IF4E5_ARATH
ID IF4E5_ARATH Reviewed; 221 AA.
AC Q9FK59; O64928;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Eukaryotic translation initiation factor NCBP;
DE AltName: Full=Novel cap-binding protein;
DE Short=nCBP;
DE AltName: Full=mRNA cap-binding protein;
GN Name=NCBP; OrderedLocusNames=At5g18110; ORFNames=MRG7.7;
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 [MRNA], AND FUNCTION.
RX PubMed=9553087; DOI=10.1074/jbc.273.17.10325;
RA Ruud K.A., Kuhlow C., Goss D.J., Browning K.S.;
RT "Identification and characterization of a novel cap-binding protein from
RT Arabidopsis thaliana.";
RL J. Biol. Chem. 273:10325-10330(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: 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. {ECO:0000269|PubMed:9553087}.
CC -!- SUBUNIT: EIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E and EIF4G. EIF4E is also known to
CC interact with other partners. In higher plants two isoforms of EIF4F
CC have been identified, named isoform EIF4F and isoform EIF(iso)4F.
CC Isoform EIF4F has subunits p220 and p26, whereas isoform EIF(iso)4F has
CC subunits p82 and p28.
CC -!- INTERACTION:
CC Q9FK59; Q17TI5: BRX; NbExp=3; IntAct=EBI-1770573, EBI-4426649;
CC Q9FK59; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-1770573, EBI-4426557;
CC -!- SIMILARITY: Belongs to the eukaryotic initiation factor 4E family.
CC {ECO:0000305}.
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DR EMBL; AF028809; AAC17220.1; -; mRNA.
DR EMBL; AB012246; BAB09469.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92508.1; -; Genomic_DNA.
DR EMBL; AY092964; AAM12963.1; -; mRNA.
DR EMBL; AY093208; AAM13207.1; -; mRNA.
DR EMBL; AY114562; AAM47881.1; -; mRNA.
DR PIR; T52138; T52138.
DR RefSeq; NP_197312.1; NM_121816.2.
DR AlphaFoldDB; Q9FK59; -.
DR SMR; Q9FK59; -.
DR BioGRID; 17205; 4.
DR IntAct; Q9FK59; 5.
DR STRING; 3702.AT5G18110.1; -.
DR iPTMnet; Q9FK59; -.
DR PaxDb; Q9FK59; -.
DR PRIDE; Q9FK59; -.
DR ProteomicsDB; 250675; -.
DR EnsemblPlants; AT5G18110.1; AT5G18110.1; AT5G18110.
DR GeneID; 831929; -.
DR Gramene; AT5G18110.1; AT5G18110.1; AT5G18110.
DR KEGG; ath:AT5G18110; -.
DR Araport; AT5G18110; -.
DR TAIR; locus:2172339; AT5G18110.
DR eggNOG; KOG1669; Eukaryota.
DR HOGENOM; CLU_043552_3_1_1; -.
DR InParanoid; Q9FK59; -.
DR OMA; ANCHGGK; -.
DR OrthoDB; 1394271at2759; -.
DR PhylomeDB; Q9FK59; -.
DR PRO; PR:Q9FK59; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK59; baseline and differential.
DR Genevisible; Q9FK59; AT.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; IBA:GO_Central.
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 Initiation factor; Protein biosynthesis; Reference proteome; RNA-binding;
KW Translation regulation.
FT CHAIN 1..221
FT /note="Eukaryotic translation initiation factor NCBP"
FT /id="PRO_0000193666"
FT CONFLICT 42
FT /note="D -> L (in Ref. 1; AAC17220)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 25745 MW; FE484870E9769C6F CRC64;
MEVLDRRDDE IRDSGNMDSI KSHYVTDSVS EERRSRELKD GDHPLRYKFS IWYTRRTPGV
RNQSYEDNIK KMVEFSTVEG FWACYCHLAR SSLLPSPTDL HFFKDGIRPL WEDGANCNGG
KWIIRFSKVV SARFWEDLLL ALVGDQLDDA DNICGAVLSV RFNEDIISVW NRNASDHQAV
MGLRDSIKRH LKLPHAYVME YKPHDASLRD NSSYRNTWLR G