNETIG FIVHEDAKTL DRDAKRRYTV
